An aldose-ketose isomerase that catalyzes the reversible interconversion of glucose 6-phosphate and fructose 6-phosphate. In prokaryotic and eukaryotic organisms it plays an essential role in glycolytic and gluconeogenic pathways. In mammalian systems the enzyme is found in the cytoplasm and as a secreted protein. This secreted form of glucose-6-phosphate isomerase has been referred to as autocrine motility factor or neuroleukin, and acts as a cytokine which binds to the AUTOCRINE MOTILITY FACTOR RECEPTOR. Deficiency of the enzyme in humans is an autosomal recessive trait, which results in CONGENITAL NONSPHEROCYTIC HEMOLYTIC ANEMIA.
An enzyme that catalyzes the reversible isomerization of D-mannose-6-phosphate to form D-fructose-6-phosphate, an important step in glycolysis. EC 5.3.1.8.
An enzyme that catalyzes reversibly the conversion of D-glyceraldehyde 3-phosphate to dihydroxyacetone phosphate. A deficiency in humans causes nonspherocytic hemolytic disease (ANEMIA, HEMOLYTIC, CONGENITAL NONSPHEROCYTIC). EC 5.3.1.1.
Enzymes that catalyze the interconversion of aldose and ketose compounds.
A hexose or fermentable monosaccharide and isomer of glucose from manna, the ash Fraxinus ornus and related plants. (From Grant & Hackh's Chemical Dictionary, 5th ed & Random House Unabridged Dictionary, 2d ed)
Trioses are monosaccharides, specifically simple sugars, that contain three carbon atoms, and can be glyceraldehydes or dihydroxyacetones, which are important intermediates in metabolic pathways such as glycolysis.
Enzymes that catalyze the epimerization of chiral centers within carbohydrates or their derivatives. EC 5.1.3.
Inorganic salts of phosphoric acid.
A class of enzymes that catalyze geometric or structural changes within a molecule to form a single product. The reactions do not involve a net change in the concentrations of compounds other than the substrate and the product.(from Dorland, 28th ed) EC 5.
A class of carbohydrates that contains five carbon atoms.
Ribulose substituted by one or more phosphoric acid moieties.
Hexosephosphates are sugar phosphate molecules, specifically those derived from hexoses (six-carbon sugars), such as glucose-6-phosphate and fructose-6-phosphate, which play crucial roles in various metabolic pathways including glycolysis, gluconeogenesis, and the pentose phosphate pathway.
Any one of a group of congenital hemolytic anemias in which there is no abnormal hemoglobin or spherocytosis and in which there is a defect of glycolysis in the erythrocyte. Common causes include deficiencies in GLUCOSE-6-PHOSPHATE ISOMERASE; PYRUVATE KINASE; and GLUCOSE-6-PHOSPHATE DEHYDROGENASE.
An enzyme that catalyzes the isomerization of proline residues within proteins. EC 5.2.1.8.
An oxidative decarboxylation process that converts GLUCOSE-6-PHOSPHATE to D-ribose-5-phosphate via 6-phosphogluconate. The pentose product is used in the biosynthesis of NUCLEIC ACIDS. The generated energy is stored in the form of NADPH. This pathway is prominent in tissues which are active in the synthesis of FATTY ACIDS and STEROIDS.
An important intermediate in lipid biosynthesis and in glycolysis.
Enzymes that catalyze the dehydrogenation of GLYCERALDEHYDE 3-PHOSPHATE. Several types of glyceraldehyde-3-phosphate-dehydrogenase exist including phosphorylating and non-phosphorylating varieties and ones that transfer hydrogen to NADP and ones that transfer hydrogen to NAD.
An enzyme of the lyase class that catalyzes the cleavage of fructose 1,6-biphosphate to form dihydroxyacetone phosphate and glyceraldehyde 3-phosphate. The enzyme also acts on (3S,4R)-ketose 1-phosphates. The yeast and bacterial enzymes are zinc proteins. (Enzyme Nomenclature, 1992) E.C. 4.1.2.13.
A pentose active in biological systems usually in its D-form.
Any salt or ester of glycerophosphoric acid.
Sulfur-sulfur bond isomerases that catalyze the rearrangement of disulfide bonds within proteins during folding. Specific protein disulfide-isomerase isoenzymes also occur as subunits of PROCOLLAGEN-PROLINE DIOXYGENASE.
A colorless liquid used as a solvent and an antiseptic. It is one of the ketone bodies produced during ketoacidosis.
Ribose substituted in the 1-, 3-, or 5-position by a phosphoric acid moiety.
An enzyme of the transferase class that catalyzes the reaction sedoheptulose 7-phosphate and D-glyceraldehyde 3-phosphate to yield D-erythrose 4-phosphate and D-fructose phosphate in the PENTOSE PHOSPHATE PATHWAY. (Dorland, 27th ed) EC 2.2.1.2.
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
Phosphoric acid esters of mannose.
Enzymes that catalyze the transposition of double bond(s) in a steroid molecule. EC 5.3.3.
Pentosephosphates are monosaccharides, specifically pentoses, that have a phosphate group attached, playing crucial roles in carbohydrate metabolism, such as being intermediates in the pentose phosphate pathway and serving as precursors for nucleotide synthesis.
A receptor that is specific for IGF-II and mannose-6-phosphate. The receptor is a 250-kDa single chain polypeptide which is unrelated in structure to the type 1 IGF receptor (RECEPTOR, IGF TYPE 1) and does not have a tyrosine kinase domain.
A carbon-carbon double bond isomerase that catalyzes the movement double bond from C3 to C2 of an unsaturated acyl-CoA. The enzyme plays a key role in allowing acyl-CoA substrates to re-enter the beta-oxidation pathway.
Enzymes that catalyze the shifting of a carbon-carbon double bond from one position to another within the same molecule. EC 5.3.3.
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
An allosteric enzyme that regulates glycolysis by catalyzing the transfer of a phosphate group from ATP to fructose-6-phosphate to yield fructose-1,6-bisphosphate. D-tagatose- 6-phosphate and sedoheptulose-7-phosphate also are acceptors. UTP, CTP, and ITP also are donors. In human phosphofructokinase-1, three types of subunits have been identified. They are PHOSPHOFRUCTOKINASE-1, MUSCLE TYPE; PHOSPHOFRUCTOKINASE-1, LIVER TYPE; and PHOSPHOFRUCTOKINASE-1, TYPE C; found in platelets, brain, and other tissues.
A genus of gram-positive, endospore-forming, thermophilic bacteria in the family BACILLACEAE.
Glucose-6-Phosphate Dehydrogenase (G6PD) is an enzyme that plays a critical role in the pentose phosphate pathway, catalyzing the oxidation of glucose-6-phosphate to 6-phosphoglucono-δ-lactone while reducing nicotinamide adenine dinucleotide phosphate (NADP+) to nicotinamide adenine dinucleotide phosphate hydrogen (NADPH), thereby protecting cells from oxidative damage and maintaining redox balance.
A subclass of lectins that are specific for CARBOHYDRATES that contain MANNOSE.
The rate dynamics in chemical or physical systems.
Enzymes that catalyze a reverse aldol condensation. A molecule containing a hydroxyl group and a carbonyl group is cleaved at a C-C bond to produce two smaller molecules (ALDEHYDES or KETONES). EC 4.1.2.
A metabolic process that converts GLUCOSE into two molecules of PYRUVIC ACID through a series of enzymatic reactions. Energy generated by this process is conserved in two molecules of ATP. Glycolysis is the universal catabolic pathway for glucose, free glucose, or glucose derived from complex CARBOHYDRATES, such as GLYCOGEN and STARCH.
A nucleoside diphosphate sugar which can be converted to the deoxy sugar GDPfucose, which provides fucose for lipopolysaccharides of bacterial cell walls. Also acts as mannose donor for glycolipid synthesis.
An ester of glucose with phosphoric acid, made in the course of glucose metabolism by mammalian and other cells. It is a normal constituent of resting muscle and probably is in constant equilibrium with fructose-6-phosphate. (Stedman, 26th ed)
Calcium salts of phosphoric acid. These compounds are frequently used as calcium supplements.
Derivatives of ACETIC ACID which contain an hydroxy group attached to the methyl carbon.
'Sugar phosphates' are organic compounds that consist of a sugar molecule linked to one or more phosphate groups, playing crucial roles in biochemical processes such as energy transfer and nucleic acid metabolism.
Fructosephosphates are organic compounds resulting from the combination of fructose with a phosphate group, playing crucial roles in various metabolic processes, particularly within carbohydrate metabolism.
Electrophoresis in which a starch gel (a mixture of amylose and amylopectin) is used as the diffusion medium.
A lipophilic glycosyl carrier of the monosaccharide mannose in the biosynthesis of oligosaccharide phospholipids and glycoproteins.
A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.
The study of crystal structure using X-RAY DIFFRACTION techniques. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
An enzyme that catalyzes the conversion of ATP and a D-hexose to ADP and a D-hexose 6-phosphate. D-Glucose, D-mannose, D-fructose, sorbitol, and D-glucosamine can act as acceptors; ITP and dATP can act as donors. The liver isoenzyme has sometimes been called glucokinase. (From Enzyme Nomenclature, 1992) EC 2.7.1.1.
Organic compounds that contain phosphorus as an integral part of the molecule. Included under this heading is broad array of synthetic compounds that are used as PESTICIDES and DRUGS.
The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.
An analytical technique for resolution of a chemical mixture into its component compounds. Compounds are separated on an adsorbent paper (stationary phase) by their varied degree of solubility/mobility in the eluting solvent (mobile phase).
The normality of a solution with respect to HYDROGEN ions; H+. It is related to acidity measurements in most cases by pH = log 1/2[1/(H+)], where (H+) is the hydrogen ion concentration in gram equivalents per liter of solution. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)
The rotation of linearly polarized light as it passes through various media.
An aldotriose which is an important intermediate in glycolysis and in tryptophan biosynthesis.
The parts of a macromolecule that directly participate in its specific combination with another molecule.
A species of parasitic EUKARYOTES that attaches itself to the intestinal mucosa and feeds on mucous secretions. The organism is roughly pear-shaped and motility is somewhat erratic, with a slow oscillation about the long axis.
A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.
Electrophoresis in which cellulose acetate is the diffusion medium.
Inorganic derivatives of phosphoric acid (H3PO4). Note that organic derivatives of phosphoric acids are listed under ORGANOPHOSPHATES.
Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.
A condition of inadequate circulating red blood cells (ANEMIA) or insufficient HEMOGLOBIN due to premature destruction of red blood cells (ERYTHROCYTES).
Structurally related forms of an enzyme. Each isoenzyme has the same mechanism and classification, but differs in its chemical, physical, or immunological characteristics.
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
Phosphoric acid esters of inositol. They include mono- and polyphosphoric acid esters, with the exception of inositol hexaphosphate which is PHYTIC ACID.
Proteins prepared by recombinant DNA technology.
An enzyme that catalyzes the reduction of a 3 beta-hydroxy-delta(5)-steroid to 3-oxo-delta(4)-steroid in the presence of NAD. It converts pregnenolone to progesterone and dehydroepiandrosterone to androstenedione. EC 1.1.1.145.
A primary source of energy for living organisms. It is naturally occurring and is found in fruits and other parts of plants in its free state. It is used therapeutically in fluid and nutrient replacement.
Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.
The extent to which an enzyme retains its structural conformation or its activity when subjected to storage, isolation, and purification or various other physical or chemical manipulations, including proteolytic enzymes and heat.
The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.
A thermostable extracellular metalloendopeptidase containing four calcium ions. (Enzyme Nomenclature, 1992) 3.4.24.27.
An individual that contains cell populations derived from different zygotes.
Carbohydrates consisting of between two (DISACCHARIDES) and ten MONOSACCHARIDES connected by either an alpha- or beta-glycosidic link. They are found throughout nature in both the free and bound form.
The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).
The species Oryctolagus cuniculus, in the family Leporidae, order LAGOMORPHA. Rabbits are born in burrows, furless, and with eyes and ears closed. In contrast with HARES, rabbits have 22 chromosome pairs.
Common name for the species Gallus gallus, the domestic fowl, in the family Phasianidae, order GALLIFORMES. It is descended from the red jungle fowl of SOUTHEAST ASIA.
The region of an enzyme that interacts with its substrate to cause the enzymatic reaction.
A hydro-lyase that catalyzes the dehydration of 2-phosphoglycerate to form PHOSPHOENOLPYRUVATE. Several different isoforms of this enzyme exist, each with its own tissue specificity.
Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.
ATP:pyruvate 2-O-phosphotransferase. A phosphotransferase that catalyzes reversibly the phosphorylation of pyruvate to phosphoenolpyruvate in the presence of ATP. It has four isozymes (L, R, M1, and M2). Deficiency of the enzyme results in hemolytic anemia. EC 2.7.1.40.
The characteristic 3-dimensional shape and arrangement of multimeric proteins (aggregates of more than one polypeptide chain).
The arrangement of two or more amino acid or base sequences from an organism or organisms in such a way as to align areas of the sequences sharing common properties. The degree of relatedness or homology between the sequences is predicted computationally or statistically based on weights assigned to the elements aligned between the sequences. This in turn can serve as a potential indicator of the genetic relatedness between the organisms.
A trihydroxy sugar alcohol that is an intermediate in carbohydrate and lipid metabolism. It is used as a solvent, emollient, pharmaceutical agent, and sweetening agent.
Enzymes that catalyze the transfer of mannose from a nucleoside diphosphate mannose to an acceptor molecule which is frequently another carbohydrate. The group includes EC 2.4.1.32, EC 2.4.1.48, EC 2.4.1.54, and EC 2.4.1.57.
Theoretical representations that simulate the behavior or activity of chemical processes or phenomena; includes the use of mathematical equations, computers, and other electronic equipment.
Proteins found in any species of bacterium.
Compounds functioning as activated glycosyl carriers in the biosynthesis of glycoproteins and glycophospholipids. They include the polyisoprenyl pyrophosphates.
The formation of crystalline substances from solutions or melts. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
'Glucosephosphates' are organic compounds resulting from the reaction of glucose with phosphoric acid, playing crucial roles in various metabolic processes, such as energy transfer and storage within cells.
Proteins obtained from ESCHERICHIA COLI.
The property of objects that determines the direction of heat flow when they are placed in direct thermal contact. The temperature is the energy of microscopic motions (vibrational and translational) of the particles of atoms.
A class of animal lectins that bind to carbohydrate in a calcium-dependent manner. They share a common carbohydrate-binding domain that is structurally distinct from other classes of lectins.
Enzymes that catalyze either the racemization or epimerization of chiral centers within amino acids or derivatives. EC 5.1.1.
These compounds function as activated monosaccharide carriers in the biosynthesis of glycoproteins and oligosaccharide phospholipids. Obtained from a nucleoside diphosphate sugar and a polyisoprenyl phosphate.
The largest class of organic compounds, including STARCH; GLYCOGEN; CELLULOSE; POLYSACCHARIDES; and simple MONOSACCHARIDES. Carbohydrates are composed of carbon, hydrogen, and oxygen in a ratio of Cn(H2O)n.
Inbred DBA mice are a strain of laboratory mice that are genetically identical and share specific characteristics, including a high incidence of deafness, coat color (black and white), and susceptibility to certain diseases, which make them useful for research purposes in biomedical studies.
Membrane proteins that are involved in the active transport of phosphate.
Antibodies that react with self-antigens (AUTOANTIGENS) of the organism that produced them.
ARTHRITIS that is induced in experimental animals. Immunological methods and infectious agents can be used to develop experimental arthritis models. These methods include injections of stimulators of the immune response, such as an adjuvant (ADJUVANTS, IMMUNOLOGIC) or COLLAGEN.
The level of protein structure in which combinations of secondary protein structures (alpha helices, beta sheets, loop regions, and motifs) pack together to form folded shapes called domains. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure. Small proteins usually consist of only one domain but larger proteins may contain a number of domains connected by segments of polypeptide chain which lack regular secondary structure.
A chronic systemic disease, primarily of the joints, marked by inflammatory changes in the synovial membranes and articular structures, widespread fibrinoid degeneration of the collagen fibers in mesenchymal tissues, and by atrophy and rarefaction of bony structures. Etiology is unknown, but autoimmune mechanisms have been implicated.
Steroid derivatives formed by oxidation of a methyl group on the side chain or a methylene group in the ring skeleton to form a ketone.
This is the active form of VITAMIN B 6 serving as a coenzyme for synthesis of amino acids, neurotransmitters (serotonin, norepinephrine), sphingolipids, aminolevulinic acid. During transamination of amino acids, pyridoxal phosphate is transiently converted into pyridoxamine phosphate (PYRIDOXAMINE).
The functional hereditary units of BACTERIA.
Contractile tissue that produces movement in animals.
Polysaccharides consisting of mannose units.
Enzymes that catalyze the rearrangement of geometry about double bonds. EC 5.2.
Cell surface proteins that bind signalling molecules external to the cell with high affinity and convert this extracellular event into one or more intracellular signals that alter the behavior of the target cell (From Alberts, Molecular Biology of the Cell, 2nd ed, pp693-5). Cell surface receptors, unlike enzymes, do not chemically alter their ligands.
A species of gram-positive bacteria that is a common soil and water saprophyte.
Xylose is a monosaccharide, a type of sugar, that is commonly found in woody plants and fruits, and it is used in medical testing to assess the absorptive capacity of the small intestine.
The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.
Glycoside hydrolases that catalyze the hydrolysis of alpha or beta linked MANNOSE.
Endogenous tissue constituents that have the ability to interact with AUTOANTIBODIES and cause an immune response.
Deoxyribonucleic acid that makes up the genetic material of protozoa.
An aldohexose that occurs naturally in the D-form in lactose, cerebrosides, gangliosides, and mucoproteins. Deficiency of galactosyl-1-phosphate uridyltransferase (GALACTOSE-1-PHOSPHATE URIDYL-TRANSFERASE DEFICIENCY DISEASE) causes an error in galactose metabolism called GALACTOSEMIA, resulting in elevations of galactose in the blood.
The sequence of carbohydrates within POLYSACCHARIDES; GLYCOPROTEINS; and GLYCOLIPIDS.
Phosphoric or pyrophosphoric acid esters of polyisoprenoids.
An enzyme that transfers acyl groups from acyl-CoA to glycerol-3-phosphate to form monoglyceride phosphates. It acts only with CoA derivatives of fatty acids of chain length above C-10. Also forms diglyceride phosphates. EC 2.3.1.15.
The chemical or biochemical addition of carbohydrate or glycosyl groups to other chemicals, especially peptides or proteins. Glycosyl transferases are used in this biochemical reaction.
The restriction of a characteristic behavior, anatomical structure or physical system, such as immune response; metabolic response, or gene or gene variant to the members of one species. It refers to that property which differentiates one species from another but it is also used for phylogenetic levels higher or lower than the species.
A rather large group of enzymes comprising not only those transferring phosphate but also diphosphate, nucleotidyl residues, and others. These have also been subdivided according to the acceptor group. (From Enzyme Nomenclature, 1992) EC 2.7.
Simple sugars, carbohydrates which cannot be decomposed by hydrolysis. They are colorless crystalline substances with a sweet taste and have the same general formula CnH2nOn. (From Dorland, 28th ed)
An amino alcohol with a long unsaturated hydrocarbon chain. Sphingosine and its derivative sphinganine are the major bases of the sphingolipids in mammals. (Dorland, 28th ed)
Any of the processes by which cytoplasmic or intercellular factors influence the differential control of gene action in bacteria.
Hexoses are simple monosaccharides, specifically six-carbon sugars, which include glucose, fructose, and galactose, and play crucial roles in biological processes such as energy production and storage, and structural components of cells.
Conjugated protein-carbohydrate compounds including mucins, mucoid, and amyloid glycoproteins.
The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.
Arthritis is a general term used to describe inflammation in the joints, often resulting in pain, stiffness, and reduced mobility, which can be caused by various conditions such as osteoarthritis, rheumatoid arthritis, gout, or lupus.
The sum of the weight of all the atoms in a molecule.
The monoanhydride of carbamic acid with PHOSPHORIC ACID. It is an important intermediate metabolite and is synthesized enzymatically by CARBAMYL-PHOSPHATE SYNTHASE (AMMONIA) and CARBAMOYL-PHOSPHATE SYNTHASE (GLUTAMINE-HYDROLYZING).
Polysaccharides are complex carbohydrates consisting of long, often branched chains of repeating monosaccharide units joined together by glycosidic bonds, which serve as energy storage molecules (e.g., glycogen), structural components (e.g., cellulose), and molecular recognition sites in various biological systems.
Arabinose is a simple, pentose sugar (a monosaccharide with five carbon atoms) that is a constituent of various polysaccharides and glycosides, particularly found in plant tissues and some microorganisms, and can be metabolized in humans as a source of energy through the pentose phosphate pathway.
Glucosamine is a naturally occurring amino sugar that plays a crucial role in the formation and maintenance of various tissues, particularly in the synthesis of proteoglycans and glycosaminoglycans, which are essential components of cartilage and synovial fluid in joints.
Derivatives of PHOSPHATIDIC ACIDS that lack one of its fatty acyl chains due to its hydrolytic removal.
Cellular processes in biosynthesis (anabolism) and degradation (catabolism) of CARBOHYDRATES.
Spectroscopic method of measuring the magnetic moment of elementary particles such as atomic nuclei, protons or electrons. It is employed in clinical applications such as NMR Tomography (MAGNETIC RESONANCE IMAGING).
Processes involved in the formation of TERTIARY PROTEIN STRUCTURE.
A group of enzymes that catalyze an intramolecular transfer of a phosphate group. It has been shown in some cases that the enzyme has a functional phosphate group, which can act as the donor. These were previously listed under PHOSPHOTRANSFERASES (EC 2.7.-). (From Enzyme Nomenclature, 1992) EC 5.4.2.
Glycosides formed by the reaction of the hydroxyl group on the anomeric carbon atom of mannose with an alcohol to form an acetal. They include both alpha- and beta-mannosides.
Proteins that bind to and are involved in the metabolism of phosphate ions.
The relationships of groups of organisms as reflected by their genetic makeup.
An enzyme that catalyzes the synthesis of fructose-6-phosphate plus GLUTAMINE from GLUTAMATE plus glucosamine-6-phosphate.
A group of enzymes that transfers a phosphate group onto an alcohol group acceptor. EC 2.7.1.
A class of morphologically heterogeneous cytoplasmic particles in animal and plant tissues characterized by their content of hydrolytic enzymes and the structure-linked latency of these enzymes. The intracellular functions of lysosomes depend on their lytic potential. The single unit membrane of the lysosome acts as a barrier between the enzymes enclosed in the lysosome and the external substrate. The activity of the enzymes contained in lysosomes is limited or nil unless the vesicle in which they are enclosed is ruptured. Such rupture is supposed to be under metabolic (hormonal) control. (From Rieger et al., Glossary of Genetics: Classical and Molecular, 5th ed)
Glycerolphosphate Dehydrogenase is an enzyme (EC 1.1.1.8) that catalyzes the reversible conversion of dihydroxyacetone phosphate to glycerol 3-phosphate, using nicotinamide adenine dinucleotide (NAD+) as an electron acceptor in the process.
Fucose is a deoxyhexose sugar, specifically a L-configuration 6-deoxygalactose, often found as a component of complex carbohydrates called glycans in various glycoproteins and glycolipids within the human body.
An enzyme that catalyzes the HYDROLYSIS of terminal, non-reducing alpha-D-mannose residues in alpha-D-mannosides. The enzyme plays a role in the processing of newly formed N-glycans and in degradation of mature GLYCOPROTEINS. There are multiple isoforms of alpha-mannosidase, each having its own specific cellular location and pH optimum. Defects in the lysosomal form of the enzyme results in a buildup of mannoside intermediate metabolites and the disease ALPHA-MANNOSIDOSIS.
A multistage process that includes cloning, physical mapping, subcloning, determination of the DNA SEQUENCE, and information analysis.
In vitro method for producing large amounts of specific DNA or RNA fragments of defined length and sequence from small amounts of short oligonucleotide flanking sequences (primers). The essential steps include thermal denaturation of the double-stranded target molecules, annealing of the primers to their complementary sequences, and extension of the annealed primers by enzymatic synthesis with DNA polymerase. The reaction is efficient, specific, and extremely sensitive. Uses for the reaction include disease diagnosis, detection of difficult-to-isolate pathogens, mutation analysis, genetic testing, DNA sequencing, and analyzing evolutionary relationships.
A 17-KDa cytoplasmic PEPTIDYLPROLYL ISOMERASE involved in immunoregulation. It is a member of the cyclophilin family of proteins that binds to CYCLOSPORINE.
Inbred C57BL mice are a strain of laboratory mice that have been produced by many generations of brother-sister matings, resulting in a high degree of genetic uniformity and homozygosity, making them widely used for biomedical research, including studies on genetics, immunology, cancer, and neuroscience.
A family of peptidyl-prolyl cis-trans isomerases that bind to CYCLOSPORINS and regulate the IMMUNE SYSTEM. EC 5.2.1.-
The phenomenon whereby certain chemical compounds have structures that are different although the compounds possess the same elemental composition. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 5th ed)
Transport proteins that carry specific substances in the blood or across cell membranes.
The characteristic 3-dimensional shape of a carbohydrate.
A chemical reaction in which an electron is transferred from one molecule to another. The electron-donating molecule is the reducing agent or reductant; the electron-accepting molecule is the oxidizing agent or oxidant. Reducing and oxidizing agents function as conjugate reductant-oxidant pairs or redox pairs (Lehninger, Principles of Biochemistry, 1982, p471).
Phosphatidylinositols in which one or more alcohol group of the inositol has been substituted with a phosphate group.

