Glycoside Hydrolases are a class of enzymes that catalyze the hydrolysis of glycosidic bonds, resulting in the breakdown of complex carbohydrates and oligosaccharides into simpler sugars.
Any compound that contains a constituent sugar, in which the hydroxyl group attached to the first carbon is substituted by an alcoholic, phenolic, or other group. They are named specifically for the sugar contained, such as glucoside (glucose), pentoside (pentose), fructoside (fructose), etc. Upon hydrolysis, a sugar and nonsugar component (aglycone) are formed. (From Dorland, 28th ed; From Miall's Dictionary of Chemistry, 5th ed)
Any member of the class of enzymes that catalyze the cleavage of the substrate and the addition of water to the resulting molecules, e.g., ESTERASES, glycosidases (GLYCOSIDE HYDROLASES), lipases, NUCLEOTIDASES, peptidases (PEPTIDE HYDROLASES), and phosphatases (PHOSPHORIC MONOESTER HYDROLASES). EC 3.
A genus of aerobic, gram-negative, motile, slightly curved, rod-shaped bacteria. (From Bergey's Manual of Determinative Bacteriology, 9th ed)
Cyclopentanophenanthrenes with a 5- or 6-membered lactone ring attached at the 17-position and SUGARS attached at the 3-position. Plants they come from have long been used in congestive heart failure. They increase the force of cardiac contraction without significantly affecting other parameters, but are very toxic at larger doses. Their mechanism of action usually involves inhibition of the NA(+)-K(+)-EXCHANGING ATPASE and they are often used in cell biological studies for that purpose.
A family of glycosidases that hydrolyse crystalline CELLULOSE into soluble sugar molecules. Within this family there are a variety of enzyme subtypes with differing substrate specificities that must work together to bring about complete cellulose hydrolysis. They are found in structures called CELLULOSOMES.
An endocellulase with specificity for the hydrolysis of 1,4-beta-glucosidic linkages in CELLULOSE, lichenin, and cereal beta-glucans.
Enzymes which catalyze the endohydrolysis of 1,4-beta-D-xylosidic linkages in XYLANS.
A group of enzymes that catalyze the hydrolysis of alpha- or beta-xylosidic linkages. EC 3.2.1.8 catalyzes the endo-hydrolysis of 1,4-beta-D-xylosidic linkages; EC 3.2.1.32 catalyzes the endo-hydrolysis of 1,3-beta-D-xylosidic linkages; EC 3.2.1.37 catalyzes the exo-hydrolysis of 1,4-beta-D-linkages from the non-reducing termini of xylans; and EC 3.2.1.72 catalyzes the exo-hydrolysis of 1,3-beta-D-linkages from the non-reducing termini of xylans. Other xylosidases have been identified that catalyze the hydrolysis of alpha-xylosidic bonds.
Polysaccharides consisting of xylose units.
A genus of gram-negative, anaerobic bacteria in the family Fibrobacteraceae, isolated from the human GASTROINTESTINAL TRACT.
A genus of gram-negative, straight or curved rods which are motile by means of a single, polar flagellum. Members of this genus are found in coastal waters and the open ocean. (From Bergey's Manual of Determinative Bacteriology, 9th ed)
A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.
Extracellular structures found in a variety of microorganisms. They contain CELLULASES and play an important role in the digestion of CELLULOSE.
A polysaccharide with glucose units linked as in CELLOBIOSE. It is the chief constituent of plant fibers, cotton being the purest natural form of the substance. As a raw material, it forms the basis for many derivatives used in chromatography, ion exchange materials, explosives manufacturing, and pharmaceutical preparations.
A genus of gram-positive bacteria in the family Lachnospiraceae that inhabits the RUMEN; LARGE INTESTINE; and CECUM of MAMMALS.
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.
The process of cleaving a chemical compound by the addition of a molecule of water.
Polysaccharides composed of repeating glucose units. They can consist of branched or unbranched chains in any linkages.
A genus of fungi in the family Neocallimasticaceae, order NEOCALLIMASTIGALES. They contain polyflagellate zoospores and grow on a range of simple and complex carbohydrates in the rumen of sheep and cattle.
A species of gram-positive, thermophilic, cellulolytic bacteria in the family Clostridaceae. It degrades and ferments CELLOBIOSE and CELLULOSE to ETHANOL in the CELLULOSOME.
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 exocellulase with specificity for a variety of beta-D-glycoside substrates. It catalyzes the hydrolysis of terminal non-reducing residues in beta-D-glucosides with release of GLUCOSE.
Cellular processes in biosynthesis (anabolism) and degradation (catabolism) of CARBOHYDRATES.
The region of an enzyme that interacts with its substrate to cause the enzymatic reaction.
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.
The relationships of groups of organisms as reflected by their genetic makeup.
Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.
A mitosporic fungal genus frequently found in soil and on wood. It is sometimes used for controlling pathogenic fungi. Its teleomorph is HYPOCREA.
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.
Proteins found in any species of bacterium.
The study of crystal structure using X-RAY DIFFRACTION techniques. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
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.
The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.
Enzymes that catalyze reversibly the formation of an epoxide or arene oxide from a glycol or aromatic diol, respectively.
The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.
A genus of gram-negative, anaerobic, rod-shaped bacteria. Its organisms are normal inhabitants of the oral, respiratory, intestinal, and urogenital cavities of humans, animals, and insects. Some species may be pathogenic.
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.
The outermost layer of a cell in most PLANTS; BACTERIA; FUNGI; and ALGAE. The cell wall is usually a rigid structure that lies external to the CELL MEMBRANE, and provides a protective barrier against physical or chemical agents.
The facilitation of biochemical reactions with the aid of naturally occurring catalysts such as ENZYMES.
A multistage process that includes cloning, physical mapping, subcloning, determination of the DNA SEQUENCE, and information analysis.
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.
Glycosides from plants of the genus DIGITALIS. Some of these are useful as cardiotonic and anti-arrhythmia agents. Included also are semi-synthetic derivatives of the naturally occurring glycosides. The term has sometimes been used more broadly to include all CARDIAC GLYCOSIDES, but here is restricted to those related to Digitalis.
The rate dynamics in chemical or physical systems.
A kingdom of eukaryotic, heterotrophic organisms that live parasitically as saprobes, including MUSHROOMS; YEASTS; smuts, molds, etc. They reproduce either sexually or asexually, and have life cycles that range from simple to complex. Filamentous fungi, commonly known as molds, refer to those that grow as multicellular colonies.
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 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.
A subclass of iridoid compounds that include a glycoside moiety, usually found at the C-1 position.
A genus of motile or nonmotile gram-positive bacteria of the family Clostridiaceae. Many species have been identified with some being pathogenic. They occur in water, soil, and in the intestinal tract of humans and lower animals.
The parts of a macromolecule that directly participate in its specific combination with another molecule.
Enzymes which catalyze the hydrolysis of carboxylic acid esters with the formation of an alcohol and a carboxylic acid anion.
A cardiac glycoside sometimes used in place of DIGOXIN. It has a longer half-life than digoxin; toxic effects, which are similar to those of digoxin, are longer lasting. (From Martindale, The Extra Pharmacopoeia, 30th ed, p665)
A genus of BACILLACEAE that are spore-forming, rod-shaped cells. Most species are saprophytic soil forms with only a few species being pathogenic.
The genetic complement of a BACTERIA as represented in its DNA.
A type of MONOTERPENES, derived from geraniol. They have the general form of cyclopentanopyran, but in some cases, one of the rings is broken as in the case of secoiridoid. They are different from the similarly named iridals (TRITERPENES).
Glucosides are glycosides that contain glucose as the sugar component, often forming part of the plant's defense mechanism and can have various pharmacological effects when extracted and used medically.
Theoretical representations that simulate the behavior or activity of chemical processes or phenomena; includes the use of mathematical equations, computers, and other electronic equipment.
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)