Carbohydrate-deficient glycoprotein syndrome type IA (phosphomannomutase-deficiency). (1/99)

The carbohydrate-deficient glycoprotein or CDG syndromes (OMIM 212065) are a recently delineated group of genetic, multisystem diseases with variable dysmorphic features. The known CDG syndromes are characterized by a partial deficiency of the N-linked glycans of secretory glycoproteins, lysosomal enzymes, and probably also membranous glycoproteins. Due to the deficiency of terminal N-acetylneuraminic acid or sialic acid, the glycan changes can be observed in serum transferrin or other glycoproteins using isoelectrofocusing with immunofixation as the most widely used diagnostic technique. Most patients show a serum sialotransferrin pattern characterized by increased di- and asialotransferrin bands (type I pattern). The majority of patients with type I are phosphomannomutase deficient (type IA), while in a few other patients, deficiencies of phosphomannose isomerase (type IB) or endoplasmic reticulum glucosyltransferase (type IC) have been demonstrated. This review is an update on CDG syndrome type IA.  (+info)

Molecular basis of carbohydrate-deficient glycoprotein syndromes type I with normal phosphomannomutase activity. (2/99)

Carbohydrate deficient glycoprotein syndromes (CDGS) are inherited disorders in glycosylation. Isoelectric focusing of serum transferrin is used as a biochemical indicator of CDGS; however, this technique cannot diagnose the molecular defect. Even though phosphomannomutase (PMM) deficiency accounts for the great majority of known CDGS cases (CDGS type Ia), newly discovered cases have significantly different clinical presentations than the PMM-deficient patients. These differences arise from other defects affecting the biosynthesis of N-linked oligosaccharides in the endoplasmic reticulum and in the Golgi compartment. The most notable is the loss of phosphomannose isomerase (PMI) (CDGS type Ib). It causes severe hypoglycemia, protein-losing enteropathy, vomiting, diarrhea, and congenital hepatic fibrosis. In contrast to PMM-deficiency, there is no developmental delay nor neuropathy. Most symptoms in the PMI-deficient patients can be successfully treated with dietary mannose supplements. Another defect is the lack of glucosylation of the lipid-linked oligosaccharide precursor. The clinical features of this form of CDGS are milder, but similar to, PMM-deficient patients. Yeast genetic and biochemical techniques were critical in unraveling these disorders since many of the defective genes were known in yeast and corresponding mutants were available for complementation. Yeast strains carrying mutations in the homologous genes are likely to provide conclusive identification of the primary defects in novel CDGS types that affect the synthesis and transfer of precursor oligosaccharides.  (+info)

Environmental heterogeneity and balancing selection in the acorn barnacle Semibalanus balanoides. (3/99)

The northern acorn barnacle Semibalans banlanoides occupies several intertidal microhabitats which vary greatly in their degree of physical stress. This environmental heterogeneity creates distinct selection regimes which can maintain genetic variation in natural populations. Despite considerable attention placed on the link between spatial variation in fitness and balancing selection at specific loci, experimental manipulations and fitness estimates for molecular polymorphisms have rarely been conducted in the wild. The aim of this transplant experiment was to manipulate the level of physical stress experienced by a cohort of barnacles in the field and then investigate the spatial variation in fitness for genotypes at three loci: two candidate allozymes and the mitochondrial DNA control region. The viability of mannose-6-phosphate isomerase (Mpi) genotypes was dependent on the level of physical stress experienced in the various treatments; alternative homozygotes were favoured in alternative high stress-low stress environments. In contrast, the fitness of genotypes at other loci was equivalent among treatments and unaffected by the manipulation. Evaluated in the light of balancing selection models, these data indicate that the presence of multiple environmental niches is sufficient to promote a stable Mpi polymorphism in barnacle populations and that allelic variation at this locus reflects the process of adaptation to the heterogeneous intertidal landscape.  (+info)

Aedes aegypti in Tahiti and Moorea (French Polynesia): isoenzyme differentiation in the mosquito population according to human population density. (4/99)

Genetic differences at five polymorphic isoenzyme loci were analyzed by starch gel electrophoresis for 28 Aedes aegypti samples. Considerable (i.e., high Fst values) and significant (i.e., P values >10(-4)) geographic differences were found. Differences in Ae. aegypti genetic structure were related to human population densities and to particularities in mosquito ecotopes in both Tahiti and Moorea islands. In highly urbanized areas (i.e., the Papeete agglomeration), mosquitoes were highly structured. Recurrent extinction events consecutive to insecticidal treatments during dengue outbreaks tend to differentiate mosquito populations. In less populated zones (i.e., the east coast of Moorea and Tahiti), differences in ecotope characteristics could explain the lack of differentiation among mosquitoes from rural environments such as the east coast of Tahiti where natural breeding sites predominate. When the lowest populated zones such as Tahiti Iti and the west coast of Moorea are compared, mosquito are less differentiated in Moorea. These results will be discussed in relation to the recent findings of variation in mosquito infection rates for dengue-2 virus.  (+info)

Mutations in multidrug efflux homologs, sugar isomerases, and antimicrobial biosynthesis genes differentially elevate activity of the sigma(X) and sigma(W) factors in Bacillus subtilis. (5/99)

The sigma(X) and sigma(W) extracytoplasmic function sigma factors regulate more than 40 genes in Bacillus subtilis. sigma(W) activates genes which function in detoxification and the production of antimicrobial compounds, while sigma(X) activates functions that modify the cell envelope. Transposon mutagenesis was used to identify loci which negatively regulate sigma(W) or sigma(X) as judged by up-regulation from the autoregulatory promoter site P(W) or P(X). Fourteen insertions that activate P(W) were identified. The largest class of insertions are likely to affect transport. These include insertions in genes encoding two multidrug efflux protein homologs (yqgE and yulE), a component of the oligopeptide uptake system (oppA), and two transmembrane proteins with weak similarity to transporters (yhdP and yueF). Expression from P(W) is also elevated as a result of inactivation of at least one member of the sigma(W) regulon (ysdB), an ArsR homolog (yvbA), a predicted rhamnose isomerase (yulE), and a gene (pksR) implicated in synthesis of difficidin, a polyketide antibiotic. In a parallel screen, we identified seven insertions that up-regulate P(X). Remarkably, these insertions were in functionally similar genes, including a multidrug efflux homolog (yitG), a mannose-6-phosphate isomerase gene (yjdE), and loci involved in antibiotic synthesis (srfAB and possibly yogA and yngK). Significantly, most insertions that activate P(W) have little or no effect on P(X), and conversely, insertions that activate P(X) have no effect on P(W). This suggests that these two regulons respond to distinct sets of molecular signals which may include toxic molecules which are exported, cell density signals, and antimicrobial compounds.  (+info)

The role of phosphomannose isomerase in Leishmania mexicana glycoconjugate synthesis and virulence. (6/99)

Phosphomannose isomerase (PMI) catalyzes the reversible interconversion of fructose 6-phosphate and mannose 6-phosphate, which is the first step in the biosynthesis of activated mannose donors required for the biosynthesis of various glycoconjugates. Leishmania species synthesize copious amounts of mannose-containing glycolipids and glycoproteins, which are involved in virulence of these parasitic protozoa. To investigate the role of PMI for parasite glycoconjugate synthesis, we have cloned the PMI gene (lmexpmi) from Leishmania mexicana, generated gene deletion mutants (Delta lmexpmi), and analyzed their phenotype. Delta lmexpmi mutants lack completely the high PMI activity found in wild type parasites, but are, in contrast to fungi, able to grow in media deficient for free mannose. The mutants are unable to synthesize phosphoglycan repeats [-6-Gal beta 1-4Man alpha 1-PO(4)-] and mannose-containing glycoinositolphospholipids, and the surface expression of the glycosylphosphatidylinositol-anchored dominant surface glycoprotein leishmanolysin is strongly decreased, unless the parasite growth medium is supplemented with mannose. The Delta lmexpmi mutant is attenuated in infections of macrophages in vitro and of mice, suggesting that PMI may be a target for anti-Leishmania drug development. L. mexicana Delta lmexpmi provides the first conditional mannose-controlled system for parasite glycoconjugate assembly with potential applications for the investigation of their biosynthesis, intracellular sorting, and function.  (+info)

Mannose phosphate isomerase isoenzymes in Plutella xylostella support common genetic bases of resistance to Bacillus thuringiensis toxins in Llpidopteran species. (7/99)

A strong correlation between two mannose phosphate isomerase (MPI) isoenzymes and resistance to Cry1A toxins from Bacillus thuringiensis has been found in a Plutella xylostella population. MPI linkage to Cry1A resistance had previously been reported for a Heliothis virescens population. The fact that the two populations share similar biochemical, genetic, and cross-resistance profiles of resistance suggests the occurrence of homologous resistance loci in both species.  (+info)

Molecular evolution of the GDP-mannose pathway genes (manB and manC) in Salmonella enterica. (8/99)

The evolutionary history of the GDP-mannose pathway in Salmonella enterica was studied via sequencing manB and manC genes from 13 representative strains for O antigens containing mannose and/or sugar derivatives of GDP-D-mannose. In addition, colanic acid (CA) manB and manC genes were sequenced from selected strains, as the basis for a detailed comparison. Interestingly, including the eight previously characterized O antigen gene clusters, 12 of the 21 S. enterica strains studied in total (each representing a different O antigen structure) possess a manB gene which displays DNA identity, ranging from 93 to 99%, to the CA manB gene of S. enterica LT2. Furthermore, the CA-like manB genes (as well as the CA manB and manC genes) display subspecies specificity, and the CA and CA-like manB genes (for individual strains) appear to be evolving in concert via gene conversion events. In comparison, the manC genes were generally not CA-like, a situation also apparent in Escherichia coli,and therefore most strongly reflected the evolutionary history of the S. enterica O antigen GDP-mannose pathway. It appears that, in relatively recent times, gene capture from a distant source has occurred infrequently, and that groups of manB and manC genes have been maintained and are continuing to evolve within S. enterica and more closely related species.  (+info)

Glucose-6-phosphate isomerase (GPI) is an enzyme involved in the glycolytic and gluconeogenesis pathways. It catalyzes the interconversion of glucose-6-phosphate (G6P) and fructose-6-phosphate (F6P), which are key metabolic intermediates in these pathways. This reaction is a reversible step that helps maintain the balance between the breakdown and synthesis of glucose in the cell.

In glycolysis, GPI converts G6P to F6P, which subsequently gets converted to fructose-1,6-bisphosphate (F1,6BP) by the enzyme phosphofructokinase-1 (PFK-1). In gluconeogenesis, the reaction is reversed, and F6P is converted back to G6P.

Deficiency or dysfunction of Glucose-6-phosphate isomerase can lead to various metabolic disorders, such as glycogen storage diseases and hereditary motor neuropathies.

Mannose-6-Phosphate Isomerase (MPI) is an enzyme that catalyzes the interconversion between mannose-6-phosphate and fructose-6-phosphate, which are both key metabolites in the glycolysis and gluconeogenesis pathways. This enzyme plays a crucial role in maintaining the balance between these two metabolic pathways, allowing cells to either break down or synthesize glucose depending on their energy needs.

The gene that encodes for MPI is called MPI1 and is located on chromosome 4 in humans. Defects in this gene can lead to a rare genetic disorder known as Mannose-6-Phosphate Isomerase Deficiency or Congenital Disorder of Glycosylation Type IIm, which is characterized by developmental delay, intellectual disability, seizures, and various other neurological symptoms.

Triose-phosphate isomerase (TPI) is a crucial enzyme in the glycolytic pathway, which is a metabolic process that converts glucose into pyruvate, producing ATP and NADH as energy currency for the cell. TPI specifically catalyzes the reversible interconversion of the triose phosphates dihydroxyacetone phosphate (DHAP) and glyceraldehyde 3-phosphate (G3P). This interconversion is a vital step in maintaining the balance of metabolites in the glycolytic pathway.

The reaction catalyzed by TPI is as follows:

Dihydroxyacetone phosphate ↔ Glyceraldehyde 3-phosphate

Deficiency or mutations in the gene encoding triose-phosphate isomerase can lead to a severe autosomal recessive disorder known as Triose Phosphate Isomerase Deficiency (TID). This condition is characterized by chronic hemolytic anemia, neuromuscular symptoms, and shortened lifespan.

Aldose-ketose isomerases are a group of enzymes that catalyze the interconversion between aldoses and ketoses, which are different forms of sugars. These enzymes play an essential role in carbohydrate metabolism by facilitating the reversible conversion of aldoses to ketoses and vice versa.

Aldoses are sugars that contain a carbonyl group (a functional group consisting of a carbon atom double-bonded to an oxygen atom) at the end of the carbon chain, while ketoses have their carbonyl group located in the middle of the chain. The isomerization process catalyzed by aldose-ketose isomerases helps maintain the balance between these two forms of sugars and enables cells to utilize them more efficiently for energy production and other metabolic processes.

There are several types of aldose-ketose isomerases, including:

1. Triose phosphate isomerase (TPI): This enzyme catalyzes the interconversion between dihydroxyacetone phosphate (a ketose) and D-glyceraldehyde 3-phosphate (an aldose), which are both trioses (three-carbon sugars). TPI plays a crucial role in glycolysis, the metabolic pathway that breaks down glucose to produce energy.
2. Xylulose kinase: This enzyme is involved in the pentose phosphate pathway, which is a metabolic route that generates reducing equivalents (NADPH) and pentoses for nucleic acid synthesis. Xylulose kinase catalyzes the conversion of D-xylulose (a ketose) to D-xylulose 5-phosphate, an important intermediate in the pentose phosphate pathway.
3. Ribulose-5-phosphate 3-epimerase: This enzyme is also part of the pentose phosphate pathway and catalyzes the interconversion between D-ribulose 5-phosphate (an aldose) and D-xylulose 5-phosphate (a ketose).
4. Phosphoglucomutase: This enzyme catalyzes the reversible conversion of glucose 1-phosphate (an aldose) to glucose 6-phosphate (an aldose), which is an important intermediate in both glycolysis and gluconeogenesis.
5. Phosphomannomutase: This enzyme catalyzes the reversible conversion of mannose 1-phosphate (a ketose) to mannose 6-phosphate (an aldose), which is involved in the biosynthesis of complex carbohydrates.

These are just a few examples of enzymes that catalyze the interconversion between aldoses and ketoses, highlighting their importance in various metabolic pathways.

Mannose is a simple sugar (monosaccharide) that is similar in structure to glucose. It is a hexose, meaning it contains six carbon atoms. Mannose is a stereoisomer of glucose, meaning it has the same chemical formula but a different structural arrangement of its atoms.

Mannose is not as commonly found in foods as other simple sugars, but it can be found in some fruits, such as cranberries, blueberries, and peaches, as well as in certain vegetables, like sweet potatoes and turnips. It is also found in some dietary fibers, such as those found in beans and whole grains.

In the body, mannose can be metabolized and used for energy, but it is also an important component of various glycoproteins and glycolipids, which are molecules that play critical roles in many biological processes, including cell recognition, signaling, and adhesion.

Mannose has been studied as a potential therapeutic agent for various medical conditions, including urinary tract infections (UTIs), because it can inhibit the attachment of certain bacteria to the cells lining the urinary tract. Additionally, mannose-binding lectins have been investigated for their potential role in the immune response to viral and bacterial infections.

Trioses are simple sugars that contain three carbon atoms and a functional group called a ketone or aldehyde. They are the simplest type of sugar molecule, after monosaccharides such as glyceraldehyde and dihydroxyacetone.

Triose sugars can exist in two structural forms:

* Dihydroxyacetone (DHA), which is a ketotriose with the formula CH2OH-CO-CH2OH, and
* Glyceraldehyde (GA), which is an aldotriose with the formula HO-CHOH-CHO.

Trioses play important roles in various metabolic pathways, including glycolysis, gluconeogenesis, and the Calvin cycle of photosynthesis. In particular, DHA and GA are intermediates in the conversion of glucose to pyruvate during glycolysis, and they are also produced from pyruvate during gluconeogenesis.

Trioses can be synthesized chemically or biochemically through various methods, such as enzymatic reactions or microbial fermentation. They have potential applications in the food, pharmaceutical, and chemical industries, as they can serve as building blocks for more complex carbohydrates or as precursors for other organic compounds.

Carbohydrate epimerases are a group of enzymes that catalyze the interconversion of specific stereoisomers (epimers) of carbohydrates by the reversible oxidation and reduction of carbon atoms, usually at the fourth or fifth position. These enzymes play important roles in the biosynthesis and modification of various carbohydrate-containing molecules, such as glycoproteins, proteoglycans, and glycolipids, which are involved in numerous biological processes including cell recognition, signaling, and adhesion.

The reaction catalyzed by carbohydrate epimerases involves the transfer of a hydrogen atom and a proton between two adjacent carbon atoms, leading to the formation of new stereochemical configurations at these positions. This process can result in the conversion of one epimer into another, thereby expanding the structural diversity of carbohydrates and their derivatives.

Carbohydrate epimerases are classified based on the type of substrate they act upon and the specific stereochemical changes they induce. Some examples include UDP-glucose 4-epimerase, which interconverts UDP-glucose and UDP-galactose; UDP-N-acetylglucosamine 2-epimerase, which converts UDP-N-acetylglucosamine to UDP-N-acetylmannosamine; and GDP-fucose synthase, which catalyzes the conversion of GDP-mannose to GDP-fucose.

Understanding the function and regulation of carbohydrate epimerases is crucial for elucidating their roles in various biological processes and developing strategies for targeting them in therapeutic interventions.

Phosphates, in a medical context, refer to the salts or esters of phosphoric acid. Phosphates play crucial roles in various biological processes within the human body. They are essential components of bones and teeth, where they combine with calcium to form hydroxyapatite crystals. Phosphates also participate in energy transfer reactions as phosphate groups attached to adenosine diphosphate (ADP) and adenosine triphosphate (ATP). Additionally, they contribute to buffer systems that help maintain normal pH levels in the body.

Abnormal levels of phosphates in the blood can indicate certain medical conditions. High phosphate levels (hyperphosphatemia) may be associated with kidney dysfunction, hyperparathyroidism, or excessive intake of phosphate-containing products. Low phosphate levels (hypophosphatemia) might result from malnutrition, vitamin D deficiency, or certain diseases affecting the small intestine or kidneys. Both hypophosphatemia and hyperphosphatemia can have significant impacts on various organ systems and may require medical intervention.

Isomerases are a class of enzymes that catalyze the interconversion of isomers of a single molecule. They do this by rearranging atoms within a molecule to form a new structural arrangement or isomer. Isomerases can act on various types of chemical bonds, including carbon-carbon and carbon-oxygen bonds.

There are several subclasses of isomerases, including:

1. Racemases and epimerases: These enzymes interconvert stereoisomers, which are molecules that have the same molecular formula but different spatial arrangements of their atoms in three-dimensional space.
2. Cis-trans isomerases: These enzymes interconvert cis and trans isomers, which differ in the arrangement of groups on opposite sides of a double bond.
3. Intramolecular oxidoreductases: These enzymes catalyze the transfer of electrons within a single molecule, resulting in the formation of different isomers.
4. Mutases: These enzymes catalyze the transfer of functional groups within a molecule, resulting in the formation of different isomers.
5. Tautomeres: These enzymes catalyze the interconversion of tautomers, which are isomeric forms of a molecule that differ in the location of a movable hydrogen atom and a double bond.

Isomerases play important roles in various biological processes, including metabolism, signaling, and regulation.

A pentose is a monosaccharide (simple sugar) that contains five carbon atoms. The name "pentose" comes from the Greek word "pente," meaning five, and "ose," meaning sugar. Pentoses play important roles in various biological processes, such as serving as building blocks for nucleic acids (DNA and RNA) and other biomolecules.

Some common pentoses include:

1. D-Ribose - A naturally occurring pentose found in ribonucleic acid (RNA), certain coenzymes, and energy-carrying molecules like adenosine triphosphate (ATP).
2. D-Deoxyribose - A pentose that lacks a hydroxyl (-OH) group on the 2' carbon atom, making it a key component of deoxyribonucleic acid (DNA).
3. Xylose - A naturally occurring pentose found in various plants and woody materials; it is used as a sweetener and food additive.
4. Arabinose - Another plant-derived pentose, arabinose can be found in various fruits, vegetables, and grains. It has potential applications in the production of biofuels and other bioproducts.
5. Lyxose - A less common pentose that can be found in some polysaccharides and glycoproteins.

Pentoses are typically less sweet than hexoses (six-carbon sugars) like glucose or fructose, but they still contribute to the overall sweetness of many foods and beverages.

Ribulose phosphates are organic compounds that play a crucial role in the Calvin cycle, which is a part of photosynthesis. The Calvin cycle is the process by which plants, algae, and some bacteria convert carbon dioxide into glucose and other simple sugars.

Ribulose phosphates are sugar phosphates that contain five carbon atoms and have the chemical formula C5H10O5P. They exist in two forms: ribulose 5-phosphate (Ru5P) and ribulose 1,5-bisphosphate (RuBP).

Ribulose 1,5-bisphosphate is the starting point for carbon fixation in the Calvin cycle. In this process, an enzyme called RuBisCO (ribulose-1,5-bisphosphate carboxylase/oxygenase) catalyzes the reaction between RuBP and carbon dioxide to form two molecules of 3-phosphoglycerate, which are then converted into glucose and other sugars.

Ribulose phosphates are also involved in other metabolic pathways, such as the pentose phosphate pathway, which generates reducing power in the form of NADPH and produces ribose-5-phosphate, a precursor for nucleotide synthesis.

Hexose phosphates are organic compounds that consist of a hexose sugar molecule (a monosaccharide containing six carbon atoms, such as glucose or fructose) that has been phosphorylated, meaning that a phosphate group has been added to it. This process is typically facilitated by enzymes called kinases, which transfer a phosphate group from a donor molecule (usually ATP) to the sugar molecule.

Hexose phosphates play important roles in various metabolic pathways, including glycolysis, gluconeogenesis, and the pentose phosphate pathway. For example, glucose-6-phosphate is a key intermediate in both glycolysis and gluconeogenesis, while fructose-6-phosphate and fructose-1,6-bisphosphate are important intermediates in glycolysis. The pentose phosphate pathway, which is involved in the production of NADPH and ribose-5-phosphate, begins with the conversion of glucose-6-phosphate to 6-phosphogluconolactone by the enzyme glucose-6-phosphate dehydrogenase.

Overall, hexose phosphates are important metabolic intermediates that help regulate energy production and utilization in cells.

Hemolytic anemia, congenital nonspherocytic is a rare type of inherited anemia characterized by the premature destruction (hemolysis) of red blood cells. This condition is caused by defects in enzymes or proteins that help maintain the structural integrity and function of red blood cells.

In this form of hemolytic anemia, the red blood cells are not spherical in shape like spherocytes; instead, they may be oval or elongated. The most common types of congenital nonspherocytic hemolytic anemia are caused by deficiencies in enzymes such as glucose-6-phosphate dehydrogenase (G6PD) and pyruvate kinase.

Symptoms of this condition may include fatigue, weakness, pale skin, jaundice, dark urine, and an enlarged spleen. Treatment may involve blood transfusions, medications to manage symptoms, and avoidance of certain triggers that can exacerbate the hemolysis. In some cases, a bone marrow transplant may be considered as a curative treatment option.

Peptidylprolyl Isomerase (PPIase) is an enzyme that catalyzes the cis-trans isomerization of peptidyl-prolyl bonds in proteins. This isomerization process, which involves the rotation around a proline bond, is a rate-limiting step in protein folding and can be a significant factor in the development of various diseases, including neurodegenerative disorders and cancer.

PPIases are classified into three families: cyclophilins, FK506-binding proteins (FKBPs), and parvulins. These enzymes play important roles in protein folding, trafficking, and degradation, as well as in signal transduction pathways and the regulation of gene expression.

Inhibitors of PPIases have been developed as potential therapeutic agents for various diseases, including transplant rejection, autoimmune disorders, and cancer. For example, cyclosporine A and FK506 are immunosuppressive drugs that inhibit cyclophilins and FKBPs, respectively, and are used to prevent transplant rejection.

The Pentose Phosphate Pathway (also known as the Hexose Monophosphate Shunt or HMP Shunt) is a metabolic pathway that runs parallel to glycolysis. It serves two major functions:

1. Providing reducing equivalents in the form of NADPH for reductive biosynthesis and detoxification processes.
2. Generating ribose-5-phosphate, a pentose sugar used in the synthesis of nucleotides and nucleic acids (DNA and RNA).

This pathway begins with the oxidation of glucose-6-phosphate to form 6-phosphogluconolactone, catalyzed by the enzyme glucose-6-phosphate dehydrogenase. The resulting NADPH is used in various anabolic reactions and antioxidant defense systems.

The Pentose Phosphate Pathway also includes a series of reactions called the non-oxidative branch, which interconverts various sugars to meet cellular needs for different types of monosaccharides. These conversions are facilitated by several enzymes including transketolase and transaldolase.

Dihydroxyacetone Phosphate (DHAP) is a 3-carbon organic compound that plays a crucial role in the metabolic pathway called glycolysis. It is an intermediate molecule formed during the conversion of glucose into pyruvate, which ultimately produces energy in the form of ATP.

In the glycolytic process, DHAP is produced from glyceraldehyde 3-phosphate (G3P) in a reaction catalyzed by the enzyme triose phosphate isomerase. Then, DHAP is converted back to G3P in a subsequent step, which prepares it for further processing in the glycolytic pathway. This reversible conversion of DHAP and G3P helps maintain the equilibrium of the glycolytic process.

Apart from its role in energy metabolism, DHAP is also involved in other biochemical processes, such as the synthesis of glucose during gluconeogenesis and the formation of lipids in the liver.

Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is an enzyme that plays a crucial role in the metabolic pathway of glycolysis. Its primary function is to convert glyceraldehyde-3-phosphate (a triose sugar phosphate) into D-glycerate 1,3-bisphosphate, while also converting nicotinamide adenine dinucleotide (NAD+) into its reduced form NADH. This reaction is essential for the production of energy in the form of adenosine triphosphate (ATP) during cellular respiration. GAPDH has also been implicated in various non-metabolic processes, including DNA replication, repair, and transcription regulation, due to its ability to interact with different proteins and nucleic acids.

Fructose-bisphosphate aldolase is a crucial enzyme in the glycolytic pathway, which is a metabolic process that breaks down glucose to produce energy. This enzyme catalyzes the conversion of fructose-1,6-bisphosphate into two triose sugars: dihydroxyacetone phosphate and glyceraldehyde-3-phosphate.

There are two main types of aldolase isoenzymes in humans, classified as aldolase A (or muscle type) and aldolase B (or liver type). Fructose-bisphosphate aldolase refers specifically to aldolase A, which is primarily found in the muscles, brain, and red blood cells. Aldolase B, on the other hand, is predominantly found in the liver, kidney, and small intestine.

Deficiency or dysfunction of fructose-bisphosphate aldolase can lead to metabolic disorders, such as hereditary fructose intolerance, which results from a deficiency in another enzyme called aldolase B. However, it is essential to note that the term "fructose-bisphosphate aldolase" typically refers to aldolase A and not aldolase B.

Ribose is a simple carbohydrate, specifically a monosaccharide, which means it is a single sugar unit. It is a type of sugar known as a pentose, containing five carbon atoms. Ribose is a vital component of ribonucleic acid (RNA), one of the essential molecules in all living cells, involved in the process of transcribing and translating genetic information from DNA to proteins. The term "ribose" can also refer to any sugar alcohol derived from it, such as D-ribose or Ribitol.

Glycerophosphates are esters of glycerol and phosphoric acid. In the context of biochemistry and medicine, glycerophosphates often refer to glycerol 3-phosphate (also known as glyceraldehyde 3-phosphate or glycerone phosphate) and its derivatives.

Glycerol 3-phosphate plays a crucial role in cellular metabolism, particularly in the process of energy production and storage. It is an important intermediate in both glycolysis (the breakdown of glucose to produce energy) and gluconeogenesis (the synthesis of glucose from non-carbohydrate precursors).

In addition, glycerophosphates are also involved in the formation of phospholipids, a major component of cell membranes. The esterification of glycerol 3-phosphate with fatty acids leads to the synthesis of phosphatidic acid, which is a key intermediate in the biosynthesis of other phospholipids.

Abnormalities in glycerophosphate metabolism have been implicated in various diseases, including metabolic disorders and neurological conditions.

Protein Disulfide-Isomerases (PDIs) are a family of enzymes found in the endoplasmic reticulum (ER) of eukaryotic cells. They play a crucial role in the folding and maturation of proteins by catalyzing the formation, breakage, and rearrangement of disulfide bonds between cysteine residues in proteins. This process helps to stabilize the three-dimensional structure of proteins and is essential for their proper function. PDIs also have chaperone activity, helping to prevent protein aggregation and assisting in the correct folding of nascent polypeptides. Dysregulation of PDI function has been implicated in various diseases, including cancer, neurodegenerative disorders, and diabetes.

Acetone is a colorless, volatile, and flammable liquid organic compound with the chemical formula (CH3)2CO. It is the simplest and smallest ketone, and its molecules consist of a carbonyl group linked to two methyl groups. Acetone occurs naturally in the human body and is produced as a byproduct of normal metabolic processes, particularly during fat burning.

In clinical settings, acetone can be measured in breath or blood to assess metabolic status, such as in cases of diabetic ketoacidosis, where an excess production of acetone and other ketones occurs due to insulin deficiency and high levels of fatty acid breakdown. High concentrations of acetone can lead to a sweet, fruity odor on the breath, often described as "fruity acetone" or "acetone breath."

Ribose monophosphates are organic compounds that play a crucial role in the metabolism of cells, particularly in energy transfer and nucleic acid synthesis. A ribose monophosphate is formed by the attachment of a phosphate group to a ribose molecule, which is a type of sugar known as a pentose.

In biochemistry, there are two important ribose monophosphates:

1. Alpha-D-Ribose 5-Phosphate (ADP-Ribose): This compound serves as an essential substrate in various cellular processes, including DNA repair, chromatin remodeling, and protein modification. The enzyme that catalyzes the formation of ADP-ribose is known as poly(ADP-ribose) polymerase (PARP).
2. Ribulose 5-Phosphate: This compound is a key intermediate in the Calvin cycle, which is the process by which plants and some bacteria convert carbon dioxide into glucose during photosynthesis. Ribulose 5-phosphate is formed from ribose 5-phosphate through a series of enzymatic reactions.

Ribose monophosphates are essential for the proper functioning of cells and have implications in various physiological processes, as well as in certain disease states.

Transaldolase is not a medical term per se, but it is a term used in biochemistry and molecular biology. Transaldolase is an enzyme involved in the pentose phosphate pathway (PPP), which is a metabolic pathway that supplies reducing energy to cells by converting glucose-6-phosphate into ribulose-5-phosphate, a key intermediate in the synthesis of nucleotides.

The medical relevance of transaldolase lies in its role in maintaining cellular redox balance and providing precursors for nucleic acid synthesis. Defects in the PPP can lead to various metabolic disorders, including some forms of congenital cataracts, neurological dysfunction, and growth retardation. However, specific diseases or conditions directly attributed to transaldolase deficiency are not well-established.

Molecular sequence data refers to the specific arrangement of molecules, most commonly nucleotides in DNA or RNA, or amino acids in proteins, that make up a biological macromolecule. This data is generated through laboratory techniques such as sequencing, and provides information about the exact order of the constituent molecules. This data is crucial in various fields of biology, including genetics, evolution, and molecular biology, allowing for comparisons between different organisms, identification of genetic variations, and studies of gene function and regulation.

I'm sorry for any confusion, but "Mannosephosphates" is not a widely recognized or established term in medicine or biochemistry. It seems that this term may be a combination of "mannose," which is a type of sugar (monosaccharide), and "phosphates," which are compounds containing phosphorus. However, without more context, it's difficult to provide an accurate medical definition for this term.

In biochemistry, mannose can be linked to phosphate groups in various ways, such as in the context of mannose-1-phosphate or mannose-6-phosphate, which are involved in different metabolic pathways. If you could provide more information about where you encountered this term, I might be able to give a more precise definition or explanation.

Steroid isomerases are a class of enzymes that catalyze the interconversion of steroids by rearranging various chemical bonds within their structures, leading to the formation of isomers. These enzymes play crucial roles in steroid biosynthesis and metabolism, enabling the production of a diverse array of steroid hormones with distinct biological activities.

There are several types of steroid isomerases, including:

1. 3-beta-hydroxysteroid dehydrogenase/delta(5)-delta(4) isomerase (3-beta-HSD): This enzyme catalyzes the conversion of delta(5) steroids to delta(4) steroids, accompanied by the oxidation of a 3-beta-hydroxyl group to a keto group. It is essential for the biosynthesis of progesterone, cortisol, and aldosterone.
2. Aromatase: This enzyme converts androgens (such as testosterone) into estrogens (such as estradiol) by introducing a phenolic ring, which results in the formation of an aromatic A-ring. It is critical for the development and maintenance of female secondary sexual characteristics.
3. 17-beta-hydroxysteroid dehydrogenase (17-beta-HSD): This enzyme catalyzes the interconversion between 17-keto and 17-beta-hydroxy steroids, playing a key role in the biosynthesis of estrogens, androgens, and glucocorticoids.
4. 5-alpha-reductase: This enzyme catalyzes the conversion of testosterone to dihydrotestosterone (DHT) by reducing the double bond between carbons 4 and 5 in the A-ring. DHT is a more potent androgen than testosterone, playing essential roles in male sexual development and prostate growth.
5. 20-alpha-hydroxysteroid dehydrogenase (20-alpha-HSD): This enzyme catalyzes the conversion of corticosterone to aldosterone, a critical mineralocorticoid involved in regulating electrolyte and fluid balance.
6. 3-beta-hydroxysteroid dehydrogenase (3-beta-HSD): This enzyme catalyzes the conversion of pregnenolone to progesterone and 17-alpha-hydroxypregnenolone to 17-alpha-hydroxyprogesterone, which are essential intermediates in steroid hormone biosynthesis.

These enzymes play crucial roles in the biosynthesis, metabolism, and elimination of various steroid hormones, ensuring proper endocrine function and homeostasis. Dysregulation or mutations in these enzymes can lead to various endocrine disorders, including congenital adrenal hyperplasia (CAH), polycystic ovary syndrome (PCOS), androgen insensitivity syndrome (AIS), and others.

Pentose phosphates are monosaccharides that contain five carbon atoms and one phosphate group. They play a crucial role in various metabolic pathways, including the pentose phosphate pathway (PPP), which is a major source of NADPH and ribose-5-phosphate for the synthesis of nucleotides.

The pentose phosphate pathway involves two main phases: the oxidative phase and the non-oxidative phase. In the oxidative phase, glucose-6-phosphate is converted to ribulose-5-phosphate, producing NADPH and CO2 as byproducts. Ribulose-5-phosphate can then be further metabolized in the non-oxidative phase to produce other pentose phosphates or converted back to glucose-6-phosphate through a series of reactions.

Pentose phosphates are also important intermediates in the synthesis of nucleotides, coenzymes, and other metabolites. Abnormalities in pentose phosphate pathway enzymes can lead to various metabolic disorders, such as defects in erythrocyte function and increased susceptibility to oxidative stress.

IGF-2 (Insulin-like Growth Factor 2) receptor is a type of transmembrane protein that plays a role in cell growth, differentiation, and survival. Unlike other receptors in the insulin and IGF family, IGF-2 receptor does not mediate the activation of intracellular signaling pathways upon binding to its ligand (IGF-2). Instead, it acts as a clearance receptor that facilitates the removal of IGF-2 from circulation by transporting it to lysosomes for degradation.

The IGF-2 receptor is also known as cation-independent mannose-6-phosphate receptor (CI-M6PR) because it can also bind and transport mannose-6-phosphate-containing enzymes to lysosomes for degradation.

Mutations in the IGF-2 receptor gene have been associated with certain types of cancer, as well as developmental disorders such as Beckwith-Wiedemann syndrome.

Dodecenoyl-CoA isomerase is an enzyme that catalyzes the conversion of dodecenoyl-CoA to trans-2-dodecenoyl-CoA in the beta-oxidation pathway of fatty acid metabolism. This enzyme plays a crucial role in the breakdown and energy production from long-chain fatty acids in the body. The isomerization reaction facilitated by this enzyme helps to introduce a double bond at a specific position during the degradation process, allowing for further oxidation and energy release.

Carbon-carbon double bond isomerases are a class of enzymes that catalyze the conversion of one geometric or positional isomer of a molecule containing a carbon-carbon double bond into another. These enzymes play an important role in the metabolism and biosynthesis of various biological compounds, including fatty acids, steroids, and carotenoids.

There are several types of carbon-carbon double bond isomerases, each with their own specific mechanisms and substrate preferences. Some examples include:

1. Ene/Yne Isomerases: These enzymes catalyze the conversion of a carbon-carbon double bond that is conjugated to an alkene or alkyne group into a new double bond location through a series of [1,5]-sigmatropic shifts.

2. Cis-Trans Isomerases: These enzymes catalyze the interconversion of cis and trans geometric isomers of carbon-carbon double bonds. They are often involved in the biosynthesis of complex lipids and other biological molecules where specific stereochemistry is required for proper function.

3. Peroxisomal Isomerases: These enzymes are involved in the metabolism of fatty acids with very long chains (VLCFA) in peroxisomes. They catalyze the conversion of cis-delta(3)-double bonds to trans-delta(2)-double bonds, which is a necessary step for further processing and degradation of VLCFAs.

4. Retinal Isomerases: These enzymes are involved in the visual cycle and catalyze the conversion of 11-cis-retinal into all-trans-retinal during the process of vision.

5. Carotenoid Isomerases: These enzymes are involved in the biosynthesis of carotenoids, which are pigments found in plants and microorganisms. They catalyze the conversion of cis-configured carotenoids into trans-configured forms, which have higher stability and bioactivity.

In general, carbon-carbon double bond isomerases function by lowering the energy barrier for a specific isomerization reaction, allowing it to occur under physiological conditions. They often require cofactors or other proteins to facilitate their activity, and their regulation is critical for maintaining proper metabolism and homeostasis in cells.

An amino acid sequence is the specific order of amino acids in a protein or peptide molecule, formed by the linking of the amino group (-NH2) of one amino acid to the carboxyl group (-COOH) of another amino acid through a peptide bond. The sequence is determined by the genetic code and is unique to each type of protein or peptide. It plays a crucial role in determining the three-dimensional structure and function of proteins.

Phosphofructokinase-1 (PFK-1) is a rate-limiting enzyme in the glycolytic pathway, which is the metabolic pathway that converts glucose into pyruvate, producing ATP and NADH as energy currency for the cell. PFK-1 plays a crucial role in regulating the rate of glycolysis by catalyzing the phosphorylation of fructose-6-phosphate to fructose-1,6-bisphosphate, using ATP as the phosphate donor.

PFK-1 is allosterically regulated by various metabolites, such as AMP, ADP, and ATP, which act as positive or negative effectors of the enzyme's activity. For example, an increase in the intracellular concentration of AMP or ADP can activate PFK-1, promoting glycolysis and energy production, while an increase in ATP levels can inhibit the enzyme's activity, conserving glucose for use under conditions of low energy demand.

Deficiencies in PFK-1 can lead to a rare genetic disorder called Tarui's disease or glycogen storage disease type VII, which is characterized by exercise intolerance, muscle cramps, and myoglobinuria (the presence of myoglobin in the urine due to muscle damage).

Geobacillus is a genus of gram-positive, spore-forming bacteria that are thermophilic, meaning they thrive at relatively high temperatures, typically between 45-70°C. These bacteria are commonly found in hot environments such as volcanic vents, hot springs, and oil fields. They have the ability to break down complex organic matter, making them of interest for potential industrial applications like bioremediation and biofuel production. Some species within this genus can also cause spoilage of canned foods when exposed to high temperatures during processing. It's worth noting that while Geobacillus spp. are generally not harmful to humans, they may be capable of causing infection in immunocompromised individuals.

Glyceraldehyde-3-phosphate dehydrogenase (GAPDH), also known as Glucosephosphate Dehydrogenase, is an enzyme that plays a crucial role in cellular metabolism, particularly in the glycolytic pathway. It catalyzes the conversion of glyceraldehyde 3-phosphate (G3P) to 1,3-bisphosphoglycerate (1,3-BPG), while also converting nicotinamide adenine dinucleotide (NAD+) to its reduced form NADH. This reaction is essential for the production of energy in the form of adenosine triphosphate (ATP) during cellular respiration. GAPDH has been widely used as a housekeeping gene in molecular biology research due to its consistent expression across various tissues and cells, although recent studies have shown that its expression can vary under certain conditions.

Mannose-binding lectins (MBLs) are a group of proteins that belong to the collectin family and play a crucial role in the innate immune system. They are primarily produced by the liver and secreted into the bloodstream. MBLs have a specific affinity for mannose sugar residues found on the surface of various microorganisms, including bacteria, viruses, fungi, and parasites.

The primary function of MBLs is to recognize and bind to these mannose-rich structures, which triggers the complement system's activation through the lectin pathway. This process leads to the destruction of the microorganism by opsonization (coating the microbe to enhance phagocytosis) or direct lysis. MBLs also have the ability to neutralize certain viruses and inhibit the replication of others, further contributing to their antimicrobial activity.

Deficiencies in MBL levels or function have been associated with an increased susceptibility to infections, particularly in children and older adults. However, the clinical significance of MBL deficiency remains a subject of ongoing research.

In the context of medicine and pharmacology, "kinetics" refers to the study of how a drug moves throughout the body, including its absorption, distribution, metabolism, and excretion (often abbreviated as ADME). This field is called "pharmacokinetics."

1. Absorption: This is the process of a drug moving from its site of administration into the bloodstream. Factors such as the route of administration (e.g., oral, intravenous, etc.), formulation, and individual physiological differences can affect absorption.

2. Distribution: Once a drug is in the bloodstream, it gets distributed throughout the body to various tissues and organs. This process is influenced by factors like blood flow, protein binding, and lipid solubility of the drug.

3. Metabolism: Drugs are often chemically modified in the body, typically in the liver, through processes known as metabolism. These changes can lead to the formation of active or inactive metabolites, which may then be further distributed, excreted, or undergo additional metabolic transformations.

4. Excretion: This is the process by which drugs and their metabolites are eliminated from the body, primarily through the kidneys (urine) and the liver (bile).

Understanding the kinetics of a drug is crucial for determining its optimal dosing regimen, potential interactions with other medications or foods, and any necessary adjustments for special populations like pediatric or geriatric patients, or those with impaired renal or hepatic function.

Aldehyde-lyases are a class of enzymes that catalyze the breakdown or synthesis of molecules involving an aldehyde group through a reaction known as lyase cleavage. This type of reaction results in the removal of a molecule, typically water or carbon dioxide, from the substrate.

In the case of aldehyde-lyases, these enzymes specifically catalyze reactions that involve the conversion of an aldehyde into a carboxylic acid or vice versa. These enzymes are important in various metabolic pathways and play a crucial role in the biosynthesis and degradation of several biomolecules, including carbohydrates, amino acids, and lipids.

The systematic name for this class of enzymes is "ald(e)hyde-lyases." They are classified under EC number 4.3.1 in the Enzyme Commission (EC) system.

Glycolysis is a fundamental metabolic pathway that occurs in the cytoplasm of cells, consisting of a series of biochemical reactions. It's the process by which a six-carbon glucose molecule is broken down into two three-carbon pyruvate molecules. This process generates a net gain of two ATP molecules (the main energy currency in cells), two NADH molecules, and two water molecules.

Glycolysis can be divided into two stages: the preparatory phase (or 'energy investment' phase) and the payoff phase (or 'energy generation' phase). During the preparatory phase, glucose is phosphorylated twice to form glucose-6-phosphate and then converted to fructose-1,6-bisphosphate. These reactions consume two ATP molecules but set up the subsequent breakdown of fructose-1,6-bisphosphate into triose phosphates in the payoff phase. In this second stage, each triose phosphate is further oxidized and degraded to produce one pyruvate molecule, one NADH molecule, and one ATP molecule through substrate-level phosphorylation.

Glycolysis does not require oxygen to proceed; thus, it can occur under both aerobic (with oxygen) and anaerobic (without oxygen) conditions. In the absence of oxygen, the pyruvate produced during glycolysis is further metabolized through fermentation pathways such as lactic acid fermentation or alcohol fermentation to regenerate NAD+, which is necessary for glycolysis to continue.

In summary, glycolysis is a crucial process in cellular energy metabolism, allowing cells to convert glucose into ATP and other essential molecules while also serving as a starting point for various other biochemical pathways.

Guanosine diphosphate mannose (GDP-mannose) is a nucleotide sugar that plays a crucial role in the biosynthesis of various glycans, including those found on proteins and lipids. It is formed from mannose-1-phosphate through the action of the enzyme mannose-1-phosphate guanylyltransferase, using guanosine triphosphate (GTP) as a source of energy.

GDP-mannose serves as a donor substrate for several glycosyltransferases involved in the biosynthesis of complex carbohydrates, such as those found in glycoproteins and glycolipids. It is also used in the synthesis of certain polysaccharides, like bacterial cell wall components.

Defects in the metabolism or utilization of GDP-mannose can lead to various genetic disorders, such as congenital disorders of glycosylation (CDG), which can affect multiple organ systems and present with a wide range of clinical manifestations.

Glucose-6-phosphate (G6P) is a vital intermediate compound in the metabolism of glucose, which is a simple sugar that serves as a primary source of energy for living organisms. G6P plays a critical role in both glycolysis and gluconeogenesis pathways, contributing to the regulation of blood glucose levels and energy production within cells.

In biochemistry, glucose-6-phosphate is defined as:

A hexose sugar phosphate ester formed by the phosphorylation of glucose at the 6th carbon atom by ATP in a reaction catalyzed by the enzyme hexokinase or glucokinase. This reaction is the first step in both glycolysis and glucose storage (glycogen synthesis) processes, ensuring that glucose can be effectively utilized for energy production or stored for later use.

G6P serves as a crucial metabolic branch point, leading to various pathways such as:

1. Glycolysis: In the presence of sufficient ATP and NAD+ levels, G6P is further metabolized through glycolysis to generate pyruvate, which enters the citric acid cycle for additional energy production in the form of ATP, NADH, and FADH2.
2. Gluconeogenesis: During periods of low blood glucose levels, G6P can be synthesized back into glucose through the gluconeogenesis pathway, primarily occurring in the liver and kidneys. This process helps maintain stable blood glucose concentrations and provides energy to cells when dietary intake is insufficient.
3. Pentose phosphate pathway (PPP): A portion of G6P can be shunted into the PPP, an alternative metabolic route that generates NADPH, ribose-5-phosphate for nucleotide synthesis, and erythrose-4-phosphate for aromatic amino acid production. The PPP is essential in maintaining redox balance within cells and supporting biosynthetic processes.

Overall, glucose-6-phosphate plays a critical role as a central metabolic intermediate, connecting various pathways to regulate energy homeostasis, redox balance, and biosynthesis in response to cellular demands and environmental cues.

Calcium phosphates are a group of minerals that are important components of bones and teeth. They are also found in some foods and are used in dietary supplements and medical applications. Chemically, calcium phosphates are salts of calcium and phosphoric acid, and they exist in various forms, including hydroxyapatite, which is the primary mineral component of bone tissue. Other forms of calcium phosphates include monocalcium phosphate, dicalcium phosphate, and tricalcium phosphate, which are used as food additives and dietary supplements. Calcium phosphates are important for maintaining strong bones and teeth, and they also play a role in various physiological processes, such as nerve impulse transmission and muscle contraction.

Glycolates are a type of chemical compound that contain the group COOCH2, which is derived from glycolic acid. In a medical context, glycolates are often used in dental and medical materials as they can be biodegradable and biocompatible. For example, they may be used in controlled-release drug delivery systems or in bone cement. However, it's important to note that some glycolate compounds can also be toxic if ingested or otherwise introduced into the body in large amounts.

Sugar phosphates are organic compounds that play crucial roles in various biological processes, particularly in the field of genetics and molecular biology. They are formed by the attachment of a phosphate group to a sugar molecule, most commonly to the 5-carbon sugar ribose or deoxyribose.

In genetics, sugar phosphates form the backbone of nucleic acids, such as DNA and RNA. In DNA, the sugar phosphate backbone consists of alternating deoxyribose (a sugar) and phosphate groups, linked together by covalent bonds between the 5' carbon atom of one sugar molecule and the 3' carbon atom of another sugar molecule. This forms a long, twisted ladder-like structure known as a double helix.

Similarly, in RNA, the sugar phosphate backbone is formed by ribose (a sugar) and phosphate groups, creating a single-stranded structure that can fold back on itself to form complex shapes. These sugar phosphate backbones provide structural support for the nucleic acids and help to protect the genetic information stored within them.

Sugar phosphates also play important roles in energy metabolism, as they are involved in the formation and breakdown of high-energy compounds such as ATP (adenosine triphosphate) and GTP (guanosine triphosphate). These molecules serve as energy currency for cells, storing and releasing energy as needed to power various cellular processes.