A set of genes descended by duplication and variation from some ancestral gene. Such genes may be clustered together on the same chromosome or dispersed on different chromosomes. Examples of multigene families include those that encode the hemoglobins, immunoglobulins, histocompatibility antigens, actins, tubulins, keratins, collagens, heat shock proteins, salivary glue proteins, chorion proteins, cuticle proteins, yolk proteins, and phaseolins, as well as histones, ribosomal RNA, and transfer RNA genes. The latter three are examples of reiterated genes, where hundreds of identical genes are present in a tandem array. (King & Stanfield, A Dictionary of Genetics, 4th ed)
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.
The above-ground plant without the roots.
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).
Proteins prepared by recombinant DNA technology.
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
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.
A mass spectrometric technique that is used for the analysis of a wide range of biomolecules, such as glycoalkaloids, glycoproteins, polysaccharides, and peptides. Positive and negative fast atom bombardment spectra are recorded on a mass spectrometer fitted with an atom gun with xenon as the customary beam. The mass spectra obtained contain molecular weight recognition as well as sequence information.
Concentrated pharmaceutical preparations of plants obtained by removing active constituents with a suitable solvent, which is evaporated away, and adjusting the residue to a prescribed standard.
C(23)-steroids with methyl groups at C-10 and C-13 and a five-membered lactone at C-17. They are aglycone constituents of CARDIAC GLYCOSIDES and must have at least one double bond in the molecule. The class includes cardadienolides and cardatrienolides. Members include DIGITOXIN and DIGOXIN and their derivatives and the STROPHANTHINS.
The level of protein structure in which regular hydrogen-bond interactions within contiguous stretches of polypeptide chain give rise to alpha helices, beta strands (which align to form beta sheets) or other types of coils. This is the first folding level of protein conformation.
Triterpenes are a class of naturally occurring compounds consisting of six isoprene units arranged to form a 30-carbon skeleton, often found in plants and some animals, with various bioactivities including anti-inflammatory, antiviral, and cytotoxic properties.
A group of 3-hydroxy-4-keto-FLAVONOIDS.
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.
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).
Glucuronidase is an enzyme (specifically, a glycosidase) that catalyzes the hydrolysis of glucuronic acid from various substrates, playing crucial roles in metabolic processes like detoxification and biotransformation within organisms.
An enzyme that catalyzes the conversion of an orthophosphoric monoester and water to an alcohol and orthophosphate. EC 3.1.3.2.
A subclass of iridoid compounds that include a glucoside moiety, usually found at the C-1 position.
Enzymes that catalyze the hydrolysis of N-acylhexosamine residues in N-acylhexosamides. Hexosaminidases also act on GLUCOSIDES; GALACTOSIDES; and several OLIGOSACCHARIDES.
Saturated derivatives of the steroid pregnane. The 5-beta series includes PROGESTERONE and related hormones; the 5-alpha series includes forms generally excreted in the urine.
The location of the atoms, groups or ions relative to one another in a molecule, as well as the number, type and location of covalent bonds.
A cardiotonic glycoside obtained mainly from Digitalis lanata; it consists of three sugars and the aglycone DIGOXIGENIN. Digoxin has positive inotropic and negative chronotropic activity. It is used to control ventricular rate in ATRIAL FIBRILLATION and in the management of congestive heart failure with atrial fibrillation. Its use in congestive heart failure and sinus rhythm is less certain. The margin between toxic and therapeutic doses is small. (From Martindale, The Extra Pharmacopoeia, 30th ed, p666)
An enzyme that catalyzes the hydrolysis of terminal, non-reducing beta-D-mannose residues in beta-D-mannosides. The enzyme plays a role in the lysosomal degradation of the N-glycosylprotein glycans. Defects in the lysosomal form of the enzyme in humans result in a buildup of mannoside intermediate metabolites and the disease BETA-MANNOSIDOSIS.
A plant genus of the family RANUNCULACEAE that contains triterpenoid saponins. Remifemin from C. racemosa is used to suppress LUTEINIZING HORMONE. It is reclassified by some to ACTAEA. The common name of black snakeroot is also used with ASARUM and SANICULA.
A flavonol glycoside found in many plants, including BUCKWHEAT; TOBACCO; FORSYTHIA; HYDRANGEA; VIOLA, etc. It has been used therapeutically to decrease capillary fragility.
Phosphoric acid esters of mannose.
A cardioactive glycoside consisting of rhamnose and ouabagenin, obtained from the seeds of Strophanthus gratus and other plants of the Apocynaceae; used like DIGITALIS. It is commonly used in cell biological studies as an inhibitor of the NA(+)-K(+)-EXCHANGING ATPASE.
An autolytic enzyme bound to the surface of bacterial cell walls. It catalyzes the hydrolysis of the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell wall glycopeptides, particularly peptidoglycan. EC 3.5.1.28.
Hydrolases that specifically cleave the peptide bonds found in PROTEINS and PEPTIDES. Examples of sub-subclasses for this group include EXOPEPTIDASES and ENDOPEPTIDASES.
Root-like underground horizontal stem of plants that produces shoots above and roots below. Distinguished from true roots which don't have buds and nodes. Similar to true roots in being underground and thickened by storage deposits.
A beta-N-Acetylhexosaminidase that catalyzes the hydrolysis of terminal, non-reducing 2-acetamido-2-deoxy-beta-glucose residues in chitobiose and higher analogs as well as in glycoproteins. Has been used widely in structural studies on bacterial cell walls and in the study of diseases such as MUCOLIPIDOSIS and various inflammatory disorders of muscle and connective tissue.
An enzyme that catalyzes the hydrolysis of an alpha L-fucoside to yield an alcohol and L-fucose. Deficiency of this enzyme can cause FUCOSIDOSIS. EC 3.2.1.51.
The buttercup plant family of the order Ranunculales, subclass Magnoliidae, class Magnoliopsida. The leaves are usually alternate and stalkless. The flowers usually have two to five free sepals and may be radially symmetrical or irregular.
A plant genus of the family ASTERACEAE. Members contain stevioside and other sweet diterpene glycosides. The leaf is used for sweetening (SWEETENING AGENTS).
A group of inherited metabolic diseases characterized by the accumulation of excessive amounts of acid mucopolysaccharides, sphingolipids, and/or glycolipids in visceral and mesenchymal cells. Abnormal amounts of sphingolipids or glycolipids are present in neural tissue. INTELLECTUAL DISABILITY and skeletal changes, most notably dysostosis multiplex, occur frequently. (From Joynt, Clinical Neurology, 1992, Ch56, pp36-7)
A type of glycoside widely distributed in plants. Each consists of a sapogenin as the aglycone moiety, and a sugar. The sapogenin may be a steroid or a triterpene and the sugar may be glucose, galactose, a pentose, or a methylpentose.
Enzymes that hydrolyze O-glucosyl-compounds. (Enzyme Nomenclature, 1992) EC 3.2.1.-.
Thiolester hydrolases are enzymes that catalyze the hydrolysis of thioester bonds, commonly found in acetyl-CoA and other coenzyme A derivatives, to produce free carboxylic acids and CoASH.
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 group of FLAVONOLS based on kaempferol. They are derived from naringenin and can be hydroxylated to QUERCETIN or reduced to leucopelargonidin.
Cholestane derivatives containing a fused lactone ring at the 16,17-position and a spiroglycosidic linkage at C-22. Members include sarsaponin, DIOSGENIN and yamogenin.
A hexosaminidase specific for non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides. It acts on GLUCOSIDES; GALACTOSIDES; and several OLIGOSACCHARIDES. Two specific mammalian isoenzymes of beta-N-acetylhexoaminidase are referred to as HEXOSAMINIDASE A and HEXOSAMINIDASE B. Deficiency of the type A isoenzyme causes TAY-SACHS DISEASE, while deficiency of both A and B isozymes causes SANDHOFF DISEASE. The enzyme has also been used as a tumor marker to distinguish between malignant and benign disease.
The sequence of carbohydrates within POLYSACCHARIDES; GLYCOPROTEINS; and GLYCOLIPIDS.
A flavonol widely distributed in plants. It is an antioxidant, like many other phenolic heterocyclic compounds. Glycosylated forms include RUTIN and quercetrin.
A plant genus of the family ASCLEPIADACEAE. This is the true milkweed; APOCYNUM & EUPHORBIA hirta are rarely called milkweed. Asclepias asthmatica has been changed to TYLOPHORA.
A family of galactoside hydrolases that hydrolyze compounds with an O-galactosyl linkage. EC 3.2.1.-.
Glycoside hydrolases that catalyze the hydrolysis of alpha or beta linked MANNOSE.
An exocellulase with specificity for the hydrolysis of 1,4-beta-D-glucosidic linkages in CELLULOSE and cellotetraose. It catalyzes the hydrolysis of terminal non-reducing ends of beta-D-glucosides with release of CELLOBIOSE.