Fructose-1,6-bisphosphate (also known as fructose 1,6-diphosphate or Fru-1,6-BP) is the chemical compound that plays a crucial role in cellular respiration and glucose metabolism. It is not accurate to refer to "fructosephosphates" as a medical term, but fructose-1-phosphate and fructose-1,6-bisphosphate are important fructose phosphates with specific functions in the body.

Fructose-1-phosphate is an intermediate metabolite formed during the breakdown of fructose in the liver, while fructose-1,6-bisphosphate is a key regulator of glycolysis, the process by which glucose is broken down to produce energy in the form of ATP. Fructose-1,6-bisphosphate allosterically regulates the enzyme phosphofructokinase, which is the rate-limiting step in glycolysis, and its levels are tightly controlled to maintain proper glucose metabolism. Dysregulation of fructose metabolism has been implicated in various metabolic disorders, including insulin resistance, type 2 diabetes, and nonalcoholic fatty liver disease (NAFLD).

Electrophoresis, starch gel is a type of electrophoretic technique used in laboratory settings for the separation and analysis of large biomolecules such as DNA, RNA, and proteins. In this method, a gel made from cooked starch is used as the supporting matrix for the molecules being separated.

The sample containing the mixture of biomolecules is loaded onto the gel and an electric field is applied, causing the negatively charged molecules to migrate towards the positive electrode. The starch gel acts as a molecular sieve, with smaller molecules moving more quickly through the gel than larger ones. This results in the separation of the mixture into individual components based on their size and charge.

Once the separation is complete, the gel can be stained to visualize the separated bands. Different staining techniques are used depending on the type of biomolecule being analyzed. For example, proteins can be stained with dyes such as Coomassie Brilliant Blue or silver nitrate, while nucleic acids can be stained with dyes such as ethidium bromide.

Starch gel electrophoresis is a relatively simple and inexpensive technique that has been widely used in molecular biology research and diagnostic applications. However, it has largely been replaced by other electrophoretic techniques, such as polyacrylamide gel electrophoresis (PAGE), which offer higher resolution and can be automated for high-throughput analysis.

Dolichol monophosphate mannose (Dol-P-Man) is a type of glycosyl donor that plays a crucial role in the process of protein glycosylation within the endoplasmic reticulum (ER) of eukaryotic cells. Protein glycosylation is the enzymatic attachment of oligosaccharide chains to proteins, which can significantly affect their structure, stability, and function.

Dolichol monophosphate mannose consists of a dolichol molecule, a long-chain polyisoprenoid alcohol, linked to a mannose sugar via a phosphate group. The dolichol component serves as a lipid anchor, allowing Dol-P-Man to participate in the synthesis of oligosaccharides on the cytoplasmic side of the ER membrane.

In the first step of the process, mannose is transferred from a donor molecule, guanosine diphosphate mannose (GDP-Man), to dolichol phosphate (Dol-P) by the enzyme alpha-1,2-mannosyltransferase. This reaction forms Dol-P-Man, which then serves as a substrate for further glycosylation reactions in the ER lumen.

In summary, Dolichol monophosphate mannose is an essential intermediate in the biosynthesis of N-linked oligosaccharides, contributing to the proper folding and functioning of proteins within eukaryotic cells.

'Escherichia coli' (E. coli) is a type of gram-negative, facultatively anaerobic, rod-shaped bacterium that commonly inhabits the intestinal tract of humans and warm-blooded animals. It is a member of the family Enterobacteriaceae and one of the most well-studied prokaryotic model organisms in molecular biology.

While most E. coli strains are harmless and even beneficial to their hosts, some serotypes can cause various forms of gastrointestinal and extraintestinal illnesses in humans and animals. These pathogenic strains possess virulence factors that enable them to colonize and damage host tissues, leading to diseases such as diarrhea, urinary tract infections, pneumonia, and sepsis.

E. coli is a versatile organism with remarkable genetic diversity, which allows it to adapt to various environmental niches. It can be found in water, soil, food, and various man-made environments, making it an essential indicator of fecal contamination and a common cause of foodborne illnesses. The study of E. coli has contributed significantly to our understanding of fundamental biological processes, including DNA replication, gene regulation, and protein synthesis.

X-ray crystallography is a technique used in structural biology to determine the three-dimensional arrangement of atoms in a crystal lattice. In this method, a beam of X-rays is directed at a crystal and diffracts, or spreads out, into a pattern of spots called reflections. The intensity and angle of each reflection are measured and used to create an electron density map, which reveals the position and type of atoms in the crystal. This information can be used to determine the molecular structure of a compound, including its shape, size, and chemical bonds. X-ray crystallography is a powerful tool for understanding the structure and function of biological macromolecules such as proteins and nucleic acids.

Hexokinase is an enzyme that plays a crucial role in the initial step of glucose metabolism, which is the phosphorylation of glucose to form glucose-6-phosphate. This reaction is the first step in most glucose catabolic pathways, including glycolysis, pentose phosphate pathway, and glycogen synthesis.

Hexokinase has a high affinity for glucose, meaning it can bind and phosphorylate glucose even at low concentrations. This property makes hexokinase an important regulator of glucose metabolism in cells. There are four isoforms of hexokinase (I-IV) found in different tissues, with hexokinase IV (also known as glucokinase) being primarily expressed in the liver and pancreas.

In summary, hexokinase is a vital enzyme involved in glucose metabolism, catalyzing the conversion of glucose to glucose-6-phosphate, and playing a crucial role in regulating cellular energy homeostasis.

Organophosphorus compounds are a class of chemical substances that contain phosphorus bonded to organic compounds. They are used in various applications, including as plasticizers, flame retardants, pesticides (insecticides, herbicides, and nerve gases), and solvents. In medicine, they are also used in the treatment of certain conditions such as glaucoma. However, organophosphorus compounds can be toxic to humans and animals, particularly those that affect the nervous system by inhibiting acetylcholinesterase, an enzyme that breaks down the neurotransmitter acetylcholine. Exposure to these compounds can cause symptoms such as nausea, vomiting, muscle weakness, and in severe cases, respiratory failure and death.

Molecular cloning is a laboratory technique used to create multiple copies of a specific DNA sequence. This process involves several steps:

1. Isolation: The first step in molecular cloning is to isolate the DNA sequence of interest from the rest of the genomic DNA. This can be done using various methods such as PCR (polymerase chain reaction), restriction enzymes, or hybridization.
2. Vector construction: Once the DNA sequence of interest has been isolated, it must be inserted into a vector, which is a small circular DNA molecule that can replicate independently in a host cell. Common vectors used in molecular cloning include plasmids and phages.
3. Transformation: The constructed vector is then introduced into a host cell, usually a bacterial or yeast cell, through a process called transformation. This can be done using various methods such as electroporation or chemical transformation.
4. Selection: After transformation, the host cells are grown in selective media that allow only those cells containing the vector to grow. This ensures that the DNA sequence of interest has been successfully cloned into the vector.
5. Amplification: Once the host cells have been selected, they can be grown in large quantities to amplify the number of copies of the cloned DNA sequence.

Molecular cloning is a powerful tool in molecular biology and has numerous applications, including the production of recombinant proteins, gene therapy, functional analysis of genes, and genetic engineering.

Paper chromatography is a type of chromatography technique that involves the separation and analysis of mixtures based on their components' ability to migrate differently upon capillary action on a paper medium. This simple and cost-effective method utilizes a paper, typically made of cellulose, as the stationary phase. The sample mixture is applied as a small spot near one end of the paper, and then the other end is dipped into a developing solvent or a mixture of solvents (mobile phase) in a shallow container.

As the mobile phase moves up the paper by capillary action, components within the sample mixture separate based on their partition coefficients between the stationary and mobile phases. The partition coefficient describes how much a component prefers to be in either the stationary or mobile phase. Components with higher partition coefficients in the mobile phase will move faster and further than those with lower partition coefficients.

Once separation is complete, the paper is dried and can be visualized under ultraviolet light or by using chemical reagents specific for the components of interest. The distance each component travels from the origin (point of application) and its corresponding solvent front position are measured, allowing for the calculation of Rf values (retardation factors). Rf is a dimensionless quantity calculated as the ratio of the distance traveled by the component to the distance traveled by the solvent front.

Rf = (distance traveled by component) / (distance traveled by solvent front)

Paper chromatography has been widely used in various applications, such as:

1. Identification and purity analysis of chemical compounds in pharmaceuticals, forensics, and research laboratories.
2. Separation and detection of amino acids, sugars, and other biomolecules in biological samples.
3. Educational purposes to demonstrate the principles of chromatography and separation techniques.

Despite its limitations, such as lower resolution compared to high-performance liquid chromatography (HPLC) and less compatibility with volatile or nonpolar compounds, paper chromatography remains a valuable tool for quick, qualitative analysis in various fields.

Hydrogen-ion concentration, also known as pH, is a measure of the acidity or basicity of a solution. It is defined as the negative logarithm (to the base 10) of the hydrogen ion activity in a solution. The standard unit of measurement is the pH unit. A pH of 7 is neutral, less than 7 is acidic, and greater than 7 is basic.

In medical terms, hydrogen-ion concentration is important for maintaining homeostasis within the body. For example, in the stomach, a high hydrogen-ion concentration (low pH) is necessary for the digestion of food. However, in other parts of the body such as blood, a high hydrogen-ion concentration can be harmful and lead to acidosis. Conversely, a low hydrogen-ion concentration (high pH) in the blood can lead to alkalosis. Both acidosis and alkalosis can have serious consequences on various organ systems if not corrected.

Optical rotation, also known as optical activity, is a property of certain substances to rotate the plane of polarization of linearly polarized light as it passes through the substance. This ability arises from the presence of optically active molecules, most commonly chiral molecules, which have a non-superimposable mirror image.

The angle and direction of rotation (either clockwise or counterclockwise) are specific to each optically active substance and can be used as a characteristic identification property. The measurement of optical rotation is an important tool in the determination of the enantiomeric purity of chiral compounds, such as drugs and natural products, in chemistry and pharmacology.

The optical rotation of a substance can be influenced by factors such as temperature, concentration, wavelength of light, and solvent used. The magnitude of the optical rotation is often reported as the specific rotation, which is the optical rotation per unit length (usually expressed in degrees) and per unit concentration (often given in grams per deciliter or g/dL).

Glyceraldehyde 3-phosphate (G3P) is a crucial intermediate in both glycolysis and gluconeogenesis metabolic pathways. It is an triose sugar phosphate, which means it contains three carbon atoms and has a phosphate group attached to it.

In the glycolysis process, G3P is produced during the third step of the process from the molecule dihydroxyacetone phosphate (DHAP) via the enzyme triosephosphate isomerase. In the following steps, G3P is converted into 1,3-bisphosphoglycerate, which eventually leads to the production of ATP and NADH.

In gluconeogenesis, G3P is produced from the reverse reaction of the glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase, using the molecule dihydroxyacetone phosphate (DHAP) as a starting point. G3P is then converted into glucose-6-phosphate, which can be further metabolized or released from the cell.

It's important to note that Glyceraldehyde 3-Phosphate plays a key role in energy production and carbohydrate metabolism.

In the context of medical and biological sciences, a "binding site" refers to a specific location on a protein, molecule, or cell where another molecule can attach or bind. This binding interaction can lead to various functional changes in the original protein or molecule. The other molecule that binds to the binding site is often referred to as a ligand, which can be a small molecule, ion, or even another protein.

The binding between a ligand and its target binding site can be specific and selective, meaning that only certain ligands can bind to particular binding sites with high affinity. This specificity plays a crucial role in various biological processes, such as signal transduction, enzyme catalysis, or drug action.

In the case of drug development, understanding the location and properties of binding sites on target proteins is essential for designing drugs that can selectively bind to these sites and modulate protein function. This knowledge can help create more effective and safer therapeutic options for various diseases.

"Giardia lamblia," also known as "Giardia duodenalis" or "Giardia intestinalis," is a species of microscopic parasitic protozoan that colonizes and reproduces in the small intestine of various vertebrates, including humans. It is the most common cause of human giardiasis, a diarrheal disease. The trophozoite (feeding form) of Giardia lamblia has a distinctive tear-drop shape and possesses flagella for locomotion. It attaches to the intestinal epithelium, disrupting the normal function of the small intestine and leading to various gastrointestinal symptoms such as diarrhea, stomach cramps, nausea, and dehydration. Giardia lamblia is typically transmitted through the fecal-oral route, often via contaminated food or water.

Substrate specificity in the context of medical biochemistry and enzymology refers to the ability of an enzyme to selectively bind and catalyze a chemical reaction with a particular substrate (or a group of similar substrates) while discriminating against other molecules that are not substrates. This specificity arises from the three-dimensional structure of the enzyme, which has evolved to match the shape, charge distribution, and functional groups of its physiological substrate(s).

Substrate specificity is a fundamental property of enzymes that enables them to carry out highly selective chemical transformations in the complex cellular environment. The active site of an enzyme, where the catalysis takes place, has a unique conformation that complements the shape and charge distribution of its substrate(s). This ensures efficient recognition, binding, and conversion of the substrate into the desired product while minimizing unwanted side reactions with other molecules.

Substrate specificity can be categorized as:

1. Absolute specificity: An enzyme that can only act on a single substrate or a very narrow group of structurally related substrates, showing no activity towards any other molecule.
2. Group specificity: An enzyme that prefers to act on a particular functional group or class of compounds but can still accommodate minor structural variations within the substrate.
3. Broad or promiscuous specificity: An enzyme that can act on a wide range of structurally diverse substrates, albeit with varying catalytic efficiencies.

Understanding substrate specificity is crucial for elucidating enzymatic mechanisms, designing drugs that target specific enzymes or pathways, and developing biotechnological applications that rely on the controlled manipulation of enzyme activities.

Electrophoresis, cellulose acetate is a laboratory technique used to separate and analyze proteins or other charged molecules based on their size and charge. The sample is applied to a sheet of cellulose acetate, a type of porous plastic film, and an electric field is applied. The proteins migrate through the film towards the electrode with the opposite charge, with smaller and more negatively charged molecules moving faster than larger and less negatively charged ones. This allows for the separation and identification of different protein components in a mixture. It is a simple and rapid method for routine protein separations and is commonly used in biochemistry and molecular biology research.

Phosphoric acids are a group of mineral acids known chemically as orthophosphoric acid and its salts or esters. The chemical formula for orthophosphoric acid is H3PO4. It is a weak acid that partially dissociates in solution to release hydrogen ions (H+), making it acidic. Phosphoric acid has many uses in various industries, including food additives, fertilizers, and detergents.

In the context of medical definitions, phosphoric acids are not typically referred to directly. However, they can be relevant in certain medical contexts, such as:

* In dentistry, phosphoric acid is used as an etching agent to prepare tooth enamel for bonding with dental materials.
* In nutrition, phosphorus is an essential mineral that plays a crucial role in many bodily functions, including energy metabolism, bone and teeth formation, and nerve function. Phosphoric acid is one form of phosphorus found in some foods and beverages.
* In medical research, phosphoric acids can be used as buffers to maintain a stable pH in laboratory experiments or as reagents in various analytical techniques.

Molecular models are three-dimensional representations of molecular structures that are used in the field of molecular biology and chemistry to visualize and understand the spatial arrangement of atoms and bonds within a molecule. These models can be physical or computer-generated and allow researchers to study the shape, size, and behavior of molecules, which is crucial for understanding their function and interactions with other molecules.

Physical molecular models are often made up of balls (representing atoms) connected by rods or sticks (representing bonds). These models can be constructed manually using materials such as plastic or wooden balls and rods, or they can be created using 3D printing technology.

Computer-generated molecular models, on the other hand, are created using specialized software that allows researchers to visualize and manipulate molecular structures in three dimensions. These models can be used to simulate molecular interactions, predict molecular behavior, and design new drugs or chemicals with specific properties. Overall, molecular models play a critical role in advancing our understanding of molecular structures and their functions.

Hemolytic anemia is a type of anemia that occurs when red blood cells are destroyed (hemolysis) faster than they can be produced. Red blood cells are essential for carrying oxygen throughout the body. When they are destroyed, hemoglobin and other cellular components are released into the bloodstream, which can lead to complications such as kidney damage and gallstones.

Hemolytic anemia can be inherited or acquired. Inherited forms of the condition may result from genetic defects that affect the structure or function of red blood cells. Acquired forms of hemolytic anemia can be caused by various factors, including infections, medications, autoimmune disorders, and certain medical conditions such as cancer or blood disorders.

Symptoms of hemolytic anemia may include fatigue, weakness, shortness of breath, pale skin, jaundice (yellowing of the skin and eyes), dark urine, and a rapid heartbeat. Treatment for hemolytic anemia depends on the underlying cause and may include medications, blood transfusions, or surgery.

Isoenzymes, also known as isoforms, are multiple forms of an enzyme that catalyze the same chemical reaction but differ in their amino acid sequence, structure, and/or kinetic properties. They are encoded by different genes or alternative splicing of the same gene. Isoenzymes can be found in various tissues and organs, and they play a crucial role in biological processes such as metabolism, detoxification, and cell signaling. Measurement of isoenzyme levels in body fluids (such as blood) can provide valuable diagnostic information for certain medical conditions, including tissue damage, inflammation, and various diseases.

A base sequence in the context of molecular biology refers to the specific order of nucleotides in a DNA or RNA molecule. In DNA, these nucleotides are adenine (A), guanine (G), cytosine (C), and thymine (T). In RNA, uracil (U) takes the place of thymine. The base sequence contains genetic information that is transcribed into RNA and ultimately translated into proteins. It is the exact order of these bases that determines the genetic code and thus the function of the DNA or RNA molecule.

Inositol phosphates are a family of molecules that consist of an inositol ring, which is a six-carbon heterocyclic compound, linked to one or more phosphate groups. These molecules play important roles as intracellular signaling intermediates and are involved in various cellular processes such as cell growth, differentiation, and metabolism.

Inositol hexakisphosphate (IP6), also known as phytic acid, is a form of inositol phosphate that is found in plant-based foods. IP6 has the ability to bind to minerals such as calcium, magnesium, and iron, which can reduce their bioavailability in the body.

Inositol phosphates have been implicated in several diseases, including cancer, diabetes, and neurodegenerative disorders. For example, altered levels of certain inositol phosphates have been observed in cancer cells, suggesting that they may play a role in tumor growth and progression. Additionally, mutations in enzymes involved in the metabolism of inositol phosphates have been associated with several genetic diseases.

Recombinant proteins are artificially created proteins produced through the use of recombinant DNA technology. This process involves combining DNA molecules from different sources to create a new set of genes that encode for a specific protein. The resulting recombinant protein can then be expressed, purified, and used for various applications in research, medicine, and industry.

Recombinant proteins are widely used in biomedical research to study protein function, structure, and interactions. They are also used in the development of diagnostic tests, vaccines, and therapeutic drugs. For example, recombinant insulin is a common treatment for diabetes, while recombinant human growth hormone is used to treat growth disorders.

The production of recombinant proteins typically involves the use of host cells, such as bacteria, yeast, or mammalian cells, which are engineered to express the desired protein. The host cells are transformed with a plasmid vector containing the gene of interest, along with regulatory elements that control its expression. Once the host cells are cultured and the protein is expressed, it can be purified using various chromatography techniques.

Overall, recombinant proteins have revolutionized many areas of biology and medicine, enabling researchers to study and manipulate proteins in ways that were previously impossible.

Progesterone reductase is not a widely recognized or used term in medical literature. However, based on the terms "progesterone" and "reductase," it can be inferred that progesterone reductase might refer to an enzyme responsible for reducing or converting progesterone into another form through a reduction reaction.

Progesterone is a steroid hormone involved in the menstrual cycle, pregnancy, and embryogenesis. Reductases are enzymes that catalyze the transfer of electrons from a donor to an acceptor, often resulting in the reduction of a substrate. In this context, progesterone reductase could potentially refer to an enzyme responsible for reducing progesterone into a different steroid hormone or metabolite.

However, it is essential to note that there is no widely accepted or established definition of "progesterone reductase" in medical literature. If you are looking for information on a specific enzyme related to progesterone metabolism, I would recommend consulting primary scientific literature or seeking guidance from a medical professional.

Glucose is a simple monosaccharide (or single sugar) that serves as the primary source of energy for living organisms. It's a fundamental molecule in biology, often referred to as "dextrose" or "grape sugar." Glucose has the molecular formula C6H12O6 and is vital to the functioning of cells, especially those in the brain and nervous system.

In the body, glucose is derived from the digestion of carbohydrates in food, and it's transported around the body via the bloodstream to cells where it can be used for energy. Cells convert glucose into a usable form through a process called cellular respiration, which involves a series of metabolic reactions that generate adenosine triphosphate (ATP)—the main currency of energy in cells.

Glucose is also stored in the liver and muscles as glycogen, a polysaccharide (multiple sugar) that can be broken down back into glucose when needed for energy between meals or during physical activity. Maintaining appropriate blood glucose levels is crucial for overall health, and imbalances can lead to conditions such as diabetes mellitus.

A mutation is a permanent change in the DNA sequence of an organism's genome. Mutations can occur spontaneously or be caused by environmental factors such as exposure to radiation, chemicals, or viruses. They may have various effects on the organism, ranging from benign to harmful, depending on where they occur and whether they alter the function of essential proteins. In some cases, mutations can increase an individual's susceptibility to certain diseases or disorders, while in others, they may confer a survival advantage. Mutations are the driving force behind evolution, as they introduce new genetic variability into populations, which can then be acted upon by natural selection.

Enzyme stability refers to the ability of an enzyme to maintain its structure and function under various environmental conditions, such as temperature, pH, and the presence of denaturants or inhibitors. A stable enzyme retains its activity and conformation over time and across a range of conditions, making it more suitable for industrial and therapeutic applications.

Enzymes can be stabilized through various methods, including chemical modification, immobilization, and protein engineering. Understanding the factors that affect enzyme stability is crucial for optimizing their use in biotechnology, medicine, and research.

Sequence homology, amino acid, refers to the similarity in the order of amino acids in a protein or a portion of a protein between two or more species. This similarity can be used to infer evolutionary relationships and functional similarities between proteins. The higher the degree of sequence homology, the more likely it is that the proteins are related and have similar functions. Sequence homology can be determined through various methods such as pairwise alignment or multiple sequence alignment, which compare the sequences and calculate a score based on the number and type of matching amino acids.

Thermolysin is not a medical term per se, but it is a bacterial enzyme that is often used in biochemistry and molecular biology research. Here's the scientific or biochemical definition:

Thermolysin is a zinc metalloprotease enzyme produced by the bacteria Geobacillus stearothermophilus. It has an optimum temperature for activity at around 65°C, and it can remain active in high temperatures, which makes it useful in various industrial applications. Thermolysin is known for its ability to cleave peptide bonds, particularly those involving hydrophobic residues, making it a valuable tool in protein research and engineering.

A chimera, in the context of medicine and biology, is a single organism that is composed of cells with different genetics. This can occur naturally in some situations, such as when fraternal twins do not fully separate in utero and end up sharing some organs or tissues. The term "chimera" can also refer to an organism that contains cells from two different species, which can happen in certain types of genetic research or medical treatments. For example, a patient's cells might be genetically modified in a lab and then introduced into their body to treat a disease; if some of these modified cells mix with the patient's original cells, the result could be a chimera.

It's worth noting that the term "chimera" comes from Greek mythology, where it referred to a fire-breathing monster that was part lion, part goat, and part snake. In modern scientific usage, the term has a specific technical meaning related to genetics and organisms, but it may still evoke images of fantastical creatures for some people.

Oligosaccharides are complex carbohydrates composed of relatively small numbers (3-10) of monosaccharide units joined together by glycosidic linkages. They occur naturally in foods such as milk, fruits, vegetables, and legumes. In the body, oligosaccharides play important roles in various biological processes, including cell recognition, signaling, and protection against pathogens.

There are several types of oligosaccharides, classified based on their structures and functions. Some common examples include:

1. Disaccharides: These consist of two monosaccharide units, such as sucrose (glucose + fructose), lactose (glucose + galactose), and maltose (glucose + glucose).
2. Trisaccharides: These contain three monosaccharide units, like maltotriose (glucose + glucose + glucose) and raffinose (galactose + glucose + fructose).
3. Oligosaccharides found in human milk: Human milk contains unique oligosaccharides that serve as prebiotics, promoting the growth of beneficial bacteria in the gut. These oligosaccharides also help protect infants from pathogens by acting as decoy receptors and inhibiting bacterial adhesion to intestinal cells.
4. N-linked and O-linked glycans: These are oligosaccharides attached to proteins in the body, playing crucial roles in protein folding, stability, and function.
5. Plant-derived oligosaccharides: Fructooligosaccharides (FOS) and galactooligosaccharides (GOS) are examples of plant-derived oligosaccharides that serve as prebiotics, promoting the growth of beneficial gut bacteria.

Overall, oligosaccharides have significant impacts on human health and disease, particularly in relation to gastrointestinal function, immunity, and inflammation.

Protein conformation refers to the specific three-dimensional shape that a protein molecule assumes due to the spatial arrangement of its constituent amino acid residues and their associated chemical groups. This complex structure is determined by several factors, including covalent bonds (disulfide bridges), hydrogen bonds, van der Waals forces, and ionic bonds, which help stabilize the protein's unique conformation.

Protein conformations can be broadly classified into two categories: primary, secondary, tertiary, and quaternary structures. The primary structure represents the linear sequence of amino acids in a polypeptide chain. The secondary structure arises from local interactions between adjacent amino acid residues, leading to the formation of recurring motifs such as α-helices and β-sheets. Tertiary structure refers to the overall three-dimensional folding pattern of a single polypeptide chain, while quaternary structure describes the spatial arrangement of multiple folded polypeptide chains (subunits) that interact to form a functional protein complex.

Understanding protein conformation is crucial for elucidating protein function, as the specific three-dimensional shape of a protein directly influences its ability to interact with other molecules, such as ligands, nucleic acids, or other proteins. Any alterations in protein conformation due to genetic mutations, environmental factors, or chemical modifications can lead to loss of function, misfolding, aggregation, and disease states like neurodegenerative disorders and cancer.

I believe there may be some confusion in your question. "Rabbits" is a common name used to refer to the Lagomorpha species, particularly members of the family Leporidae. They are small mammals known for their long ears, strong legs, and quick reproduction.

However, if you're referring to "rabbits" in a medical context, there is a term called "rabbit syndrome," which is a rare movement disorder characterized by repetitive, involuntary movements of the fingers, resembling those of a rabbit chewing. It is also known as "finger-chewing chorea." This condition is usually associated with certain medications, particularly antipsychotics, and typically resolves when the medication is stopped or adjusted.

"Chickens" is a common term used to refer to the domesticated bird, Gallus gallus domesticus, which is widely raised for its eggs and meat. However, in medical terms, "chickens" is not a standard term with a specific definition. If you have any specific medical concern or question related to chickens, such as food safety or allergies, please provide more details so I can give a more accurate answer.

A catalytic domain is a portion or region within a protein that contains the active site, where the chemical reactions necessary for the protein's function are carried out. This domain is responsible for the catalysis of biological reactions, hence the name "catalytic domain." The catalytic domain is often composed of specific amino acid residues that come together to form the active site, creating a unique three-dimensional structure that enables the protein to perform its specific function.

In enzymes, for example, the catalytic domain contains the residues that bind and convert substrates into products through chemical reactions. In receptors, the catalytic domain may be involved in signal transduction or other regulatory functions. Understanding the structure and function of catalytic domains is crucial to understanding the mechanisms of protein function and can provide valuable insights for drug design and therapeutic interventions.

Phosphopyruvate Hydratase is an enzyme also known as Enolase. It plays a crucial role in the glycolytic pathway, which is a series of reactions that occur in the cell to break down glucose into pyruvate, producing ATP and NADH as energy-rich intermediates.

Specifically, Phosphopyruvate Hydratase catalyzes the conversion of 2-phospho-D-glycerate (2-PG) to phosphoenolpyruvate (PEP), which is the second to last step in the glycolytic pathway. This reaction includes the removal of a water molecule from 2-PG, resulting in the formation of PEP and the release of a molecule of water.

The enzyme requires magnesium ions as a cofactor for its activity, and it is inhibited by fluoride ions. Deficiency or dysfunction of Phosphopyruvate Hydratase can lead to various metabolic disorders, including some forms of muscular dystrophy and neurodegenerative diseases.

Electrophoresis, polyacrylamide gel (EPG) is a laboratory technique used to separate and analyze complex mixtures of proteins or nucleic acids (DNA or RNA) based on their size and electrical charge. This technique utilizes a matrix made of cross-linked polyacrylamide, a type of gel, which provides a stable and uniform environment for the separation of molecules.

In this process:

1. The polyacrylamide gel is prepared by mixing acrylamide monomers with a cross-linking agent (bis-acrylamide) and a catalyst (ammonium persulfate) in the presence of a buffer solution.
2. The gel is then poured into a mold and allowed to polymerize, forming a solid matrix with uniform pore sizes that depend on the concentration of acrylamide used. Higher concentrations result in smaller pores, providing better resolution for separating smaller molecules.
3. Once the gel has set, it is placed in an electrophoresis apparatus containing a buffer solution. Samples containing the mixture of proteins or nucleic acids are loaded into wells on the top of the gel.
4. An electric field is applied across the gel, causing the negatively charged molecules to migrate towards the positive electrode (anode) while positively charged molecules move toward the negative electrode (cathode). The rate of migration depends on the size, charge, and shape of the molecules.
5. Smaller molecules move faster through the gel matrix and will migrate farther from the origin compared to larger molecules, resulting in separation based on size. Proteins and nucleic acids can be selectively stained after electrophoresis to visualize the separated bands.

EPG is widely used in various research fields, including molecular biology, genetics, proteomics, and forensic science, for applications such as protein characterization, DNA fragment analysis, cloning, mutation detection, and quality control of nucleic acid or protein samples.

Pyruvate kinase is an enzyme that plays a crucial role in the final step of glycolysis, a process by which glucose is broken down to produce energy in the form of ATP (adenosine triphosphate). Specifically, pyruvate kinase catalyzes the transfer of a phosphate group from phosphoenolpyruvate (PEP) to adenosine diphosphate (ADP), resulting in the formation of pyruvate and ATP.

There are several isoforms of pyruvate kinase found in different tissues, including the liver, muscle, and brain. The type found in red blood cells is known as PK-RBC or PK-M2. Deficiencies in pyruvate kinase can lead to a genetic disorder called pyruvate kinase deficiency, which can result in hemolytic anemia due to the premature destruction of red blood cells.

Quaternary protein structure refers to the arrangement and interaction of multiple folded protein molecules in a multi-subunit complex. These subunits can be identical or different forms of the same protein or distinctly different proteins that associate to form a functional complex. The quaternary structure is held together by non-covalent interactions, such as hydrogen bonds, ionic bonds, and van der Waals forces. Understanding quaternary structure is crucial for comprehending the function, regulation, and assembly of many protein complexes involved in various cellular processes.

In genetics, sequence alignment is the process of arranging two or more DNA, RNA, or protein sequences to identify regions of similarity or homology between them. This is often done using computational methods to compare the nucleotide or amino acid sequences and identify matching patterns, which can provide insight into evolutionary relationships, functional domains, or potential genetic disorders. The alignment process typically involves adjusting gaps and mismatches in the sequences to maximize the similarity between them, resulting in an aligned sequence that can be visually represented and analyzed.

Glycerol, also known as glycerine or glycerin, is a simple polyol (a sugar alcohol) with a sweet taste and a thick, syrupy consistency. It is a colorless, odorless, viscous liquid that is slightly soluble in water and freely miscible with ethanol and ether.

In the medical field, glycerol is often used as a medication or supplement. It can be used as a laxative to treat constipation, as a source of calories and energy for people who cannot eat by mouth, and as a way to prevent dehydration in people with certain medical conditions.

Glycerol is also used in the production of various medical products, such as medications, skin care products, and vaccines. It acts as a humectant, which means it helps to keep things moist, and it can also be used as a solvent or preservative.

In addition to its medical uses, glycerol is also widely used in the food industry as a sweetener, thickening agent, and moisture-retaining agent. It is generally recognized as safe (GRAS) by the U.S. Food and Drug Administration (FDA).

Mannosyltransferases are a group of enzymes that catalyze the transfer of mannose (a type of sugar) to specific acceptor molecules during the process of glycosylation. Glycosylation is the attachment of carbohydrate groups, or glycans, to proteins and lipids, which plays a crucial role in various biological processes such as protein folding, quality control, trafficking, and cell-cell recognition.

In particular, mannosyltransferases are involved in the addition of mannose residues to the core oligosaccharide structure of N-linked glycans in the endoplasmic reticulum (ER) and Golgi apparatus of eukaryotic cells. These enzymes use a donor substrate, typically dolichol-phosphate-mannose (DPM), to add mannose molecules to the acceptor substrate, which is an asparagine residue within a growing glycan chain.

There are several classes of mannosyltransferases, each responsible for adding mannose to specific positions within the glycan structure. Defects in these enzymes can lead to various genetic disorders known as congenital disorders of glycosylation (CDG), which can affect multiple organ systems and result in a wide range of clinical manifestations.

A chemical model is a simplified representation or description of a chemical system, based on the laws of chemistry and physics. It is used to explain and predict the behavior of chemicals and chemical reactions. Chemical models can take many forms, including mathematical equations, diagrams, and computer simulations. They are often used in research, education, and industry to understand complex chemical processes and develop new products and technologies.

For example, a chemical model might be used to describe the way that atoms and molecules interact in a particular reaction, or to predict the properties of a new material. Chemical models can also be used to study the behavior of chemicals at the molecular level, such as how they bind to each other or how they are affected by changes in temperature or pressure.

It is important to note that chemical models are simplifications of reality and may not always accurately represent every aspect of a chemical system. They should be used with caution and validated against experimental data whenever possible.

Bacterial proteins are a type of protein that are produced by bacteria as part of their structural or functional components. These proteins can be involved in various cellular processes, such as metabolism, DNA replication, transcription, and translation. They can also play a role in bacterial pathogenesis, helping the bacteria to evade the host's immune system, acquire nutrients, and multiply within the host.

Bacterial proteins can be classified into different categories based on their function, such as:

1. Enzymes: Proteins that catalyze chemical reactions in the bacterial cell.
2. Structural proteins: Proteins that provide structural support and maintain the shape of the bacterial cell.
3. Signaling proteins: Proteins that help bacteria to communicate with each other and coordinate their behavior.
4. Transport proteins: Proteins that facilitate the movement of molecules across the bacterial cell membrane.
5. Toxins: Proteins that are produced by pathogenic bacteria to damage host cells and promote infection.
6. Surface proteins: Proteins that are located on the surface of the bacterial cell and interact with the environment or host cells.

Understanding the structure and function of bacterial proteins is important for developing new antibiotics, vaccines, and other therapeutic strategies to combat bacterial infections.

Polyisoprenyl phosphate sugars are a type of glycosylated lipid that plays a crucial role in the biosynthesis of isoprenoid-derived natural products, including sterols and dolichols. These molecules consist of a polyisoprenyl phosphate group linked to one or more sugar moieties, such as glucose, mannose, or fructose. They serve as essential intermediates in the biosynthetic pathways that produce various isoprenoid-derived compounds, which have diverse functions in cellular metabolism and homeostasis.

The polyisoprenyl phosphate group is synthesized from isopentenyl pyrophosphate (IPP) and dimethylallyl pyrophosphate (DMAPP), the building blocks of isoprenoid biosynthesis, through a series of enzymatic reactions. The sugar moiety is then transferred to the polyisoprenyl phosphate group by specific glycosyltransferases, resulting in the formation of polyisoprenyl phosphate sugars.

These molecules are involved in various cellular processes, such as protein prenylation, where they serve as lipid anchors that facilitate the attachment of isoprenoid groups to proteins, thereby modulating their localization, stability, and activity. Additionally, polyisoprenyl phosphate sugars participate in the biosynthesis of bacterial cell wall components, such as peptidoglycan and lipopolysaccharides, highlighting their importance in both eukaryotic and prokaryotic organisms.

In summary, polyisoprenyl phosphate sugars are a class of glycosylated lipids that play a critical role in isoprenoid biosynthesis and related cellular processes, including protein prenylation and bacterial cell wall synthesis.

Crystallization is a process in which a substance transitions from a liquid or dissolved state to a solid state, forming a crystal lattice. In the medical context, crystallization can refer to the formation of crystals within the body, which can occur under certain conditions such as changes in pH, temperature, or concentration of solutes. These crystals can deposit in various tissues and organs, leading to the formation of crystal-induced diseases or disorders.

For example, in patients with gout, uric acid crystals can accumulate in joints, causing inflammation, pain, and swelling. Similarly, in nephrolithiasis (kidney stones), minerals in the urine can crystallize and form stones that can obstruct the urinary tract. Crystallization can also occur in other medical contexts, such as in the formation of dental calculus or plaque, and in the development of cataracts in the eye.

Glucose phosphates are organic compounds that result from the reaction of glucose (a simple sugar) with phosphate groups. These compounds play a crucial role in various metabolic processes, particularly in energy metabolism within cells. The addition of phosphate groups to glucose makes it more reactive and enables it to undergo further reactions that lead to the formation of important molecules such as adenosine triphosphate (ATP), which is a primary source of energy for cellular functions.

One notable example of a glucose phosphate is glucose 1-phosphate, which is an intermediate in several metabolic pathways, including glycogenesis (the process of forming glycogen, a storage form of glucose) and glycolysis (the breakdown of glucose to release energy). Another example is glucose 6-phosphate, which is a key regulator of carbohydrate metabolism and serves as an important intermediate in the pentose phosphate pathway, a metabolic route that generates reducing equivalents (NADPH) and ribose sugars for nucleotide synthesis.

In summary, glucose phosphates are essential compounds in cellular metabolism, facilitating energy production, storage, and utilization.

'Escherichia coli (E. coli) proteins' refer to the various types of proteins that are produced and expressed by the bacterium Escherichia coli. These proteins play a critical role in the growth, development, and survival of the organism. They are involved in various cellular processes such as metabolism, DNA replication, transcription, translation, repair, and regulation.

E. coli is a gram-negative, facultative anaerobe that is commonly found in the intestines of warm-blooded organisms. It is widely used as a model organism in scientific research due to its well-studied genetics, rapid growth, and ability to be easily manipulated in the laboratory. As a result, many E. coli proteins have been identified, characterized, and studied in great detail.

Some examples of E. coli proteins include enzymes involved in carbohydrate metabolism such as lactase, sucrase, and maltose; proteins involved in DNA replication such as the polymerases, single-stranded binding proteins, and helicases; proteins involved in transcription such as RNA polymerase and sigma factors; proteins involved in translation such as ribosomal proteins, tRNAs, and aminoacyl-tRNA synthetases; and regulatory proteins such as global regulators, two-component systems, and transcription factors.

Understanding the structure, function, and regulation of E. coli proteins is essential for understanding the basic biology of this important organism, as well as for developing new strategies for combating bacterial infections and improving industrial processes involving bacteria.

Temperature, in a medical context, is a measure of the degree of hotness or coldness of a body or environment. It is usually measured using a thermometer and reported in degrees Celsius (°C), degrees Fahrenheit (°F), or kelvin (K). In the human body, normal core temperature ranges from about 36.5-37.5°C (97.7-99.5°F) when measured rectally, and can vary slightly depending on factors such as time of day, physical activity, and menstrual cycle. Elevated body temperature is a common sign of infection or inflammation, while abnormally low body temperature can indicate hypothermia or other medical conditions.

C-type lectins are a family of proteins that contain one or more carbohydrate recognition domains (CRDs) with a characteristic pattern of conserved sequence motifs. These proteins are capable of binding to specific carbohydrate structures in a calcium-dependent manner, making them important in various biological processes such as cell adhesion, immune recognition, and initiation of inflammatory responses.

C-type lectins can be further classified into several subfamilies based on their structure and function, including selectins, collectins, and immunoglobulin-like receptors. They play a crucial role in the immune system by recognizing and binding to carbohydrate structures on the surface of pathogens, facilitating their clearance by phagocytic cells. Additionally, C-type lectins are involved in various physiological processes such as cell development, tissue repair, and cancer progression.

It is important to note that some C-type lectins can also bind to self-antigens and contribute to autoimmune diseases. Therefore, understanding the structure and function of these proteins has important implications for developing new therapeutic strategies for various diseases.

Amino acid isomerases are a class of enzymes that catalyze the conversion of one amino acid stereoisomer to another. These enzymes play a crucial role in the metabolism and biosynthesis of amino acids, which are the building blocks of proteins.

Amino acids can exist in two forms, called L- and D-stereoisomers, based on the spatial arrangement of their constituent atoms around a central carbon atom. While most naturally occurring amino acids are of the L-configuration, some D-amino acids are also found in certain proteins and peptides, particularly in bacteria and lower organisms.

Amino acid isomerases can convert one stereoisomer to another by breaking and reforming chemical bonds in a process that requires energy. This conversion can be important for the proper functioning of various biological processes, such as protein synthesis, neurotransmitter metabolism, and immune response.

Examples of amino acid isomerases include proline racemase, which catalyzes the interconversion of L-proline and D-proline, and serine hydroxymethyltransferase, which converts L-serine to D-serine. These enzymes are essential for maintaining the balance of amino acids in living organisms and have potential therapeutic applications in various diseases, including neurodegenerative disorders and cancer.

Polyisoprenyl phosphate monosaccharides are a type of glycosylated lipid intermediate molecule involved in the biosynthesis of isoprenoid-linked oligosaccharides, which are crucial for various cellular processes such as protein glycosylation and membrane trafficking.

These molecules consist of a polyisoprenyl phosphate tail, typically formed by the addition of multiple isoprene units (such as farnesyl or geranylgeranyl groups), which is attached to a single monosaccharide sugar moiety, such as glucose, mannose, or galactose.

The polyisoprenyl phosphate tail serves as a lipid anchor that helps tether the glycosylated molecule to cellular membranes during biosynthesis and transport. The monosaccharide component can be further modified by the addition of additional sugar residues, leading to the formation of more complex oligosaccharides that play important roles in various biological processes.

Carbohydrates are a major nutrient class consisting of organic compounds that primarily contain carbon, hydrogen, and oxygen atoms. They are classified as saccharides, which include monosaccharides (simple sugars), disaccharides (double sugars), oligosaccharides (short-chain sugars), and polysaccharides (complex carbohydrates).

Monosaccharides, such as glucose, fructose, and galactose, are the simplest form of carbohydrates. They consist of a single sugar molecule that cannot be broken down further by hydrolysis. Disaccharides, like sucrose (table sugar), lactose (milk sugar), and maltose (malt sugar), are formed from two monosaccharide units joined together.

Oligosaccharides contain a small number of monosaccharide units, typically less than 20, while polysaccharides consist of long chains of hundreds to thousands of monosaccharide units. Polysaccharides can be further classified into starch (found in plants), glycogen (found in animals), and non-starchy polysaccharides like cellulose, chitin, and pectin.

Carbohydrates play a crucial role in providing energy to the body, with glucose being the primary source of energy for most cells. They also serve as structural components in plants (cellulose) and animals (chitin), participate in various metabolic processes, and contribute to the taste, texture, and preservation of foods.

'DBA' is an abbreviation for 'Database of Genotypes and Phenotypes,' but in the context of "Inbred DBA mice," it refers to a specific strain of laboratory mice that have been inbred for many generations. The DBA strain is one of the oldest inbred strains, and it was established in 1909 by C.C. Little at the Bussey Institute of Harvard University.

The "Inbred DBA" mice are genetically identical mice that have been produced by brother-sister matings for more than 20 generations. This extensive inbreeding results in a homozygous population, where all members of the strain have the same genetic makeup. The DBA strain is further divided into several sub-strains, including DBA/1, DBA/2, and DBA/J, among others.

DBA mice are known for their black coat color, which can fade to gray with age, and they exhibit a range of phenotypic traits that make them useful for research purposes. For example, DBA mice have a high incidence of retinal degeneration, making them a valuable model for studying eye diseases. They also show differences in behavior, immune response, and susceptibility to various diseases compared to other inbred strains.

In summary, "Inbred DBA" mice are a specific strain of laboratory mice that have been inbred for many generations, resulting in a genetically identical population with distinct phenotypic traits. They are widely used in biomedical research to study various diseases and biological processes.

Phosphate transport proteins are membrane-bound proteins responsible for the active transport of phosphate ions across cell membranes. They play a crucial role in maintaining appropriate phosphate concentrations within cells and between intracellular compartments, which is essential for various biological processes such as energy metabolism, signal transduction, and bone formation.

These proteins utilize the energy derived from ATP hydrolysis or other sources to move phosphate ions against their concentration gradient, thereby facilitating cellular uptake of phosphate even when extracellular concentrations are low. Phosphate transport proteins can be classified based on their structure, function, and localization into different types, including sodium-dependent and sodium-independent transporters, secondary active transporters, and channels.

Dysregulation of phosphate transport proteins has been implicated in several pathological conditions, such as renal Fanconi syndrome, tumoral calcinosis, and hypophosphatemic rickets. Therefore, understanding the molecular mechanisms underlying phosphate transport protein function is essential for developing targeted therapies to treat these disorders.

Autoantibodies are defined as antibodies that are produced by the immune system and target the body's own cells, tissues, or organs. These antibodies mistakenly identify certain proteins or molecules in the body as foreign invaders and attack them, leading to an autoimmune response. Autoantibodies can be found in various autoimmune diseases such as rheumatoid arthritis, lupus, and thyroiditis. The presence of autoantibodies can also be used as a diagnostic marker for certain conditions.

Experimental arthritis refers to the induction of joint inflammation in animal models for the purpose of studying the disease process and testing potential treatments. This is typically achieved through the use of various methods such as injecting certain chemicals or proteins into the joints, genetically modifying animals to develop arthritis-like symptoms, or immunizing animals to induce an autoimmune response against their own joint tissues. These models are crucial for advancing our understanding of the underlying mechanisms of arthritis and for developing new therapies to treat this debilitating disease.

Tertiary protein structure refers to the three-dimensional arrangement of all the elements (polypeptide chains) of a single protein molecule. It is the highest level of structural organization and results from interactions between various side chains (R groups) of the amino acids that make up the protein. These interactions, which include hydrogen bonds, ionic bonds, van der Waals forces, and disulfide bridges, give the protein its unique shape and stability, which in turn determines its function. The tertiary structure of a protein can be stabilized by various factors such as temperature, pH, and the presence of certain ions. Any changes in these factors can lead to denaturation, where the protein loses its tertiary structure and thus its function.

Rheumatoid arthritis (RA) is a systemic autoimmune disease that primarily affects the joints. It is characterized by persistent inflammation, synovial hyperplasia, and subsequent damage to the articular cartilage and bone. The immune system mistakenly attacks the body's own tissues, specifically targeting the synovial membrane lining the joint capsule. This results in swelling, pain, warmth, and stiffness in affected joints, often most severely in the hands and feet.

RA can also have extra-articular manifestations, affecting other organs such as the lungs, heart, skin, eyes, and blood vessels. The exact cause of RA remains unknown, but it is believed to involve a complex interplay between genetic susceptibility and environmental triggers. Early diagnosis and treatment are crucial in managing rheumatoid arthritis to prevent joint damage, disability, and systemic complications.

Ketosteroids are a type of steroid compound that contain a ketone functional group in their chemical structure. They are derived from cholesterol and are present in both animal and plant tissues. Some ketosteroids are produced endogenously, while others can be introduced exogenously through the diet or medication.

Endogenous ketosteroids include steroid hormones such as testosterone, estradiol, and cortisol, which contain a ketone group in their structure. Exogenous ketosteroids can be found in certain medications, such as those used to treat hormonal imbalances or inflammation.

Ketosteroids have been studied for their potential therapeutic uses, including as anti-inflammatory agents and for the treatment of hormone-related disorders. However, more research is needed to fully understand their mechanisms of action and potential benefits.

Pyridoxal phosphate (PLP) is the active form of vitamin B6 and functions as a cofactor in various enzymatic reactions in the human body. It plays a crucial role in the metabolism of amino acids, carbohydrates, lipids, and neurotransmitters. Pyridoxal phosphate is involved in more than 140 different enzyme-catalyzed reactions, making it one of the most versatile cofactors in human biochemistry.

As a cofactor, pyridoxal phosphate helps enzymes carry out their functions by facilitating chemical transformations in substrates (the molecules on which enzymes act). In particular, PLP is essential for transamination, decarboxylation, racemization, and elimination reactions involving amino acids. These processes are vital for the synthesis and degradation of amino acids, neurotransmitters, hemoglobin, and other crucial molecules in the body.

Pyridoxal phosphate is formed from the conversion of pyridoxal (a form of vitamin B6) by the enzyme pyridoxal kinase, using ATP as a phosphate donor. The human body obtains vitamin B6 through dietary sources such as whole grains, legumes, vegetables, nuts, and animal products like poultry, fish, and pork. It is essential to maintain adequate levels of pyridoxal phosphate for optimal enzymatic function and overall health.

A bacterial gene is a segment of DNA (or RNA in some viruses) that contains the genetic information necessary for the synthesis of a functional bacterial protein or RNA molecule. These genes are responsible for encoding various characteristics and functions of bacteria such as metabolism, reproduction, and resistance to antibiotics. They can be transmitted between bacteria through horizontal gene transfer mechanisms like conjugation, transformation, and transduction. Bacterial genes are often organized into operons, which are clusters of genes that are transcribed together as a single mRNA molecule.