The characteristic 3-dimensional shape of a carbohydrate.
A group of DITERPENES cyclized into four rings.
A group of FLAVONOIDS characterized with a 4-ketone.
Plants whose roots, leaves, seeds, bark, or other constituent parts possess therapeutic, tonic, purgative, curative or other pharmacologic attributes, when administered to man or animals.
The figwort plant family of the order Lamiales. The family is characterized by bisexual flowers with tubular corollas (fused petals) that are bilaterally symmetrical (two-lips) and have four stamens in most, two of which are usually shorter.
Enzymes that catalyze the exohydrolysis of 1,4-alpha-glucosidic linkages with release of alpha-glucose. Deficiency of alpha-1,4-glucosidase may cause GLYCOGEN STORAGE DISEASE TYPE II.
A group of enzymes that catalyze the hydrolysis of diphosphate bonds in compounds such as nucleoside di- and tri-phosphates, and sulfonyl-containing anhydrides such as adenylylsulfate. (Enzyme Nomenclature, 1992) EC 3.6.
An enzyme that catalyzes the active transport system of sodium and potassium ions across the cell wall. Sodium and potassium ions are closely coupled with membrane ATPase which undergoes phosphorylation and dephosphorylation, thereby providing energy for transport of these ions against concentration gradients.
Enzymes that catalyze the hydrolysis of a phenol sulfate to yield a phenol and sulfate. Arylsulfatase A, B, and C have been separated. A deficiency of arylsulfatases is one of the causes of metachromatic leukodystrophy (LEUKODYSTROPHY, METACHROMATIC). EC 3.1.6.1.
Thirteen-carbon butene cyclohexene degradation products formed by the cleavage of CAROTENOIDS. They contribute to the flavor of some FRUIT. Ionone should not be confused with the similarly named ionol.
A group of phenyl benzopyrans named for having structures like FLAVONES.
Disaccharidases are a group of enzymes, including maltase, sucrase, lactase, and trehalase, found primarily in the brush border of the small intestine, responsible for breaking down complex disaccharides into simpler monosaccharides for absorption.
Oligosaccharides containing two monosaccharide units linked by a glycosidic bond.
A plant genus of the family CRASSULACEAE. Members contain rhodioloside. This roseroot is unrelated to the familiar rose (ROSA). Some species in this genus are called stonecrop which is also a common name for SEDUM.
Expanded structures, usually green, of vascular plants, characteristically consisting of a bladelike expansion attached to a stem, and functioning as the principal organ of photosynthesis and transpiration. (American Heritage Dictionary, 2d ed)
A group of enzymes within the class EC 3.6.1.- that catalyze the hydrolysis of diphosphate bonds, chiefly in nucleoside di- and triphosphates. They may liberate either a mono- or diphosphate. EC 3.6.1.-.
Liquid chromatographic techniques which feature high inlet pressures, high sensitivity, and high speed.
A group of lysosomal proteinases or endopeptidases found in aqueous extracts of a variety of animal tissues. They function optimally within an acidic pH range. The cathepsins occur as a variety of enzyme subtypes including SERINE PROTEASES; ASPARTIC PROTEINASES; and CYSTEINE PROTEASES.
Amidohydrolases are enzymes that catalyze the hydrolysis of amides and related compounds, playing a crucial role in various biological processes including the breakdown and synthesis of bioactive molecules.
Enzymes that catalyze the transfer of glycosyl groups to an acceptor. Most often another carbohydrate molecule acts as an acceptor, but inorganic phosphate can also act as an acceptor, such as in the case of PHOSPHORYLASES. Some of the enzymes in this group also catalyze hydrolysis, which can be regarded as transfer of a glycosyl group from the donor to water. Subclasses include the HEXOSYLTRANSFERASES; PENTOSYLTRANSFERASES; SIALYLTRANSFERASES; and those transferring other glycosyl groups. EC 2.4.
Chinese herbal or plant extracts which are used as drugs to treat diseases or promote general well-being. The concept does not include synthesized compounds manufactured in China.
The characteristic three-dimensional shape of a molecule.
Esterases are hydrolase enzymes that catalyze the hydrolysis of ester bonds, converting esters into alcohols and acids, playing crucial roles in various biological processes including metabolism and detoxification.
A class of enzymes involved in the hydrolysis of the N-glycosidic bond of nitrogen-linked sugars.
An intracellular proteinase found in a variety of tissue. It has specificity similar to but narrower than that of pepsin A. The enzyme is involved in catabolism of cartilage and connective tissue. EC 3.4.23.5. (Formerly EC 3.4.4.23).
A genus of fungi in the family Neocallimasticaceae, order NEOCALLIMASTICALES, containing uniflagellate zoospores.
The mint plant family. They are characteristically aromatic, and many of them are cultivated for their oils. Most have square stems, opposite leaves, and two-lipped, open-mouthed, tubular corollas (united petals), with five-lobed, bell-like calyxes (united sepals).
A plant family of the order Lamiales. It is characterized by simple leaves in opposite pairs, cystoliths (enlarged cells containing crystals of calcium carbonate), and bilaterally symmetrical and bisexual flowers that are usually crowded together. The common name for Ruellia of wild petunia is easily confused with PETUNIA.
An enzyme that catalyzes the conversion of acetate esters and water to alcohols and acetate. EC 3.1.1.6.
A plant genus of the family OROBANCHACEAE. Members contain phenylethanoid glycosides.
The usually underground portions of a plant that serve as support, store food, and through which water and mineral nutrients enter the plant. (From American Heritage Dictionary, 1982; Concise Dictionary of Biology, 1990)
An imperfect fungus causing smut or black mold of several fruits, vegetables, etc.
Chromatography on thin layers of adsorbents rather than in columns. The adsorbent can be alumina, silica gel, silicates, charcoals, or cellulose. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
An organophosphate insecticide that inhibits monoamine oxidase and acetylcholinesterase. It has been shown to be genotoxic.
A class of enzymes that transfers substituted phosphate groups. EC 2.7.8.
The morning glory family of flowering plants, of the order Solanales, which includes about 50 genera and at least 1,400 species. Leaves are alternate and flowers are funnel-shaped. Most are twining and erect herbs, with a few woody vines, trees, and shrubs.
Spectrophotometry in the infrared region, usually for the purpose of chemical analysis through measurement of absorption spectra associated with rotational and vibrational energy levels of molecules. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
Chitinase is an enzyme that catalyzes the hydrolysis of chitin, a polysaccharide that makes up the exoskeleton of insects and the cell walls of fungi, into simpler sugars.
The Madder plant family of the order Rubiales, subclass Asteridae, class Magnoliopsida includes important medicinal plants that provide QUININE; IPECAC; and COFFEE. They have opposite leaves and interpetiolar stipules.
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.
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)
A xylosidase that catalyses the random hydrolysis of 1,3-beta-D-xylosidic linkages in 1,3-beta-D-xylans.
Flammable, amorphous, vegetable products of secretion or disintegration, usually formed in special cavities of plants. They are generally insoluble in water and soluble in alcohol, carbon tetrachloride, ether, or volatile oils. They are fusible and have a conchoidal fracture. They are the oxidation or polymerization products of the terpenes, and are mixtures of aromatic acids and esters. Most are soft and sticky, but harden after exposure to cold. (From Grant & Hackh's Chemical Dictionary, 5th ed & Dorland, 28th ed)
A plant genus of the family RUBIACEAE. Members contain genepin, from which geniposide is obtained for use as a crosslinking agent in ADHESIVES, and 3-caffeoyl-4-sinapoylquinic acid.
An endocellulase with specificity for the hydrolysis of 1,3-beta-D-glucosidic linkages in 1,3-beta-D-glucans including laminarin, paramylon, and pachyman.
The phenomenon whereby compounds whose molecules have the same number and kind of atoms and the same atomic arrangement, but differ in their spatial relationships. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 5th ed)
A plant genus of the family CORNACEAE. It is widely cultivated for the attractive flowers.
A plant genus of the family MYRTACEAE that bears an edible fruit and contains guavin B and quercetin glycosides.
A plant genus of the family ASCLEPIADACEAE. Members contain steroidal glycosides and cytotoxic phenanthroindolizidine N-oxide alkaloids.
Polyacenes with four ortho-fused benzene rings in a straight linear arrangement. This group is best known for the subclass called TETRACYCLINES.