It's important to note that the term "bacterial gene" is used to describe genetic elements found in bacteria, but not all genetic elements in bacteria are considered genes. For example, some DNA sequences may not encode functional products and are therefore not considered genes. Additionally, some bacterial genes may be plasmid-borne or phage-borne, rather than being located on the bacterial chromosome.

A muscle is a soft tissue in our body that contracts to produce force and motion. It is composed mainly of specialized cells called muscle fibers, which are bound together by connective tissue. There are three types of muscles: skeletal (voluntary), smooth (involuntary), and cardiac. Skeletal muscles attach to bones and help in movement, while smooth muscles are found within the walls of organs and blood vessels, helping with functions like digestion and circulation. Cardiac muscle is the specific type that makes up the heart, allowing it to pump blood throughout the body.

Mannans are a type of complex carbohydrate, specifically a heteropolysaccharide, that are found in the cell walls of certain plants, algae, and fungi. They consist of chains of mannose sugars linked together, often with other sugar molecules such as glucose or galactose.

Mannans have various biological functions, including serving as a source of energy for microorganisms that can break them down. In some cases, mannans can also play a role in the immune response and are used as a component of vaccines to stimulate an immune response.

In the context of medicine, mannans may be relevant in certain conditions such as gut dysbiosis or allergic reactions to foods containing mannans. Additionally, some research has explored the potential use of mannans as a delivery vehicle for drugs or other therapeutic agents.

Cis-trans isomeres are molecules that have the same molecular formula and skeletal structure, but differ in the arrangement of their atoms around a double bond. In a cis isomer, the two larger groups or atoms are on the same side of the double bond, while in a trans isomer, they are on opposite sides.

Cis-trans isomerases are enzymes that catalyze the interconversion between cis and trans isomers of various molecules, such as fatty acids, steroids, and retinals. These enzymes play important roles in various biological processes, including membrane fluidity, vision, and the biosynthesis of hormones and other signaling molecules.

Examples of cis-trans isomerases include:

* Fatty acid desaturases, which introduce double bonds into fatty acids and can convert trans isomers to cis isomers
* Retinal isomerases, which interconvert the cis and trans isomers of retinal, a molecule involved in vision
* Steroid isomerases, which catalyze the interconversion of various steroids, including cholesterol and its derivatives.

Cell surface receptors, also known as membrane receptors, are proteins located on the cell membrane that bind to specific molecules outside the cell, known as ligands. These receptors play a crucial role in signal transduction, which is the process of converting an extracellular signal into an intracellular response.

Cell surface receptors can be classified into several categories based on their structure and mechanism of action, including:

1. Ion channel receptors: These receptors contain a pore that opens to allow ions to flow across the cell membrane when they bind to their ligands. This ion flux can directly activate or inhibit various cellular processes.
2. G protein-coupled receptors (GPCRs): These receptors consist of seven transmembrane domains and are associated with heterotrimeric G proteins that modulate intracellular signaling pathways upon ligand binding.
3. Enzyme-linked receptors: These receptors possess an intrinsic enzymatic activity or are linked to an enzyme, which becomes activated when the receptor binds to its ligand. This activation can lead to the initiation of various signaling cascades within the cell.
4. Receptor tyrosine kinases (RTKs): These receptors contain intracellular tyrosine kinase domains that become activated upon ligand binding, leading to the phosphorylation and activation of downstream signaling molecules.
5. Integrins: These receptors are transmembrane proteins that mediate cell-cell or cell-matrix interactions by binding to extracellular matrix proteins or counter-receptors on adjacent cells. They play essential roles in cell adhesion, migration, and survival.

Cell surface receptors are involved in various physiological processes, including neurotransmission, hormone signaling, immune response, and cell growth and differentiation. Dysregulation of these receptors can contribute to the development of numerous diseases, such as cancer, diabetes, and neurological disorders.

'Bacillus subtilis' is a gram-positive, rod-shaped bacterium that is commonly found in soil and vegetation. It is a facultative anaerobe, meaning it can grow with or without oxygen. This bacterium is known for its ability to form durable endospores during unfavorable conditions, which allows it to survive in harsh environments for long periods of time.

'Bacillus subtilis' has been widely studied as a model organism in microbiology and molecular biology due to its genetic tractability and rapid growth. It is also used in various industrial applications, such as the production of enzymes, antibiotics, and other bioproducts.

Although 'Bacillus subtilis' is generally considered non-pathogenic, there have been rare cases of infection in immunocompromised individuals. It is important to note that this bacterium should not be confused with other pathogenic species within the genus Bacillus, such as B. anthracis (causative agent of anthrax) or B. cereus (a foodborne pathogen).

Xylose is a type of sugar that is commonly found in plants and wood. In the context of medical definitions, xylose is often used in tests to assess the function of the small intestine. The most common test is called the "xylose absorption test," which measures the ability of the small intestine to absorb this sugar.

In this test, a patient is given a small amount of xylose to drink, and then several blood and/or urine samples are collected over the next few hours. The amount of xylose that appears in these samples is measured and used to determine how well the small intestine is absorbing nutrients.

Abnormal results on a xylose absorption test can indicate various gastrointestinal disorders, such as malabsorption syndromes, celiac disease, or bacterial overgrowth in the small intestine.

Catalysis is the process of increasing the rate of a chemical reaction by adding a substance known as a catalyst, which remains unchanged at the end of the reaction. A catalyst lowers the activation energy required for the reaction to occur, thereby allowing the reaction to proceed more quickly and efficiently. This can be particularly important in biological systems, where enzymes act as catalysts to speed up metabolic reactions that are essential for life.

Mannosidases are a group of enzymes that catalyze the hydrolysis of mannose residues from glycoproteins, oligosaccharides, and glycolipids. These enzymes play a crucial role in the processing and degradation of N-linked glycans, which are carbohydrate structures attached to proteins in eukaryotic cells.

There are several types of mannosidases, including alpha-mannosidase and beta-mannosidase, which differ in their specificity for the type of linkage they cleave. Alpha-mannosidases hydrolyze alpha-1,2-, alpha-1,3-, alpha-1,6-mannosidic bonds, while beta-mannosidases hydrolyze beta-1,4-mannosidic bonds.

Deficiencies in mannosidase activity can lead to various genetic disorders, such as alpha-mannosidosis and beta-mannosidosis, which are characterized by the accumulation of unprocessed glycoproteins and subsequent cellular dysfunction.

Autoantigens are substances that are typically found in an individual's own body, but can stimulate an immune response because they are recognized as foreign by the body's own immune system. In autoimmune diseases, the immune system mistakenly attacks and damages healthy tissues and organs because it recognizes some of their components as autoantigens. These autoantigens can be proteins, DNA, or other molecules that are normally present in the body but have become altered or exposed due to various factors such as infection, genetics, or environmental triggers. The immune system then produces antibodies and activates immune cells to attack these autoantigens, leading to tissue damage and inflammation.

There doesn't seem to be a specific medical definition for "DNA, protozoan" as it is simply a reference to the DNA found in protozoa. Protozoa are single-celled eukaryotic organisms that can be found in various environments such as soil, water, and the digestive tracts of animals.

Protozoan DNA refers to the genetic material present in these organisms. It is composed of nucleic acids, including deoxyribonucleic acid (DNA) and ribonucleic acid (RNA), which contain the instructions for the development, growth, and reproduction of the protozoan.

The DNA in protozoa, like in other organisms, is made up of two strands of nucleotides that coil together to form a double helix. The four nucleotide bases that make up protozoan DNA are adenine (A), thymine (T), guanine (G), and cytosine (C). These bases pair with each other to form the rungs of the DNA ladder, with A always pairing with T and G always pairing with C.

The genetic information stored in protozoan DNA is encoded in the sequence of these nucleotide bases. This information is used to synthesize proteins, which are essential for the structure and function of the organism's cells. Protozoan DNA also contains other types of genetic material, such as regulatory sequences that control gene expression and repetitive elements with no known function.

Understanding the DNA of protozoa is important for studying their biology, evolution, and pathogenicity. It can help researchers develop new treatments for protozoan diseases and gain insights into the fundamental principles of genetics and cellular function.

Galactose is a simple sugar or monosaccharide that is a constituent of lactose, the disaccharide found in milk and dairy products. It's structurally similar to glucose but with a different chemical structure, and it plays a crucial role in various biological processes.

Galactose can be metabolized in the body through the action of enzymes such as galactokinase, galactose-1-phosphate uridylyltransferase, and UDP-galactose 4'-epimerase. Inherited deficiencies in these enzymes can lead to metabolic disorders like galactosemia, which can cause serious health issues if not diagnosed and treated promptly.

In summary, Galactose is a simple sugar that plays an essential role in lactose metabolism and other biological processes.

A "carbohydrate sequence" refers to the specific arrangement or order of monosaccharides (simple sugars) that make up a carbohydrate molecule, such as a polysaccharide or an oligosaccharide. Carbohydrates are often composed of repeating units of monosaccharides, and the sequence in which these units are arranged can have important implications for the function and properties of the carbohydrate.

For example, in glycoproteins (proteins that contain carbohydrate chains), the specific carbohydrate sequence can affect how the protein is processed and targeted within the cell, as well as its stability and activity. Similarly, in complex carbohydrates like starch or cellulose, the sequence of glucose units can determine whether the molecule is branched or unbranched, which can have implications for its digestibility and other properties.

Therefore, understanding the carbohydrate sequence is an important aspect of studying carbohydrate structure and function in biology and medicine.

Polyisoprenyl phosphates are a type of organic compound that play a crucial role in the biosynthesis of various essential biomolecules in cells. They are formed by the addition of isoprene units, which are five-carbon molecules with a branched structure, to a phosphate group.

In medical terms, polyisoprenyl phosphates are primarily known for their role as intermediates in the biosynthesis of dolichols and farnesylated proteins. Dolichols are long-chain isoprenoids that function as lipid carriers in the synthesis of glycoproteins, which are proteins that contain carbohydrate groups attached to them. Farnesylated proteins, on the other hand, are proteins that have been modified with a farnesyl group, which is a 15-carbon isoprenoid. This modification plays a role in the localization and function of certain proteins within the cell.

Abnormalities in the biosynthesis of polyisoprenyl phosphates and their downstream products have been implicated in various diseases, including cancer, neurological disorders, and genetic syndromes. Therefore, understanding the biology and regulation of these compounds is an active area of research with potential therapeutic implications.

Glycerol-3-Phosphate O-Acyltransferase (GPAT) is an enzyme that plays a crucial role in the biosynthesis of triacylglycerols and phospholipids, which are major components of cellular membranes and energy storage molecules. The GPAT enzyme catalyzes the initial and rate-limiting step in the glycerolipid synthesis pathway, specifically the transfer of an acyl group from an acyl-CoA donor to the sn-1 position of glycerol-3-phosphate, forming lysophosphatidic acid (LPA). This reaction is essential for the production of various glycerolipids, including phosphatidic acid, diacylglycerol, and triacylglycerol. There are four isoforms of GPAT (GPAT1-4) in humans, each with distinct subcellular localizations and functions. Dysregulation of GPAT activity has been implicated in several pathological conditions, such as metabolic disorders, cardiovascular diseases, and cancers.

Glycosylation is the enzymatic process of adding a sugar group, or glycan, to a protein, lipid, or other organic molecule. This post-translational modification plays a crucial role in modulating various biological functions, such as protein stability, trafficking, and ligand binding. The structure and composition of the attached glycans can significantly influence the functional properties of the modified molecule, contributing to cell-cell recognition, signal transduction, and immune response regulation. Abnormal glycosylation patterns have been implicated in several disease states, including cancer, diabetes, and neurodegenerative disorders.

Species specificity is a term used in the field of biology, including medicine, to refer to the characteristic of a biological entity (such as a virus, bacterium, or other microorganism) that allows it to interact exclusively or preferentially with a particular species. This means that the biological entity has a strong affinity for, or is only able to infect, a specific host species.

For example, HIV is specifically adapted to infect human cells and does not typically infect other animal species. Similarly, some bacterial toxins are species-specific and can only affect certain types of animals or humans. This concept is important in understanding the transmission dynamics and host range of various pathogens, as well as in developing targeted therapies and vaccines.

Phosphotransferases are a group of enzymes that catalyze the transfer of a phosphate group from a donor molecule to an acceptor molecule. This reaction is essential for various cellular processes, including energy metabolism, signal transduction, and biosynthesis.

The systematic name for this group of enzymes is phosphotransferase, which is derived from the general reaction they catalyze: D-donor + A-acceptor = D-donor minus phosphate + A-phosphate. The donor molecule can be a variety of compounds, such as ATP or a phosphorylated protein, while the acceptor molecule is typically a compound that becomes phosphorylated during the reaction.

Phosphotransferases are classified into several subgroups based on the type of donor and acceptor molecules they act upon. For example, kinases are a subgroup of phosphotransferases that transfer a phosphate group from ATP to a protein or other organic compound. Phosphatases, another subgroup, remove phosphate groups from molecules by transferring them to water.

Overall, phosphotransferases play a critical role in regulating many cellular functions and are important targets for drug development in various diseases, including cancer and neurological disorders.

Monosaccharides are simple sugars that cannot be broken down into simpler units by hydrolysis. They are the most basic unit of carbohydrates and are often referred to as "simple sugars." Monosaccharides typically contain three to seven atoms of carbon, but the most common monosaccharides contain five or six carbon atoms.

The general formula for a monosaccharide is (CH2O)n, where n is the number of carbon atoms in the molecule. The majority of monosaccharides have a carbonyl group (aldehyde or ketone) and multiple hydroxyl groups. These functional groups give monosaccharides their characteristic sweet taste and chemical properties.

The most common monosaccharides include glucose, fructose, and galactose, all of which contain six carbon atoms and are known as hexoses. Other important monosaccharides include pentoses (five-carbon sugars) such as ribose and deoxyribose, which play crucial roles in the structure and function of nucleic acids (DNA and RNA).

Monosaccharides can exist in various forms, including linear and cyclic structures. In aqueous solutions, monosaccharides often form cyclic structures through a reaction between the carbonyl group and a hydroxyl group, creating a hemiacetal or hemiketal linkage. These cyclic structures can adopt different conformations, known as anomers, depending on the orientation of the hydroxyl group attached to the anomeric carbon atom.

Monosaccharides serve as essential building blocks for complex carbohydrates, such as disaccharides (e.g., sucrose, lactose, and maltose) and polysaccharides (e.g., starch, cellulose, and glycogen). They also participate in various biological processes, including energy metabolism, cell recognition, and protein glycosylation.

Sphingosine is not a medical term per se, but rather a biological compound with importance in the field of medicine. It is a type of sphingolipid, a class of lipids that are crucial components of cell membranes. Sphingosine itself is a secondary alcohol with an amino group and two long-chain hydrocarbons.

Medically, sphingosine is significant due to its role as a precursor in the synthesis of other sphingolipids, such as ceramides, sphingomyelins, and gangliosides, which are involved in various cellular processes like signal transduction, cell growth, differentiation, and apoptosis (programmed cell death).

Moreover, sphingosine-1-phosphate (S1P), a derivative of sphingosine, is an important bioactive lipid mediator that regulates various physiological functions, including immune response, vascular maturation, and neuronal development. Dysregulation of S1P signaling has been implicated in several diseases, such as cancer, inflammation, and cardiovascular disorders.

In summary, sphingosine is a crucial biological compound with medical relevance due to its role as a precursor for various sphingolipids involved in cellular processes and as a precursor for the bioactive lipid mediator S1P.

Gene expression regulation in bacteria refers to the complex cellular processes that control the production of proteins from specific genes. This regulation allows bacteria to adapt to changing environmental conditions and ensure the appropriate amount of protein is produced at the right time.

Bacteria have a variety of mechanisms for regulating gene expression, including:

1. Operon structure: Many bacterial genes are organized into operons, which are clusters of genes that are transcribed together as a single mRNA molecule. The expression of these genes can be coordinately regulated by controlling the transcription of the entire operon.
2. Promoter regulation: Transcription is initiated at promoter regions upstream of the gene or operon. Bacteria have regulatory proteins called sigma factors that bind to the promoter and recruit RNA polymerase, the enzyme responsible for transcribing DNA into RNA. The binding of sigma factors can be influenced by environmental signals, allowing for regulation of transcription.
3. Attenuation: Some operons have regulatory regions called attenuators that control transcription termination. These regions contain hairpin structures that can form in the mRNA and cause transcription to stop prematurely. The formation of these hairpins is influenced by the concentration of specific metabolites, allowing for regulation of gene expression based on the availability of those metabolites.
4. Riboswitches: Some bacterial mRNAs contain regulatory elements called riboswitches that bind small molecules directly. When a small molecule binds to the riboswitch, it changes conformation and affects transcription or translation of the associated gene.
5. CRISPR-Cas systems: Bacteria use CRISPR-Cas systems for adaptive immunity against viruses and plasmids. These systems incorporate short sequences from foreign DNA into their own genome, which can then be used to recognize and cleave similar sequences in invading genetic elements.

Overall, gene expression regulation in bacteria is a complex process that allows them to respond quickly and efficiently to changing environmental conditions. Understanding these regulatory mechanisms can provide insights into bacterial physiology and help inform strategies for controlling bacterial growth and behavior.

Hexoses are simple sugars (monosaccharides) that contain six carbon atoms. The most common hexoses include glucose, fructose, and galactose. These sugars play important roles in various biological processes, such as serving as energy sources or forming complex carbohydrates like starch and cellulose. Hexoses are essential for the structure and function of living organisms, including humans.

Glycoproteins are complex proteins that contain oligosaccharide chains (glycans) covalently attached to their polypeptide backbone. These glycans are linked to the protein through asparagine residues (N-linked) or serine/threonine residues (O-linked). Glycoproteins play crucial roles in various biological processes, including cell recognition, cell-cell interactions, cell adhesion, and signal transduction. They are widely distributed in nature and can be found on the outer surface of cell membranes, in extracellular fluids, and as components of the extracellular matrix. The structure and composition of glycoproteins can vary significantly depending on their function and location within an organism.

Protein binding, in the context of medical and biological sciences, refers to the interaction between a protein and another molecule (known as the ligand) that results in a stable complex. This process is often reversible and can be influenced by various factors such as pH, temperature, and concentration of the involved molecules.

In clinical chemistry, protein binding is particularly important when it comes to drugs, as many of them bind to proteins (especially albumin) in the bloodstream. The degree of protein binding can affect a drug's distribution, metabolism, and excretion, which in turn influence its therapeutic effectiveness and potential side effects.

Protein-bound drugs may be less available for interaction with their target tissues, as only the unbound or "free" fraction of the drug is active. Therefore, understanding protein binding can help optimize dosing regimens and minimize adverse reactions.

Arthritis is a medical condition characterized by inflammation in one or more joints, leading to symptoms such as pain, stiffness, swelling, and reduced range of motion. There are many different types of arthritis, including osteoarthritis, rheumatoid arthritis, psoriatic arthritis, gout, and lupus, among others.

Osteoarthritis is the most common form of arthritis and is caused by wear and tear on the joints over time. Rheumatoid arthritis, on the other hand, is an autoimmune disorder in which the body's immune system mistakenly attacks the joint lining, causing inflammation and damage.

Arthritis can affect people of all ages, including children, although it is more common in older adults. Treatment for arthritis may include medications to manage pain and reduce inflammation, physical therapy, exercise, and in some cases, surgery.

Molecular weight, also known as molecular mass, is the mass of a molecule. It is expressed in units of atomic mass units (amu) or daltons (Da). Molecular weight is calculated by adding up the atomic weights of each atom in a molecule. It is a useful property in chemistry and biology, as it can be used to determine the concentration of a substance in a solution, or to calculate the amount of a substance that will react with another in a chemical reaction.

Carbamyl Phosphate is a chemical compound that plays a crucial role in the biochemical process of nitrogen metabolism, particularly in the urea cycle. It is synthesized in the liver and serves as an important intermediate in the conversion of ammonia to urea, which is then excreted by the kidneys.

In medical terms, Carbamyl Phosphate Synthetase I (CPS I) deficiency is a rare genetic disorder that affects the production of Carbamyl Phosphate. This deficiency can lead to hyperammonemia, which is an excess of ammonia in the bloodstream, and can cause severe neurological symptoms and brain damage if left untreated.

It's important to note that while Carbamyl Phosphate is a critical component of the urea cycle, it is not typically used as a medication or therapeutic agent in clinical practice.

Polysaccharides are complex carbohydrates consisting of long chains of monosaccharide units (simple sugars) bonded together by glycosidic linkages. They can be classified based on the type of monosaccharides and the nature of the bonds that connect them.

Polysaccharides have various functions in living organisms. For example, starch and glycogen serve as energy storage molecules in plants and animals, respectively. Cellulose provides structural support in plants, while chitin is a key component of fungal cell walls and arthropod exoskeletons.

Some polysaccharides also have important roles in the human body, such as being part of the extracellular matrix (e.g., hyaluronic acid) or acting as blood group antigens (e.g., ABO blood group substances).

Arabinose is a simple sugar or monosaccharide that is a stereoisomer of xylose. It is a pentose, meaning it contains five carbon atoms, and is classified as a hexahydroxyhexital because it has six hydroxyl (-OH) groups attached to the carbon atoms. Arabinose is found in various plant polysaccharides, such as hemicelluloses, gums, and pectic substances. It can also be found in some bacteria and yeasts, where it plays a role in their metabolism. In humans, arabinose is not an essential nutrient and must be metabolized by specific enzymes if consumed.

Glucosamine is a natural compound found in the body, primarily in the fluid around joints. It is a building block of cartilage, which is the tissue that cushions bones and allows for smooth joint movement. Glucosamine can also be produced in a laboratory and is commonly sold as a dietary supplement.

Medical definitions of glucosamine describe it as a type of amino sugar that plays a crucial role in the formation and maintenance of cartilage, ligaments, tendons, and other connective tissues. It is often used as a supplement to help manage osteoarthritis symptoms, such as pain, stiffness, and swelling in the joints, by potentially reducing inflammation and promoting cartilage repair.

There are different forms of glucosamine available, including glucosamine sulfate, glucosamine hydrochloride, and N-acetyl glucosamine. Glucosamine sulfate is the most commonly used form in supplements and has been studied more extensively than other forms. While some research suggests that glucosamine may provide modest benefits for osteoarthritis symptoms, its effectiveness remains a topic of ongoing debate among medical professionals.

Lysophospholipids are a type of glycerophospholipid, which is a major component of cell membranes. They are characterized by having only one fatty acid chain attached to the glycerol backbone, as opposed to two in regular phospholipids. This results in a more polar and charged molecule, which can play important roles in cell signaling and regulation.

Lysophospholipids can be derived from the breakdown of regular phospholipids through the action of enzymes such as phospholipase A1 or A2. They can also be synthesized de novo in the cell. Some lysophospholipids, such as lysophosphatidic acid (LPA) and sphingosine-1-phosphate (S1P), have been found to act as signaling molecules that bind to specific G protein-coupled receptors and regulate various cellular processes, including proliferation, survival, and migration.

Abnormal levels of lysophospholipids have been implicated in several diseases, such as cancer, inflammation, and neurological disorders. Therefore, understanding the biology of lysophospholipids has important implications for developing new therapeutic strategies.

Carbohydrate metabolism is the process by which the body breaks down carbohydrates into glucose, which is then used for energy or stored in the liver and muscles as glycogen. This process involves several enzymes and chemical reactions that convert carbohydrates from food into glucose, fructose, or galactose, which are then absorbed into the bloodstream and transported to cells throughout the body.

The hormones insulin and glucagon regulate carbohydrate metabolism by controlling the uptake and storage of glucose in cells. Insulin is released from the pancreas when blood sugar levels are high, such as after a meal, and promotes the uptake and storage of glucose in cells. Glucagon, on the other hand, is released when blood sugar levels are low and signals the liver to convert stored glycogen back into glucose and release it into the bloodstream.

Disorders of carbohydrate metabolism can result from genetic defects or acquired conditions that affect the enzymes or hormones involved in this process. Examples include diabetes, hypoglycemia, and galactosemia. Proper management of these disorders typically involves dietary modifications, medication, and regular monitoring of blood sugar levels.

Magnetic Resonance Spectroscopy (MRS) is a non-invasive diagnostic technique that provides information about the biochemical composition of tissues, including their metabolic state. It is often used in conjunction with Magnetic Resonance Imaging (MRI) to analyze various metabolites within body tissues, such as the brain, heart, liver, and muscles.

During MRS, a strong magnetic field, radio waves, and a computer are used to produce detailed images and data about the concentration of specific metabolites in the targeted tissue or organ. This technique can help detect abnormalities related to energy metabolism, neurotransmitter levels, pH balance, and other biochemical processes, which can be useful for diagnosing and monitoring various medical conditions, including cancer, neurological disorders, and metabolic diseases.

There are different types of MRS, such as Proton (^1^H) MRS, Phosphorus-31 (^31^P) MRS, and Carbon-13 (^13^C) MRS, each focusing on specific elements or metabolites within the body. The choice of MRS technique depends on the clinical question being addressed and the type of information needed for diagnosis or monitoring purposes.