N-Linked glycosylation and sialylation of the acid-labile subunit. Role in complex formation with insulin-like growth factor (IGF)-binding protein-3 and the IGFs. (1/4049)

Over 75% of the circulating insulin-like growth factors (IGF-I and -II) are bound in 140-kDa ternary complexes with IGF-binding protein-3 (IGFBP-3) and the 84-86-kDa acid-labile subunit (ALS), a glycoprotein containing 20 kDa of carbohydrate. The ternary complexes regulate IGF availability to the tissues. Since interactions of glycoproteins can be influenced by their glycan moieties, this study aimed to determine the role of ALS glycosylation in ternary complex formation. Complete deglycosylation abolished the ability of ALS to associate with IGFBP-3. To examine this further, seven recombinant ALS mutants each lacking one of the seven glycan attachment sites were expressed in CHO cells. All the mutants bound IGFBP-3, demonstrating that this interaction is not dependent on any single glycan chain. Enzymatic desialylation of ALS caused a shift in isoelectric point from 4.5 toward 7, demonstrating a substantial contribution of anionic charge by sialic acid. Ionic interactions are known to be involved in the association between ALS and IGFBP-3. Desialylation reduced the affinity of ALS for IGFBP-3. IGF complexes by 50-80%. Since serum protein glycosylation is often modified in disease states, the dependence of IGF ternary complex formation on the glycosylation state of ALS suggests a novel mechanism for regulation of IGF bioavailability.  (+info)

The structure of a glycopeptide (GP-II) isolated from Rhizopus saccharogenic amylase. (2/4049)

Mild alkaline treatment of glycopeptide (GP-II) resulted in the loss of 1 mole of serine and 5 moles of threonine per mole of GP-II, suggesting the presence of O-glycosyl bonds between 1 serine and 5 threonine residues and carbohydrate chains. Treatment of GP-II with alkaline borohydride released only disaccharide. Methylation studies of the carbohydrate moiety gave 2,3,4,6-tetra-O-methyl and 2,4,6-tri-O-methyl derivatives of mannose in a ratio of approximately 1:1. In addition, one step of Smith degradation resulted in the loss of about 6 residues of mannose per mole of GP-II. Moreover, alpha-mannosidase [EC 3.2.1.24] liberated about 6 residles of mannose per mole of GP-II. On the basis of these data, the structure of the carbohydrate moiety of GP-II was confirmed to be 3-O-alpha-mannosylmannose. The amino- and carboxyl-terminal amino acids of GP-II were determined to be threonine and serine, respectively. On reductive cleavage of N-proline bonds with metallic sodium in liquid ammonia, 2 moles of alanine per mole of GP-II were lost. From the compositions of three fragments isolated from the reductive cleavage products, the amino acid sequence of the peptide portion of GP-II was determined. Based on these data, a probable structure was proposed for GP-II.  (+info)

Relationship between glycosyl hydrolase inventory and growth physiology of the hyperthermophile Pyrococcus furiosus on carbohydrate-based media. (3/4049)

Utilization of a range of carbohydrates for growth by the hyperthermophile Pyrococcus furiosus was investigated by examining the spectrum of glycosyl hydrolases produced by this microorganism and the thermal labilities of various saccharides. Previously, P. furiosus had been found to grow in batch cultures on several alpha-linked carbohydrates and cellobiose but not on glucose or other beta-linked sugars. Although P. furiosus was not able to grow on any nonglucan carbohydrate or any form of cellulose in this study (growth on oat spelt arabinoxylan was attributed to glucan contamination of this substrate), significant growth at 98 degrees C occurred on beta-1,3- and beta-1,3-beta-1,4-linked glucans. Oligosaccharides generated by digestion with a recombinant laminarinase derived from P. furiosus were the compounds that were most effective in stimulating growth of the microorganism. In several cases, periodic addition of beta-glucan substrates to fed-batch cultures limited adverse thermochemical modifications of the carbohydrates (i.e., Maillard reactions and caramelization) and led to significant increases (as much as two- to threefold) in the cell yields. While glucose had only a marginally positive effect on growth in batch culture, the final cell densities nearly tripled when glucose was added by the fed-batch procedure. Nonenzymatic browning reactions were found to be significant at 98 degrees C for saccharides with degrees of polymerization (DP) ranging from 1 to 6; glucose was the most labile compound on a mass basis and the least labile compound on a molar basis. This suggests that for DP of 2 or greater protection of the nonreducing monosaccharide component may be a factor in substrate availability. For P. furiosus, carbohydrate utilization patterns were found to reflect the distribution of the glycosyl hydrolases which are known to be produced by this microorganism.  (+info)

Rapid identification of Actinomycetaceae and related bacteria. (4/4049)