Protein folding is the process by which a protein molecule naturally folds into its three-dimensional structure, following the synthesis of its amino acid chain. This complex process is determined by the sequence and properties of the amino acids, as well as various environmental factors such as temperature, pH, and the presence of molecular chaperones. The final folded conformation of a protein is crucial for its proper function, as it enables the formation of specific interactions between different parts of the molecule, which in turn define its biological activity. Protein misfolding can lead to various diseases, including neurodegenerative disorders such as Alzheimer's and Parkinson's disease.

Mannosides are glycosylated compounds that consist of a mannose sugar molecule (a type of monosaccharide) linked to another compound, often a protein or lipid. They are formed when an enzyme called a glycosyltransferase transfers a mannose molecule from a donor substrate, such as a nucleotide sugar (like GDP-mannose), to an acceptor molecule.

Mannosides can be found on the surface of many types of cells and play important roles in various biological processes, including cell recognition, signaling, and protein folding. They are also involved in the immune response and have been studied as potential therapeutic targets for a variety of diseases, including infectious diseases and cancer.

It's worth noting that mannosides can be further classified based on the specific linkage between the mannose molecule and the acceptor compound. For example, an N-linked mannoside is one in which the mannose is linked to a nitrogen atom on the acceptor protein, while an O-linked mannoside is one in which the mannose is linked to an oxygen atom on the acceptor protein.

Phosphate-binding proteins are a type of protein that play a crucial role in regulating the concentration of phosphates in cells. They function by binding to phosphate ions and facilitating their transport, storage, or excretion. These proteins can be found in various organisms, including bacteria, plants, and animals.

In humans, one example of a phosphate-binding protein is the plasma protein known as fetuin-A. Fetuin-A helps regulate the amount of phosphate in the blood by binding to it and preventing it from forming insoluble precipitates with calcium, which can lead to the formation of kidney stones or calcifications in soft tissues.

Another example is the intracellular protein called alkaline phosphatase, which plays a role in removing phosphate groups from molecules within the cell. This enzyme helps regulate the levels of phosphates and other ions within the cell, as well as contributing to various metabolic processes.

Overall, phosphate-binding proteins are essential for maintaining proper phosphate homeostasis in the body, which is critical for numerous physiological functions, including energy metabolism, bone health, and signal transduction.

Phylogeny is the evolutionary history and relationship among biological entities, such as species or genes, based on their shared characteristics. In other words, it refers to the branching pattern of evolution that shows how various organisms have descended from a common ancestor over time. Phylogenetic analysis involves constructing a tree-like diagram called a phylogenetic tree, which depicts the inferred evolutionary relationships among organisms or genes based on molecular sequence data or other types of characters. This information is crucial for understanding the diversity and distribution of life on Earth, as well as for studying the emergence and spread of diseases.

Lysosomes are membrane-bound organelles found in the cytoplasm of eukaryotic cells. They are responsible for breaking down and recycling various materials, such as waste products, foreign substances, and damaged cellular components, through a process called autophagy or phagocytosis. Lysosomes contain hydrolytic enzymes that can break down biomolecules like proteins, nucleic acids, lipids, and carbohydrates into their basic building blocks, which can then be reused by the cell. They play a crucial role in maintaining cellular homeostasis and are often referred to as the "garbage disposal system" of the cell.

Glycerol-3-phosphate dehydrogenase (GPD) is an enzyme that plays a crucial role in the metabolism of glucose and lipids. It catalyzes the conversion of dihydroxyacetone phosphate (DHAP) to glycerol-3-phosphate (G3P), which is a key intermediate in the synthesis of triglycerides, phospholipids, and other glycerophospholipids.

There are two main forms of GPD: a cytoplasmic form (GPD1) and a mitochondrial form (GPD2). The cytoplasmic form is involved in the production of NADH, which is used in various metabolic processes, while the mitochondrial form is involved in the production of ATP, the main energy currency of the cell.

Deficiencies or mutations in GPD can lead to a variety of metabolic disorders, including glycerol kinase deficiency and congenital muscular dystrophy. Elevated levels of GPD have been observed in certain types of cancer, suggesting that it may play a role in tumor growth and progression.

Fucose is a type of sugar molecule that is often found in complex carbohydrates known as glycans, which are attached to many proteins and lipids in the body. It is a hexose sugar, meaning it contains six carbon atoms, and is a type of L-sugar, which means that it rotates plane-polarized light in a counterclockwise direction.

Fucose is often found at the ends of glycan chains and plays important roles in various biological processes, including cell recognition, signaling, and interaction. It is also a component of some blood group antigens and is involved in the development and function of the immune system. Abnormalities in fucosylation (the addition of fucose to glycans) have been implicated in various diseases, including cancer, inflammation, and neurological disorders.

Alpha-Mannosidase is an enzyme that belongs to the glycoside hydrolase family 47. It is responsible for cleaving alpha-1,3-, alpha-1,6-mannosidic linkages in N-linked oligosaccharides during the process of glycoprotein degradation. A deficiency or malfunction of this enzyme can lead to a lysosomal storage disorder known as alpha-Mannosidosis.

DNA Sequence Analysis is the systematic determination of the order of nucleotides in a DNA molecule. It is a critical component of modern molecular biology, genetics, and genetic engineering. The process involves determining the exact order of the four nucleotide bases - adenine (A), guanine (G), cytosine (C), and thymine (T) - in a DNA molecule or fragment. This information is used in various applications such as identifying gene mutations, studying evolutionary relationships, developing molecular markers for breeding, and diagnosing genetic diseases.

The process of DNA Sequence Analysis typically involves several steps, including DNA extraction, PCR amplification (if necessary), purification, sequencing reaction, and electrophoresis. The resulting data is then analyzed using specialized software to determine the exact sequence of nucleotides.

In recent years, high-throughput DNA sequencing technologies have revolutionized the field of genomics, enabling the rapid and cost-effective sequencing of entire genomes. This has led to an explosion of genomic data and new insights into the genetic basis of many diseases and traits.

Polymerase Chain Reaction (PCR) is a laboratory technique used to amplify specific regions of DNA. It enables the production of thousands to millions of copies of a particular DNA sequence in a rapid and efficient manner, making it an essential tool in various fields such as molecular biology, medical diagnostics, forensic science, and research.

The PCR process involves repeated cycles of heating and cooling to separate the DNA strands, allow primers (short sequences of single-stranded DNA) to attach to the target regions, and extend these primers using an enzyme called Taq polymerase, resulting in the exponential amplification of the desired DNA segment.

In a medical context, PCR is often used for detecting and quantifying specific pathogens (viruses, bacteria, fungi, or parasites) in clinical samples, identifying genetic mutations or polymorphisms associated with diseases, monitoring disease progression, and evaluating treatment effectiveness.

Cyclophilin A is a type of intracellular protein that belongs to the immunophilin family. It has peptidyl-prolyl cis-trans isomerase activity, which means it helps in folding and assembling other proteins by catalyzing the cis-trans isomerization of proline residues.

Cyclophilin A is widely distributed in various tissues and cells, including immune cells such as T lymphocytes. It plays a crucial role in the immune system by binding to and activating the immunosuppressive drug cyclosporine A, which is used to prevent rejection of transplanted organs.

In addition to its role in protein folding and immunosuppression, Cyclophilin A has been implicated in various cellular processes such as signal transduction, gene expression, and apoptosis (programmed cell death). It also plays a role in viral replication, particularly of HIV-1, the virus that causes AIDS.

C57BL/6 (C57 Black 6) is an inbred strain of laboratory mouse that is widely used in biomedical research. The term "inbred" refers to a strain of animals where matings have been carried out between siblings or other closely related individuals for many generations, resulting in a population that is highly homozygous at most genetic loci.

The C57BL/6 strain was established in 1920 by crossing a female mouse from the dilute brown (DBA) strain with a male mouse from the black strain. The resulting offspring were then interbred for many generations to create the inbred C57BL/6 strain.

C57BL/6 mice are known for their robust health, longevity, and ease of handling, making them a popular choice for researchers. They have been used in a wide range of biomedical research areas, including studies of cancer, immunology, neuroscience, cardiovascular disease, and metabolism.

One of the most notable features of the C57BL/6 strain is its sensitivity to certain genetic modifications, such as the introduction of mutations that lead to obesity or impaired glucose tolerance. This has made it a valuable tool for studying the genetic basis of complex diseases and traits.

Overall, the C57BL/6 inbred mouse strain is an important model organism in biomedical research, providing a valuable resource for understanding the genetic and molecular mechanisms underlying human health and disease.

Cyclophilins are a family of proteins that have peptidyl-prolyl isomerase activity, which means they help with the folding and functioning of other proteins in cells. They were first identified as binding proteins for the immunosuppressive drug cyclosporine A, hence their name.

Cyclophilins are found in various organisms, including humans, and play important roles in many cellular processes such as signal transduction, protein trafficking, and gene expression. In addition to their role in normal cell function, cyclophilins have also been implicated in several diseases, including viral infections, cancer, and neurodegenerative disorders.

In medicine, the most well-known use of cyclophilins is as a target for immunosuppressive drugs used in organ transplantation. Cyclosporine A and its derivatives work by binding to cyclophilins, which inhibits their activity and subsequently suppresses the immune response.

Isomerism is a term used in chemistry and biochemistry, including the field of medicine, to describe the existence of molecules that have the same molecular formula but different structural formulas. This means that although these isomers contain the same number and type of atoms, they differ in the arrangement of these atoms in space.

There are several types of isomerism, including constitutional isomerism (also known as structural isomerism) and stereoisomerism. Constitutional isomers have different arrangements of atoms, while stereoisomers have the same arrangement of atoms but differ in the spatial arrangement of their atoms in three-dimensional space.

Stereoisomerism can be further divided into subcategories such as enantiomers (mirror-image stereoisomers), diastereomers (non-mirror-image stereoisomers), and conformational isomers (stereoisomers that can interconvert by rotating around single bonds).

In the context of medicine, isomerism can be important because different isomers of a drug may have different pharmacological properties. For example, some drugs may exist as pairs of enantiomers, and one enantiomer may be responsible for the desired therapeutic effect while the other enantiomer may be inactive or even harmful. In such cases, it may be important to develop methods for producing pure enantiomers of the drug in order to maximize its efficacy and minimize its side effects.

Carrier proteins, also known as transport proteins, are a type of protein that facilitates the movement of molecules across cell membranes. They are responsible for the selective and active transport of ions, sugars, amino acids, and other molecules from one side of the membrane to the other, against their concentration gradient. This process requires energy, usually in the form of ATP (adenosine triphosphate).

Carrier proteins have a specific binding site for the molecule they transport, and undergo conformational changes upon binding, which allows them to move the molecule across the membrane. Once the molecule has been transported, the carrier protein returns to its original conformation, ready to bind and transport another molecule.

Carrier proteins play a crucial role in maintaining the balance of ions and other molecules inside and outside of cells, and are essential for many physiological processes, including nerve impulse transmission, muscle contraction, and nutrient uptake.

Carbohydrate conformation refers to the three-dimensional shape and structure of a carbohydrate molecule. Carbohydrates, also known as sugars, can exist in various conformational states, which are determined by the rotation of their component bonds and the spatial arrangement of their functional groups.

The conformation of a carbohydrate molecule can have significant implications for its biological activity and recognition by other molecules, such as enzymes or antibodies. Factors that can influence carbohydrate conformation include the presence of intramolecular hydrogen bonds, steric effects, and intermolecular interactions with solvent molecules or other solutes.

In some cases, the conformation of a carbohydrate may be stabilized by the formation of cyclic structures, in which the hydroxyl group at one end of the molecule forms a covalent bond with the carbonyl carbon at the other end, creating a ring structure. The most common cyclic carbohydrates are monosaccharides, such as glucose and fructose, which can exist in various conformational isomers known as anomers.

Understanding the conformation of carbohydrate molecules is important for elucidating their biological functions and developing strategies for targeting them with drugs or other therapeutic agents.

Oxidation-Reduction (redox) reactions are a type of chemical reaction involving a transfer of electrons between two species. The substance that loses electrons in the reaction is oxidized, and the substance that gains electrons is reduced. Oxidation and reduction always occur together in a redox reaction, hence the term "oxidation-reduction."

In biological systems, redox reactions play a crucial role in many cellular processes, including energy production, metabolism, and signaling. The transfer of electrons in these reactions is often facilitated by specialized molecules called electron carriers, such as nicotinamide adenine dinucleotide (NAD+/NADH) and flavin adenine dinucleotide (FAD/FADH2).

The oxidation state of an element in a compound is a measure of the number of electrons that have been gained or lost relative to its neutral state. In redox reactions, the oxidation state of one or more elements changes as they gain or lose electrons. The substance that is oxidized has a higher oxidation state, while the substance that is reduced has a lower oxidation state.

Overall, oxidation-reduction reactions are fundamental to the functioning of living organisms and are involved in many important biological processes.

Phosphatidylinositol phosphates (PIPs) are a family of lipid molecules that play crucial roles as secondary messengers in intracellular signaling pathways. They are formed by the phosphorylation of the hydroxyl group on the inositol ring of phosphatidylinositol (PI), a fundamental component of cell membranes.

There are seven main types of PIPs, classified based on the number and position of phosphate groups attached to the inositol ring:

1. Phosphatidylinositol 4-monophosphate (PI4P) - one phosphate group at the 4th position
2. Phosphatidylinositol 5-monophosphate (PI5P) - one phosphate group at the 5th position
3. Phosphatidylinositol 3,4-bisphosphate (PI(3,4)P2) - two phosphate groups at the 3rd and 4th positions
4. Phosphatidylinositol 3,5-bisphosphate (PI(3,5)P2) - two phosphate groups at the 3rd and 5th positions
5. Phosphatidylinositol 4,5-bisphosphate [PI(4,5)P2] - two phosphate groups at the 4th and 5th positions
6. Phosphatidylinositol 3,4,5-trisphosphate [PI(3,4,5)P3] - three phosphate groups at the 3rd, 4th, and 5th positions
7. Phosphatidylinositol 3-phosphate (PI3P) - one phosphate group at the 3rd position

These PIPs are involved in various cellular processes such as membrane trafficking, cytoskeleton organization, cell survival, and metabolism. Dysregulation of PIP metabolism has been implicated in several diseases, including cancer, diabetes, and neurological disorders.