Identification of new isolates belonging to the family Actinomycetaceae requires extensive numbers of biochemical tests, supplemented with gas-liquid chromatography determination of fermentation end products and, often, analysis of cell wall composition. This paper describes the results of the testing of 162 strains of Actinomycetaceae and related taxa for 20 different enzymatic activities including phosphatases, esterases, aminopeptidases, and glycosidases. The results of all tests were read after 4 h of incubation. The results obtained in the study provide significant new information on the biochemical properties of these groups of bacteria. An identification scheme based upon 13 selected tests, which allow the identification of these groups of bacteria within 4 h, is proposed.  (+info)

Purification and characterization of Aspergillus ficuum endoinulinase. (5/4049)

Endoinulinase from Aspergillus ficuum, which catalyzes the hydrolysis of inulin via an endo-cleavage mode, was purified by chromatography from Novozym 230 as a starting commercial enzyme mixture on CM-Sephadex and DEAE-Sepharose, and by preparative electrophoresis under native conditions. The enzyme was estimated to be pure on the basis of its I/S ratio, whose value was infinite in our assay conditions. Two forms separated by using this method. SDS gel electrophoresis showed the two purified forms to respectively exhibit molecular weights of 64,000 +/- 500 and 66,000 +/- 1,000. The results of deglycosylation indicated that the two forms were originally the same protein but with different sugar contents. A molecular weight of 54,800 +/- 1,500 was found by gel filtration of the native enzyme, indicating the native functional protein to be a monomer. The enzyme showed nearly absolute substrate specificity towards inulin and inulooligosaccharides, and acted via an endo-attack to produce mainly inulotriose during the late stage of the reaction. The apparent Km and Vmax values for inulin hydrolysis were 8.1 +/- 1.0 mM and 773 +/- 60 U/mg, respectively. The internal peptides of the enzyme showed sequence homology to the endoinulinase of Penicillium purpurogenum.  (+info)

Insertion analysis of putative functional elements in the promoter region of the Aspergillus oryzae Taka-amylase A gene (amyB) using a heterologous Aspergillus nidulans amdS-lacZ fusion gene system. (6/4049)

Expression of the Taka-amylase A gene (amyB) of Aspergillus oryzae is induced by starch or maltose. The A. oryzae amyB gene promoter contains three highly conserved sequences, designated Regions I, II, and III, compared with promoter regions of the A. oryzae glaA encoding glucoamylase and the agdA encoding alpha-glucosidase. To identify the function of these sequences within the amyB promoter, various fragments containing conserved sequences in the amyB promoter were introduced into the upstream region of the heterologous A. nidulans amdS gene (encoding acetamidase) fused to the Escherichia coli lacZ gene as a reporter. Introduction of the sequence between -290 to -233 (the number indicates the distance in base pairs from the translation initiation point (+1)) containing Region III significantly increased the expression of the lacZ reporter gene in the presence of maltose. The sequence between -377 to -290 containing Region I also increased the lacZ activity, but its maltose inducibility was less than that of Region III. The sequence between -233 to -181 containing Region II had no effect on the expression. These results indicated that Region III is most likely involved in the maltose induction of the amyB gene expression.  (+info)

A single limit dextrinase gene is expressed both in the developing endosperm and in germinated grains of barley. (7/4049)

The single gene encoding limit dextrinase (pullulan 6-glucanohydrolase; EC 3.2.1.41) in barley (Hordeum vulgare) has 26 introns that range in size from 93 to 822 base pairs. The mature polypeptide encoded by the gene has 884 amino acid residues and a calculated molecular mass of 97,417 D. Limit dextrinase mRNA is abundant in gibberellic acid-treated aleurone layers and in germinated grain. Gibberellic acid response elements were found in the promoter region of the gene. These observations suggest that the enzyme participates in starch hydrolysis during endosperm mobilization in germinated grain. The mRNA encoding the enzyme is present at lower levels in the developing endosperm of immature grain, a location consistent with a role for limit dextrinase in starch synthesis. Enzyme activity was also detected in developing grain. The limit dextrinase has a presequence typical of transit peptides that target nascent polypeptides to amyloplasts, but this would not be expected to direct secretion of the mature enzyme from aleurone cells in germinated grain. It remains to be discovered how the enzyme is released from the aleurone and whether another enzyme, possibly of the isoamylase group, might be equally important for starch hydrolysis in germinated grain.  (+info)

Characterization of the divergent sacBK and sacAR operons, involved in sucrose utilization by Lactococcus lactis. (8/4049)

The divergently transcribed sacBK and sacAR operons, which are involved in the utilization of sucrose by Lactococcus lactis NZ9800, were examined by transcriptional and gene inactivation studies. Northern analyses of RNA isolated from cells grown at the expense of different carbon sources revealed three sucrose-inducible transcripts: one of 3.2 kb containing sacB and sacK, a second of 3.4 kb containing sacA and sacR, and a third of 1.8 kb containing only sacR. The inactivation of the sacR gene by replacement recombination resulted in the constitutive transcription of the sacBK and sacAR operons in the presence of different carbon sources, indicating that SacR acts as a repressor of transcription.  (+info)

Glycoside hydrolases are a class of enzymes that catalyze the hydrolysis of glycosidic bonds found in various substrates such as polysaccharides, oligosaccharides, and glycoproteins. These enzymes break down complex carbohydrates into simpler sugars by cleaving the glycosidic linkages that connect monosaccharide units.

Glycoside hydrolases are classified based on their mechanism of action and the type of glycosidic bond they hydrolyze. The classification system is maintained by the International Union of Biochemistry and Molecular Biology (IUBMB). Each enzyme in this class is assigned a unique Enzyme Commission (EC) number, which reflects its specificity towards the substrate and the type of reaction it catalyzes.

These enzymes have various applications in different industries, including food processing, biofuel production, pulp and paper manufacturing, and biomedical research. In medicine, glycoside hydrolases are used to diagnose and monitor certain medical conditions, such as carbohydrate-deficient glycoprotein syndrome, a rare inherited disorder affecting the structure of glycoproteins.

Glycosides are organic compounds that consist of a glycone (a sugar component) linked to a non-sugar component, known as an aglycone, via a glycosidic bond. They can be found in various plants, microorganisms, and some animals. Depending on the nature of the aglycone, glycosides can be classified into different types, such as anthraquinone glycosides, cardiac glycosides, and saponin glycosides.

These compounds have diverse biological activities and pharmacological effects. For instance:

* Cardiac glycosides, like digoxin and digitoxin, are used in the treatment of heart failure and certain cardiac arrhythmias due to their positive inotropic (contractility-enhancing) and negative chronotropic (heart rate-slowing) effects on the heart.
* Saponin glycosides have potent detergent properties and can cause hemolysis (rupture of red blood cells). They are used in various industries, including cosmetics and food processing, and have potential applications in drug delivery systems.
* Some glycosides, like amygdalin found in apricot kernels and bitter almonds, can release cyanide upon hydrolysis, making them potentially toxic.

It is important to note that while some glycosides have therapeutic uses, others can be harmful or even lethal if ingested or otherwise introduced into the body in large quantities.

Hydrolases are a class of enzymes that help facilitate the breakdown of various types of chemical bonds through a process called hydrolysis, which involves the addition of water. These enzymes catalyze the cleavage of bonds in substrates by adding a molecule of water, leading to the formation of two or more smaller molecules.

Hydrolases play a crucial role in many biological processes, including digestion, metabolism, and detoxification. They can act on a wide range of substrates, such as proteins, lipids, carbohydrates, and nucleic acids, breaking them down into smaller units that can be more easily absorbed or utilized by the body.

Examples of hydrolases include:

1. Proteases: enzymes that break down proteins into smaller peptides or amino acids.
2. Lipases: enzymes that hydrolyze lipids, such as triglycerides, into fatty acids and glycerol.
3. Amylases: enzymes that break down complex carbohydrates, like starches, into simpler sugars, such as glucose.
4. Nucleases: enzymes that cleave nucleic acids, such as DNA or RNA, into smaller nucleotides or oligonucleotides.
5. Phosphatases: enzymes that remove phosphate groups from various substrates, including proteins and lipids.
6. Esterases: enzymes that hydrolyze ester bonds in a variety of substrates, such as those found in some drugs or neurotransmitters.

Hydrolases are essential for maintaining proper cellular function and homeostasis, and their dysregulation can contribute to various diseases and disorders.

"Cellvibrio" is a genus of bacteria that belongs to the family of Oxalobacteraceae. These bacteria are gram-negative, facultatively anaerobic rods that are commonly found in various environments such as soil, water, and plant material. They are known for their ability to degrade complex organic compounds, including polysaccharides like cellulose and xylan. Some species of Cellvibrio have potential applications in biotechnology and bioenergy production due to their ability to produce enzymes that can break down plant biomass into fermentable sugars. However, there is no specific medical definition or association with human diseases for the genus "Cellvibrio".

Cardiac glycosides are a group of naturally occurring compounds that have a toxic effect on the heart. They are found in certain plants, including foxglove and lily of the valley, as well as in some toads and beetles. The most well-known cardiac glycoside is digoxin, which is derived from the foxglove plant and is used as a medication to treat heart failure and atrial arrhythmias.

Cardiac glycosides work by inhibiting the sodium-potassium pump in heart muscle cells, leading to an increase in intracellular calcium levels. This increases the force of heart contractions, which can be beneficial in treating heart failure. However, if the dose is too high, cardiac glycosides can also cause dangerous arrhythmias and even death.

It's important for healthcare professionals to carefully monitor patients taking cardiac glycosides, as the therapeutic and toxic doses are very close together. Additionally, certain medications and medical conditions can interact with cardiac glycosides and increase the risk of toxicity.

Cellulases are a group of enzymes that break down cellulose, which is a complex carbohydrate and the main structural component of plant cell walls. These enzymes are produced by various organisms, including bacteria, fungi, and protozoa. They play an important role in the natural decomposition process and have various industrial applications, such as in the production of biofuels, paper, and textiles.

Cellulases work by hydrolyzing the beta-1,4 glycosidic bonds between the glucose molecules that make up cellulose, breaking it down into simpler sugars like glucose. This process is known as saccharification. The specific type of cellulase enzyme determines where on the cellulose molecule it will cleave the bond.

There are three main types of cellulases: endoglucanases, exoglucanases, and beta-glucosidases. Endoglucanases randomly attack internal bonds in the amorphous regions of cellulose, creating new chain ends for exoglucanases to act on. Exoglucanases (also known as cellobiohydrolases) cleave cellobiose units from the ends of the cellulose chains, releasing cellobiose or glucose. Beta-glucosidases convert cellobiose into two molecules of glucose, which can then be further metabolized by the organism.

In summary, cellulases are a group of enzymes that break down cellulose into simpler sugars through hydrolysis. They have various industrial applications and play an essential role in natural decomposition processes.

Cellulase is a type of enzyme that breaks down cellulose, which is a complex carbohydrate and the main structural component of plant cell walls. Cellulases are produced by certain bacteria, fungi, and protozoans, and are used in various industrial applications such as biofuel production, food processing, and textile manufacturing. In the human body, there are no known physiological roles for cellulases, as humans do not produce these enzymes and cannot digest cellulose.

Endo-1,4-beta Xylanases are a type of enzyme that catalyze the endohydrolysis of 1,4-beta-D-xylosidic linkages in xylans, which are complex polysaccharides made up of beta-1,4-linked xylose residues. Xylan is a major hemicellulose component found in the cell walls of plants, and endo-1,4-beta Xylanases play an important role in the breakdown and digestion of plant material by various organisms, including bacteria, fungi, and animals. These enzymes are widely used in industrial applications, such as biofuel production, food processing, and pulp and paper manufacturing, to break down xylans and improve the efficiency of various processes.

Xylosidases are a group of enzymes that catalyze the hydrolysis of xylosides, which are glycosides with a xylose sugar. Specifically, they cleave the terminal β-1,4-linked D-xylopyranoside residues from various substrates such as xylooligosaccharides and xylan. These enzymes play an important role in the breakdown and metabolism of plant-derived polysaccharides, particularly hemicelluloses, which are a major component of plant biomass. Xylosidases have potential applications in various industrial processes, including biofuel production and animal feed manufacturing.