PMI is inhibited by erythrose 4-phosphate, mannitol 1-phosphate, and to a lesser extent, the alpha anomer of M6P. MPI must ... anomeric form used by phosphomannose isomerase and its 1-epimerization by phosphoglucose isomerase". The Journal of Biological ... "Structural basis for phosphomannose isomerase activity in phosphoglucose isomerase from Pyrobaculum aerophilum: a subtle ... Because mannose and glucose are stereoisomers at C2, which is crucial to the mechanism for both enzymes, PMI must allow extra ...
I-cell disease Insulin-like growth factor 2 receptor Mannose Mannose 1-phosphate Alberts, Bruce; et al. (2002). Molecular ... Mannose-6-phosphate (M6P) is a molecule bound by lectin in the immune system. M6P is converted to fructose 6-phosphate by ... mannose phosphate isomerase. M6P is a key targeting signal for acid hydrolase precursor proteins that are destined for ... Mannose-6-Phosphate+Receptor at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Role of M6P in protein ...
Mannose phosphate isomerase Berg, Jeremy M.; Tymoczko, Stryer (2002). Biochemistry (5th ed.). New York: W.H. Freeman and ... Fructose is predominantly converted to fructose 1-phosphate by fructokinase following cellular import. The name Neuberg ester ... Fructose 6-phosphate (sometimes called the Neuberg ester) is a derivative of fructose, which has been phosphorylated at the 6- ... Fructose 6-phosphate lies within the glycolysis metabolic pathway and is produced by isomerisation of glucose 6-phosphate. It ...
... triose-phosphate isomerase MeSH D08.811.399.475.400 - carbon-carbon double bond isomerases MeSH D08.811.399.475.400.700 - ... mannose-binding protein-associated serine proteases MeSH D08.811.277.656.300.760.560 - pancreatic elastase MeSH D08.811.277.656 ... myo-inositol-1-phosphate synthase MeSH D08.811.399.475.200 - aldose-ketose isomerases MeSH D08.811.399.475.200.174 - autocrine ... steroid isomerases MeSH D08.811.399.475.800 - sulfur-sulfur bond isomerases MeSH D08.811.399.475.800.550 - protein disulfide- ...
L-arabinose isomerase EC 5.3.1.5: xylose isomerase EC 5.3.1.6: ribose-5-phosphate isomerase EC 5.3.1.7: mannose isomerase EC ... 3-dione isomerase * EC 5.3.1.33: L-erythrulose 1-phosphate isomerase * EC 5.3.1.34: D-erythrulose 4-phosphate isomerase * EC ... β-carotene isomerase EC 5.3.1.1: triose-phosphate isomerase EC 5.3.1.2: deleted EC 5.3.1.3: D-arabinose isomerase EC 5.3.1.4: ... arabinose-5-phosphate isomerase EC 5.3.1.14: L-rhamnose isomerase EC 5.3.1.15: D-lyxose ketol-isomerase EC 5.3.1.16: 1-(5- ...
... the result could be mannose-6-phosphate if carbon C2 is given the wrong chirality, but the enzyme does not permit that result ... This gene encodes a member of the glucose phosphate isomerase protein family. The encoded protein has been identified as a ... Walker JI, Faik P, Morgan MJ (August 1990). "Characterization of the 5' end of the gene for human glucose phosphate isomerase ( ... Xu W, Lee P, Beutler E (October 1995). "Human glucose phosphate isomerase: exon mapping and gene structure". Genomics. 29 (3): ...
... alpha-D-mannose 1-phosphate, and one product, D-mannose 6-phosphate. This enzyme belongs to the family of isomerases, ... doi:10.1016/0031-9422(79)80123-5. Portal: Biology v t e (EC 5.4.2, Enzymes of known structure, All stub articles, Isomerase ... is an enzyme that catalyzes the chemical reaction alpha-D-mannose 1-phosphate ⇌ {\displaystyle \rightleftharpoons } D-mannose 6 ... Other names in common use include mannose phosphomutase, phosphomannose mutase, and D-mannose 1,6-phosphomutase. This enzyme ...
Lectin mannose binding 2 LNCR3 encoding protein Lung cancer susceptibility 3 LPCAT1: Lysophosphatidylcholine acyltransferase 1 ... Chromosome 5 spans about 182 million base pairs (the building blocks of DNA) and represents almost 6% of the total DNA in cells ... Glucosamine-6-phosphate isomerase 1 GPBP1: Vasculin HEXB: hexosaminidase B (beta polypeptide) HMGXB3: encoding protein HMG-box ... serine protease inhibitor Kazal-type 6 SPINK9: serine protease inhibitor Kazal-type 9 (LEKTI-2) SPZ1: Spermatogenic leucine ...
Among them, all other monosaccharides such as fructose (via the polyol pathway), mannose (the epimer of glucose at position 2 ... Furthermore, addition of the high-energy phosphate group activates glucose for subsequent breakdown in later steps of ... Glucose can also be converted from bacterial xylose isomerase to fructose. In addition, glucose metabolites produce all ... In dilute sodium hydroxide or other dilute bases, the monosaccharides mannose, glucose and fructose interconvert (via a Lobry ...
... being used by bacteria for sugar uptake particularly exogenous hexoses in the case of mannose XYZ to release the phosphate ... by the enzyme phosphomannose isomerase, and then enters the glycolytic pathway or is converted to glucose-6-phosphate by the ... mannose to prevent or treat UTIs. Mannose differs from glucose by inversion of the C-2 chiral center. Mannose displays a 4 C 1 ... Mannose is a sugar monomer of the aldohexose series of carbohydrates. It is a C-2 epimer of glucose. Mannose is important in ...
Phosphomannose isomerase deficiency and mannose therapy". The Journal of Clinical Investigation. 101 (7): 1414-20. doi:10.1172/ ... Dolichol Phosphate N-Acetylglucosamine-1 Phosphate Transferase (DPAGT1) causes a novel congenital disorder of Glycosylation ... phosphomannose isomerase (PMI). A functional therapy for MPI-CDG, alimentary mannose was also described. The characterization ... and its deficiency leads to a shortage in GDP-mannose and dolichol (Dol)-mannose (Man), two donors required for the synthesis ...
KduI/IolB isomerase family - kilobase - kinase - Klenow fragment - Knock-down - knock-out - knock-out experiment - knockout - ... mannose-6-phosphate 6-reductase - mapping - marker - melanoma - melting - menaquinol oxidase (H+-transporting) - Johann Mendel ... undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose transferase - untranslated RNA - upstream - upstream activator sequence ... glycerol-3-phosphate-transporting ATPase - glycoprotein - glycosylation - Golgi apparatus - GRE - guanine - guanine- ...
Binding of dTDP is stabilised by ionic interactions to the phosphate group and by a combination of ionic and hydrophobic ... This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on carbohydrates and ... Biosynthesis of 6-deoxy-L-talose". J. Biol. Chem. 248 (17): 6041-9. doi:10.1016/S0021-9258(19)43505-9. PMID 4199258. Melo A, ... The systematic name of this enzyme class is dTDP-4-dehydro-6-deoxy-D-glucose 3,5-epimerase. Other names in common use include ...
"Triosephosphate Isomerase Deficiency". NORD. Retrieved 14 December 2013. "Triose phosphate isomerase deficiency -TPI" (PDF). ... For example, D-glucose and D-mannose differ in configuration at just one chiral carbon. This class is further broken down by ... Generally, "the names of isomerases are formed as "substrate isomerase" (for example, enoyl CoA isomerase), or as "substrate ... "Triose phosphate-isomerase deficiency". Orphanet. Retrieved 14 November 2013. Celotto AM, Frank AC, Seigle JL, Palladino MJ ( ...
L-fuculose-phosphate aldolase EC 4.1.2.18: 2-dehydro-3-deoxy-L-pentonate aldolase EC 4.1.2.19: rhamnulose-1-phosphate aldolase ... GDP-mannose 4,6-dehydratase EC 4.2.1.48: D-glutamate cyclase EC 4.2.1.49: urocanate hydratase EC 4.2.1.50: pyrazolylalanine ... phosphinomethylmalate isomerase * EC 4.2.1.167: (R)-2-hydroxyglutaryl-CoA dehydratase * EC 4.2.1.168: GDP-4-dehydro-6-deoxy-α-D ... ketotetrose-phosphate aldolase EC 4.1.2.3: deleted, was pentosealdolase. EC 4.1.2.4: deoxyribose-phosphate aldolase EC 4.1.2.5 ...
Triose phosphate catabolism switches over to MGS when phosphate concentrations are too low for glyceraldehyde-3-phosphate ... "Liberation of the triosephosphate isomerase reaction intermediate and its trapping by isomerase, yeast aldolase, and ... and mannose). This suggests that MGS production of methylglyoxal plays a role in controlling expression of sugar-specific ... Ser55 in the active site of MGS is responsible for discriminating the binding of an inorganic phosphate from the phosphate ...
A study about sickle cell anemia in Arabs article about Birth defects Glucose phosphate isomerase deficiency responsible for ... Lebanese type of mannose 6--phosphate receptor recognition defect (1984) •• Algerian type of spondylometaphyseal dysplasia ( ... Shalev O, Leibowitz G, Brok-Simoni F (June 1994). "[Glucose phosphate isomerase deficiency with congenital nonspherocytic ... 99 (6): 1316-1324. doi:10.1016/j.ajhg.2016.10.012. PMC 5142112. PMID 27889059. Hodgson, Jason A. (2014). "Early Back-to-Africa ...
The rough endoplasmic reticulum is key in multiple functions: Manufacture of lysosomal enzymes with a mannose-6-phosphate ... and the peptidylprolyl isomerase family. Only properly folded proteins are transported from the rough ER to the Golgi apparatus ... 9-branching mannose, and 3-glucose at the end) to the side-chain nitrogen of Asn. In most cells the smooth endoplasmic ... including protein disulfide isomerase (PDI), ERp29, the Hsp70 family member BiP/Grp78, calnexin, calreticulin, ...
... cyclic phosphate phosphodiesterase EC 3.1.4.57: phosphoribosyl 1,2-cyclic phosphate 1,2-diphosphodiesterase * EC 3.1.4.58: RNA ... muconolactone Δ-isomerase) and EC 3.1.1.24 (3-oxoadipate enol-lactonase) EC 3.1.1.17: gluconolactonase EC 3.1.1.18: deleted, ... dolichylphosphate-mannose phosphodiesterase EC 3.1.4.50: glycosylphosphatidylinositol phospholipase D EC 3.1.4.51: glucose-1- ... glycerol-3-phosphate-transporting ATPase EC 3.6.3.21: Now EC 7.4.2.1, ABC-type polar-amino-acid transporter EC 3.6.3.22: Now EC ...
PPID Peptidyl-prolyl cis-trans isomerase D PPIE Peptidyl-prolyl cis-trans isomerase E PPIF Peptidyl-prolyl cis-trans isomerase ... FTH1 Heavy chain of Ferritin GDI2 rab/ras vesicular trafficking GUK1 Guanylate kinase transfers phosphate from ATP to GMP HPRT ... kinase PGAM5 ENOPH1 Enolase phosphatase LDHA Lactate dehydrogenase TALDO1 Transaldolase in pentose shunt TSTA3 Mannose ... 8 (6): e1002736. doi:10.1371/journal.pgen.1002736. PMC 3375229. PMID 22723752. Lam KC, Chung HR, Semplicio G, Iyer SS, Gaub A, ...
... mannose-1-phosphate guanylyltransferase EC 2.7.7.14: ethanolamine-phosphate cytidylyltransferase EC 2.7.7.15: choline-phosphate ... tRNA ribosyltransferase-isomerase EC 2.4.99.18: dolichyl-diphosphooligosaccharide-protein glycotransferase EC 2.4.99.19: ... glucose-1-phosphate cytidylyltransferase EC 2.7.7.34: glucose-1-phosphate guanylyltransferase EC 2.7.7.35: ribose-5-phosphate ... acyl phosphate:glycerol-3-phosphate acyltransferase (*) EC 2.3.1.276: galactosamine-1-phosphate N-acetyltransferase (*) EC 2.3. ...
... propanediol-phosphate dehydrogenase EC 1.1.1.8: glycerol-3-phosphate dehydrogenase (NAD+) EC 1.1.1.9: D-xylulose reductase EC ... GDP-mannose 6-dehydrogenase EC 1.1.1.133: dTDP-4-dehydrorhamnose reductase EC 1.1.1.134: dTDP-6-deoxy-L-talose 4-dehydrogenase ... aurachin C monooxygenase/isomerase EC 1.14.13.223: 3-hydroxy-4-methylanthranilyl-[aryl-carrier protein] 5-monooxygenase EC 1.14 ... sn-glycerol-1-phosphate dehydrogenase EC 1.1.1.262: 4-hydroxythreonine-4-phosphate dehydrogenase EC 1.1.1.263: 1,5-anhydro-D- ...
PMI is inhibited by erythrose 4-phosphate, mannitol 1-phosphate, and to a lesser extent, the alpha anomer of M6P. MPI must ... anomeric form used by phosphomannose isomerase and its 1-epimerization by phosphoglucose isomerase". The Journal of Biological ... "Structural basis for phosphomannose isomerase activity in phosphoglucose isomerase from Pyrobaculum aerophilum: a subtle ... Because mannose and glucose are stereoisomers at C2, which is crucial to the mechanism for both enzymes, PMI must allow extra ...
ACT, β-actin; ASAT, aspartate aminotransferase; GAPDH, glyceraldeyde-3-phosphate dehydrogenase; GPI, glucose-6-phosphate ... mannose-6-phosphate isomerase; NA, not available; NADP, nicotinamide adenine dinucleotide phosphate; ORF, open reading frame; ... isomerase; G6PDH, glucose-6-phosphate dehydrogenase; HSP70, heat-shock protein 70; ICD, isocitrate dehydrogenase; ID, identity ... Volume 27, Number 6-June 2021 Dispatch. Cutaneous Leishmaniasis Caused by an Unknown Leishmania Strain, Arizona, USA Marcos de ...
... glyceraldehyde-3-phosphate dehydrogenase; 69, triose-phosphate isomerase; 70, fructose-bisphosphate aldolase; 71, fructose-1,6- ... mannose-1-phosphate guanylyltransferase/mannose-6-phosphate isomerase (#17), D-hexose-6-phosphate mutarotase (#18), ... triose-phosphate isomerase; 47, type I glyceraldehyde-3-phosphate dehydrogenase; 48, phosphoglycerate kinase; 49, ... JS666, has genes encoding both glycolysis and the ED pathway as well as an incomplete pentose phosphate pathway (Mattes et al ...
PDB Description: the crystal structure of phosphoglucose isomerase from pyrococcus furiosus in complex with mannose 6-phosphate ... PDB Compounds: (A:) Glucose-6-phosphate isomerase. SCOP Domain Sequences for d2gc3a1:. Sequence; same for both SEQRES and ATOM ... Protein Glucose-6-phosphate isomerase, GPI [89404] (2 species). Type II phosphoglucose isomerase. ... d2gc3a1 b.82.1.7 (A:0-186) Glucose-6-phosphate isomerase, GPI {Archaeon Thermococcus litoralis [TaxId: 2265]} ...
mannose-1-phosphate guanylyltransferase (EC 2.7.7.13). 48%. 442.2. med. AO353_10250. mannose-1-phosphate guanylyltransferase. ... Phosphomannose isomerase; Short=PMI; ... GDP-mannose pyrophosphorylase 1; GMP 1; GMPP 1; EC 2.7.7.13. 53 ... mannose-1-phosphate guanyltransferase. mannose-1-phosphate guanylyltransferase (EC 2.7.7.13) (characterized). 49%. 98%. 448.4. ... mannose-1-phosphate guanylyltransferase (EC 2.7.7.13) (characterized). 43%. 98%. 383.6. Mannose-1-phosphate guanylyltransferase ...
Comment: SMc03111 (P29954) is specifically important for utilizing mannose, which confirms it is mannose 6-phosphate isomerase ... Phosphomannose isomerase; Short=PMI; ... manA: mannose-6-phosphate isomerase, class I (EC 5.3.1.8) ( ... mannose-6-phosphate isomerase (EC 5.3.1.8) (characterized). 83%. 100%. 645.6. hi. BWI76_RS16280. mannose-6-phosphate isomerase ... 1 candidates for manA: mannose-6-phosphate isomerase. Score. Gene. Description. Similar to. Id.. Cov.. Bits. Other hit. Other ...
Ribose 5-phosphate isomerase B. 95.86%. PM0084032. 62. A0A6M2Y7D8. Carbamate kinase. 95.94%. PM0083630. ... Mannose-6-phosphate isomerase. 95.27%. PM0083650. 21. A0A385XM27. Mature parasite-infected erythrocyte surface antigen. 95.27% ... Among these antibiotics Ribostamycin was identified as a potent drug against the Protein Disulphide Isomerase with a ... 7.35Kcal/mol with the protein disulphide isomerase of Erysipelothrix rhusiopathiae and forms 5 hydrogen bonds with ASP-31, GLU- ...
Mannose-6-phosphate isomerase. $1500 $950. LT0425. MultiTag Control Protein for Western Blot. $250 $149. ...
... phosphomannose isomerase) ; mannose-1-phosphate guanylyl transferase (GDP-mannose pyrophosphorylase). NC_006510:3321426:3349516 ... mannose-1-phosphate guanylyltransferase (GDP) ;mannose-6-phosphate isomerase, type 2. NC_014002:80967:85866. NC_014002:80967. ... mannose-1-phosphate guanylyltransferase/mannose-6-phosphate isomerase. NC_014839:253961:273752. NC_014839:253961. Pantoea sp. ... mannose-1-phosphate guanylyltransferase/mannose-6-phosphate isomerase. NC_009505:531000:552565. NC_009505:531000. Brucella ovis ...
isomerase activity. IEP. Enrichment. BP. GO:0019693. ribose phosphate metabolic process. IEP. Enrichment. ... mannose-6-phosphate isomerase activity. IEP. Enrichment. MF. GO:0004743. pyruvate kinase activity. IEP. Enrichment. ... phosphate-containing compound metabolic process. None. Extended. BP. GO:0006807. nitrogen compound metabolic process. None. ... nucleoside phosphate catabolic process. None. Extended. BP. GO:1901360. organic cyclic compound metabolic process. None. ...
glucose-1-phosphate thymidylyltransferase (NCBI). 112, 333. GSU2088. GSU2088. glycosyl transferase, group 2 family protein ( ... mannose-6-phosphate isomerase (NCBI). 112, 156. GSU2382. trpG. anthranilate synthase component II (NCBI). 47, 196. ... POSITION A C G T 1 0.0 0.4 0.0 0.6 2 0.0 0.0 0.2 0.8 3 0.4 0.6 0.0 0.0 4 0.0 0.0 0.0 1.0 5 0.2 0.0 0.0 0.8 6 0.0 0.0 0.0 1.0 7 ... 0.333333 0.0 0.666667 2 0.0 1.0 0.0 0.0 3 0.222222 0.777778 0.0 0.0 4 0.0 0.0 0.777778 0.222222 5 0.0 0.444444 0.555556 0.0 6 ...
Cupin (CL0029) MannoseP_isomer; Mannose-6-phosphate isomerase (PF01050; HMM-score: 14.7) ...
mannose-6-phosphate isomerase activity. IEP. Enrichment. MF. GO:0004553. hydrolase activity, hydrolyzing O-glycosyl compounds. ...
mannose-6-phosphate isomerase activity. IEP. Enrichment. MF. GO:0004576. oligosaccharyl transferase activity. IEP. Enrichment. ...
Phosphomannose isomerase (PMI) catalyses the reversible isomerization of fructose-6-phosphate (F6P) and mannose-6-phosphate ( ... The x-ray crystal structure of phosphomannose isomerase from Candida albicans at 1.7 angstrom resolution. ... cupin signature is found as a central component of many microbial proteins including certain types of phosphomannose isomerase ...
triosephosphate isomerase. PLASTID ISOFORM TRIOSE PHOSPHATE. ISOMERASE, triosephosphate. isomerase. 0.84. 0.31. -0.32. ... Mannose-6-phosphate isomerase, type I. MATERNAL EFFECT EMBRYO ARREST 31,. PHOSPHOMANNOSE ISOMERASE 1. 0.74. 0.32. -0.33. ... 15-cis-zeta-carotene isomerase. 15-cis-zeta-carotene isomerase,. Z-ISO1.1, Z-ISO1.2. 0.7. 0.31. -0.32. ... FKBP-like peptidyl-prolyl cis-trans isomerase family. protein. 0.74. 0.32. -0.31. ...
... ribose-5-phosphate isomerase B1; rpiB2 (CD3480), ribose-5-phosphate isomerase B2; rbsK (CD0299), ribokinase; tkt (CD2321), ... PTS mannose-specific IIA, IIB, IIC; ptsG (CD2667, CD2666), PTS glucose-specific IIA, IICB; pmi (CD2491), mannose-6-phosphate ... triosephosphate isomerase; gapA (CD3174) and gapB (CD1767), glyceraldehyde-3-phosphate dehydrogenase; pgk (CD3173), ... and mannose (CD3015-CD3013) PTS, whereas the synthesis of some PTS of secondary carbon sources, such as sorbitol (CD0764-CD0768 ...
Agnathan triosephosphate isomerase. Isozyme Bulletin 21: 189.. *Matson, R. H. 1987. Mannose-6-phosphate isomerase in birds. ...
Funciton: Mannose-specific PTS, IIA component (EC 2.7.1.69) Locus tag: AHA_2341. Name: manX. Funciton: Mannose-specific PTS, ...
","Muconolactone Delta-isomerase [Ensembl]. Muconolactone delta-isomerase [Interproscan].","protein_coding" "CRP33198","catA"," ... "GDP-mannose 6-dehydrogenase [Ensembl]. UDP-glucose/GDP-mannose dehydrogenase family [Interproscan].","protein_coding" "CRO10061 ... Mannose-6-phosphate isomerase [Interproscan].","protein_coding" "CRO14921","ppc","Pseudomonas aeruginosa","Phosphoenolpyruvate ...
DIN9 (DARK INDUCIBLE 9) MANNOSE-6-PHOSPHATE ISOMERASE Downloads. Fasta sequences:. Proteins. DNA. ... AT3G56700 - ( FAR6 (FATTY ACID REDUCTASE 6) fatty acyl-CoA reductase (alcohol-forming)/ oxidoreductase acting on the CH-CH ...
Human Mannose-6-phosphate isomerase (MPI) ELISA Kit $339.00. - $24,569.00. * Human Triggering receptor expressed on myeloid ... LinKine™ AbFluor™ 594 Labeling Kit (Optimized for samples with molecular weight of 6 KD to 20 KD) $209.00. - $339.00. ...
Phosphomannose isomerase (PMI) catalyses the reversible isomerization of fructose-6-phosphate (F6P) and mannose-6-phosphate ( ... The x-ray crystal structure of phosphomannose isomerase from Candida albicans at 1.7 angstrom resolution. ... cupin signature is found as a central component of many microbial proteins including certain types of phosphomannose isomerase ...
Mannose phosphate isomerase. Congenital disorder of glycosylation MPI-CDG EBI Database, IPRO16305 Mannose-6-phosphate Isomerase ... GDP-mannose is used for synthesis of dolichol-phosphate-mannose, which is essential for N-linked glycosylation and thus the ... ... "Deficiency of dolichol-phosphate-mannose synthase-1 causes congenital disorder of glycosylation type Ie". The Journal of ... ... Enzymes that catalyze the transfer of mannose from a nucleoside diphosphate mannose to an acceptor molecule which is frequently ...
Mannose-6-phosphate isomerase, catalyzes the interconversion of fructose-6-P and mannose-6-P; required for early steps in ... GMP synthase, an enzyme that catalyzes the second step in the biosynthesis of GMP from inosine 5-phosphate (IMP); ... Guanylate kinase, converts GMP to GDP; required for growth and mannose outer chain elongation of cell wall N-linked ... Alpha-1,3-mannosyltransferase, integral membrane glycoprotein of the Golgi complex, required for addition of alpha1,3-mannose ...
Untreated HFI patients present an abnormal transferrin (Tf) glycosylation pattern due to the inhibition of mannose-6-phosphate ... isomerase by fructose-1-phosphate. Hence, elevated serum carbohydrate-deficient Tf (CDT) may allow the prompt detection of HFI ...
... a TaqMan qPCR for diagnostics of the agent targeting genes encoding a heat shock protein of the Hsp20 family and mannose-6- ... phosphate isomerase. Quantitation with synthetic oligonucleotides as standard showed that the developed TaqMan qPCR assays ...
  • Mannose-6 phosphate isomerase (MPI), alternately phosphomannose isomerase (PMI) (EC 5.3.1.8) is an enzyme which facilitates the interconversion of fructose 6-phosphate (F6P) and mannose-6-phosphate (M6P). (wikipedia.org)
  • An enzyme that catalyzes the reversible isomerization of D-mannose-6-phosphate to form D-fructose-6-phosphate, an important step in glycolysis. (lookformedical.com)
  • The HBP and glycolysis share the first two steps and diverge at fructose-6-phosphate (F6P) (Fig. 1 ). (biomedcentral.com)
  • Glutamine fructose-6-phosphate amidotransferase (GFAT) converts F6P and glutamine to glucosamine-6-phosphate and glutamate in the rate-limiting step of HBP [ 6 ]. (biomedcentral.com)
  • Glucose enters the cell and undergoes two-step conversion to fructose-6P (fructose-6-phosphate), after which approximately 95% of it proceeds to glycolysis and 3-5% of it is converted to glucosamine-6P (glucosamine-6-phosphate) by the enzyme GFAT (glutamine:fructose-6-phosphate amidotransferase), utilizing glutamine that enters the cell. (biomedcentral.com)
  • It has been shown in some cases that the enzyme has a functional phosphate group, which can act as the donor. (lookformedical.com)
  • Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Human Peroxiredoxin 6 (PRDX6) in serum, plasma, tissue homogenates and other biological fluids. (lotuskringpoeldijk.nl)
  • Description: Enzyme-linked immunosorbent assay based on the Double-antibody Sandwich method for detection of Human Peroxiredoxin 6 (PRDX6) in samples from serum, plasma, tissue homogenates and other biological fluids with no significant corss-reactivity with analogues from other species. (lotuskringpoeldijk.nl)
  • Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Human Baculoviral IAP Repeat Containing Protein 6 (BIRC6) in Tissue homogenates, cell lysates and other biological fluids. (1elisakits.com)
  • Description: Enzyme-linked immunosorbent assay based on the Double-antibody Sandwich method for detection of Human Baculoviral IAP Repeat Containing Protein 6 (BIRC6) in samples from Tissue homogenates, cell lysates and other biological fluids with no significant corss-reactivity with analogues from other species. (1elisakits.com)
  • In the next step, the enzyme glucosamine-phosphate N-acetyltransferase (GNPNAT) catalyzes Ac-CoA and glucosamine-6-phosphate to generate N-acetylglucosamine-6-phosphate (GlcNAc-6P) and CoA. (biomedcentral.com)
  • This is followed by GlcNAc phosphomutase (PGM3/AGM1)-mediated isomerization into GlcNAc-1-phosphate (GlcNAc-1-P). Finally, UTP and GlcNAc-1Pz produce UDP-GlcNAc through UDP-N-acetylglucosamine pyrophosphorylase (UAP1/AGX1) enzyme [ 6 , 7 ]. (biomedcentral.com)
  • The enzyme also converts D -erythrose 4-phosphate into D -erythrulose 4-phosphate and D -threose 4-phosphate. (qmul.ac.uk)
  • The PMM2 gene encodes an enzyme (PMM2) responsible for converting mannose-6-phosphate to mannose-1-phosphate. (cdghub.com)
  • Studies on phosphomannose isomerase. (wikipedia.org)
  • This cupin signature is found as a central component of many microbial proteins including certain types of phosphomannose isomerase, polyketide synthase, epimerase, and dioxygenase. (embl-heidelberg.de)
  • M6P can be converted to F6P by mannose-6-phosphate isomerase and subsequently utilized in several metabolic pathways including glycolysis and capsular polysaccharide biosynthesis. (wikipedia.org)
  • The glucose 6-phosphate that is formed during the phosphoglucomutase process can be absorbed into glycolysis or a different pathway, such as the pentose phosphate pathway. (microbiologynote.com)
  • What is the advantage of activating pyruvate kinase with fructose-1,6-bisphosphate? (flashcardmachine.com)
  • The X-linked markers glucose-6-phosphate dehydrogenase (G6PD), phosphoglycerate kinase (PGK), and hypoxanthine phosphoribosyl transferase (HPRT), and the non-X-linked markers pyruvate kinase (PKM2) mannose phosphate isomerase (MPI), N-acetyl hexosaminidase A (HEXA) and beta2-microglubulin (beta2-m) all segregated in concordance with the X/15 translocation chromosome. (ox.ac.uk)
  • Phosphoglucose isomerase (PGI) has a very similar function to PMI, (as it catalyzes the interconversion of glucose 6-phosphate and F6P) however PGI can anomerize alpha and beta G6P, and may also catalyze the conversion of alpha M6P to beta M6P, while PMI may not anomerize M6P. (wikipedia.org)
  • Because mannose and glucose are stereoisomers at C2, which is crucial to the mechanism for both enzymes, PMI must allow extra space in the active site to allow for rotation of mannose to form the cis-enediol intermediate, which is the same intermediate formed by phosphoglucose isomerase. (wikipedia.org)
  • Is there an energetic benefit of Glucose over Mannose? (flashcardmachine.com)
  • 4) glycosidic linkage, which connects to Iast the two sugar residues on a non-reducing end, creating glucose 1-phosphate as well as the polymer, which is one that is a glucose unit smaller. (microbiologynote.com)
  • PhosphoroLyses conserves a portion of the energy contained in the glycosidic bond within the phosphate ester of glucose 1-phosphate. (microbiologynote.com)
  • The glycogen phosphorylase can be converted into glucose 6-phosphate via phosphoglucomutase which is responsible for catalyzing the reversible reaction. (microbiologynote.com)
  • Among these antibiotics Ribostamycin was identified as a potent drug against the Protein Disulphide Isomerase with a significant binding energy of -7.35Kcal/mol with formation of 5 hydrogen bonds. (ijpsr.com)
  • Herein, we introduce a TaqMan qPCR for diagnostics of the agent targeting genes encoding a heat shock protein of the Hsp20 family and mannose-6-phosphate isomerase. (uibk.ac.at)
  • PMI is inhibited by erythrose 4-phosphate, mannitol 1-phosphate, and to a lesser extent, the alpha anomer of M6P. (wikipedia.org)
  • Structure differs from phosphoglucose isomerase by a threonine residue (Thr291) which creates extra space in the active site of PMI to accommodate the different stereochemistry of M6P. (wikipedia.org)
  • Human fibroblasts containing a translocation between the X chromosome and chromosome 15 were fused with the 6-thioguanine-resistant mouse cell line, IR. (ox.ac.uk)
  • Hybrids which were counterselected in 6-thioguanine lost this chromosome. (ox.ac.uk)
  • Chromosome 5 spans about 181 million base pairs (the building blocks of DNA ) and represents almost 6% of the total DNA in cells . (wikidoc.org)
  • This is then converted to GlcNAc-1P (N-acetylglucosamine 1-phosphate) by PGM3/AGM1 (phosphoglucomutase) and further to UDP-GlcNAc (uridine diphosphate N-acetylglucosamine) by UAP/AGX1 (UDP-N-acetylhexosamine pyrophosphorylase), utilizing UTP from the nucleotide metabolism pathway. (biomedcentral.com)
  • Description: A sandwich ELISA kit for detection of Peroxiredoxin 6 from Human in samples from blood, serum, plasma, cell culture fluid and other biological fluids. (lotuskringpoeldijk.nl)
  • Both parasite species were identified as L. (V.) peruviana based on cytochrome b and mannose phosphate isomerase gene analyses. (edu.pe)
  • 2. Dickens, F. and Williamson, D.H. Pentose phosphate isomerase and epimerase from animal tissues. (qmul.ac.uk)
  • Approximately, 200 biotic (organisms or particles mixtures of many proteins [4, 6]. (cdc.gov)
  • Enzymes that catalyze the transfer of mannose from a nucleoside diphosphate mannose to an acceptor molecule which is frequently another carbohydrate. (lookformedical.com)
  • Mutases are a class of isomerases, enzymes that convert stereoisomers and the structural and positional isomers. (microbiologynote.com)
  • Congenital disorder of glycosylation MPI-CDG EBI Database, IPRO16305 Mannose-6-phosphate Isomerase. (wikipedia.org)
  • There are over 1000 confirmed cases to date, making it the most common congenital disorder of glycosylation 1,6,7 . (cdghub.com)
  • MPI must convert an aldose (mannose) to a ketose (fructose), in addition to opening and closing the rings for these sugars. (wikipedia.org)
  • A group of enzymes that catalyze an intramolecular transfer of a phosphate group. (lookformedical.com)
  • 6]. Some of the best examples of high-molecular-weight sectors, workers are at increased risk of becoming sensitized occupational allergens are the fungal enzymes. (cdc.gov)
  • Description: A sandwich quantitative ELISA assay kit for detection of Human Peroxiredoxin 6 (PRDX6) in samples from serum, plasma, tissue homogenates or other biological fluids. (lotuskringpoeldijk.nl)
  • Description: Quantitative sandwich ELISA for measuring Human Peroxiredoxin-6 (PRDX6) in samples from cell culture supernatants, serum, whole blood, plasma and other biological fluids. (lotuskringpoeldijk.nl)
  • GNA1/GNPNAT1 (glucosamine-6-phosphate N-acetyltransferase) then converts glucosamine-6P (which can also be made by glucosamine entering the cell) into GlcNAc-6P (N-acetylglucosamine-6-Phosphate), also utilizing acetyl-CoA that is made from fatty acid metabolism. (biomedcentral.com)
  • Structures of mannose-6-phosphate isomerase from Salmonella typhimurium bound to metal atoms and substrate: implications for catalytic mechanism" (PDF). (wikipedia.org)
  • This regulatory mechanism ensures that following 6 step in equilibrium are "pulled" into completion. (flashcardmachine.com)
  • Mannose-6-phosphate isomerase may also enable the synthesis of GDP-mannose in eukaryotic organisms. (wikipedia.org)
  • Pathogenic strains then produce two toxins (TcdA and TcdB), which are considered as the major virulence factors, that lead to the disruption of the actin cytoskeleton of intestinal epithelium cells (6,7), therefore, conferring the CDI symptoms (diarrhoea, epithelial apoptosis and ulceration). (studyres.com)
  • The breakdown of polysaccharides in food like glycogen and starch inside the intestinal tract through hydrolysis, rather than phosphorolysis, will not result in any energy gain Sugar phosphates cannot be transferred into the cells of the intestine, but they must first be dephosphorylated and converted to sugar free. (microbiologynote.com)
  • In the United States, the 2010 civilian workforce accounted tion of immunoglobulin E (IgE) results in the release of for 139 million people [1] who spend up to a quarter mediators from mast cells and eosinophils [6, 7]. (cdc.gov)
  • Mannose-1-phosphate is a precursor for GDP-mannose, which is the mannose donor used in the construction of mannose-containing sugar chains ( glycans ) in the cytoplasm. (cdghub.com)
  • Glucosamine entering the cell is also converted to glucosamine-6-phosphate using GNK (GlcNAc kinase). (biomedcentral.com)
  • The study sites were determined by reports try [ 1-6 ]. (who.int)
  • 2]. With changes in the global market, particularly with induce OA have been identified [4, 6, 7]. (cdc.gov)