Xylans are a type of complex carbohydrate, specifically a hemicellulose, that are found in the cell walls of many plants. They are made up of a backbone of beta-1,4-linked xylose sugar molecules and can be substituted with various side groups such as arabinose, glucuronic acid, and acetyl groups. Xylans are indigestible by humans, but they can be broken down by certain microorganisms in the gut through a process called fermentation, which can produce short-chain fatty acids that have beneficial effects on health.

Fibrobacter is a genus of anaerobic, gram-negative bacteria that primarily resides in the gastrointestinal tracts of ruminants and other herbivorous animals. These bacteria are specialized in breaking down complex plant fibers, such as cellulose and xylan, into simpler sugars through fermentation. This process plays a crucial role in the digestion and nutrient acquisition from plant-based diets in these animals.

In human medicine, Fibrobacter species have been found in the oral cavity and gastrointestinal tract, but their significance in human health and disease is not well understood. Some studies suggest that an increased abundance of Fibrobacter may be associated with certain gut disorders like irritable bowel syndrome or inflammatory bowel disease; however, more research is needed to establish a clear relationship and understand the underlying mechanisms.

"Alteromonas" is a genus of gram-negative, aerobic bacteria that are commonly found in marine environments. These bacteria are known for their ability to produce various enzymes and metabolites that allow them to adapt to and thrive in the diverse conditions found in the ocean. Some species of Alteromonas have been shown to have potential applications in bioremediation, as they are able to break down oil and other pollutants. They may also play a role in carbon cycling in the ocean, as they are capable of utilizing various organic compounds as a source of energy.

It's important to note that while Alteromonas species are generally not harmful to humans, some strains have been found to be opportunistic pathogens, causing infections in individuals with weakened immune systems. However, such cases are relatively rare.

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.

Cellulosomes are large, complex enzymatic structures produced by certain anaerobic bacteria that allow them to break down and consume cellulose, a major component of plant biomass. These structures are composed of multiple enzymes that work together in a coordinated manner to degrade cellulose into simpler sugars, which the bacteria can then use as a source of energy and carbon.

The individual enzymes in a cellulosome are non-covalently associated with a central scaffoldin protein, forming a multi-enzyme complex. The scaffoldin protein contains cohesin modules that bind to dockerin modules on the enzyme subunits, creating a highly organized and stable structure.

Cellulosomes have been identified in several species of anaerobic bacteria, including members of the genera Clostridium and Ruminococcus. They are thought to play a key role in the global carbon cycle by breaking down plant material and releasing carbon dioxide back into the atmosphere.

Cellulose is a complex carbohydrate that is the main structural component of the cell walls of green plants, many algae, and some fungi. It is a polysaccharide consisting of long chains of beta-glucose molecules linked together by beta-1,4 glycosidic bonds. Cellulose is insoluble in water and most organic solvents, and it is resistant to digestion by humans and non-ruminant animals due to the lack of cellulase enzymes in their digestive systems. However, ruminants such as cows and sheep can digest cellulose with the help of microbes in their rumen that produce cellulase.

Cellulose has many industrial applications, including the production of paper, textiles, and building materials. It is also used as a source of dietary fiber in human food and animal feed. Cellulose-based materials are being explored for use in biomedical applications such as tissue engineering and drug delivery due to their biocompatibility and mechanical properties.

Ruminococcus is a genus of obligate anaerobic, gram-positive bacteria that are commonly found in the gastrointestinal tracts of humans and other animals. These bacteria play a crucial role in breaking down complex carbohydrates and fibers in the gut through fermentation, producing short-chain fatty acids (SCFAs) as byproducts. Ruminococcus species are particularly abundant in the rumen of ruminants such as cows and sheep, where they help to digest plant material. In humans, Ruminococcus species have been associated with various aspects of health and disease, including gut inflammation, colon cancer, and metabolic disorders. However, more research is needed to fully understand the complex relationship between these bacteria and human health.

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.

Hydrolysis is a chemical process, not a medical one. However, it is relevant to medicine and biology.

Hydrolysis is the breakdown of a chemical compound due to its reaction with water, often resulting in the formation of two or more simpler compounds. In the context of physiology and medicine, hydrolysis is a crucial process in various biological reactions, such as the digestion of food molecules like proteins, carbohydrates, and fats. Enzymes called hydrolases catalyze these hydrolysis reactions to speed up the breakdown process in the body.

Glucans are polysaccharides (complex carbohydrates) that are made up of long chains of glucose molecules. They can be found in the cell walls of certain plants, fungi, and bacteria. In medicine, beta-glucans derived from yeast or mushrooms have been studied for their potential immune-enhancing effects. However, more research is needed to fully understand their role and effectiveness in human health.

Neocallimastix is a genus of anaerobic fungi that are commonly found in the digestive tracts of herbivorous mammals and birds, where they play a crucial role in breaking down complex plant material into simpler compounds that can be absorbed and utilized by their hosts. These fungi are characterized by their ability to produce enzymes that can break down cellulose, hemicellulose, and lignin, the major structural components of plant cell walls. Under a microscope, Neocallimastix species appear as branching, septate hyphae with rounded or pointed ends, and they reproduce by forming spores within specialized structures called sporangia.

'Clostridium thermocellum' is a type of anaerobic, gram-positive bacterium that is known for its ability to produce cellulases and break down cellulose. It is thermophilic, meaning it grows optimally at higher temperatures, typically between 55-70°C. This organism is of interest in the field of bioenergy because of its potential to convert plant biomass into useful products such as biofuels. However, it's important to note that this bacterium can also produce harmful metabolic byproducts and can be potentially pathogenic to humans.

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.

Beta-glucosidase is an enzyme that breaks down certain types of complex sugars, specifically those that contain a beta-glycosidic bond. This enzyme is found in various organisms, including humans, and plays a role in the digestion of some carbohydrates, such as cellulose and other plant-based materials.

In the human body, beta-glucosidase is produced by the lysosomes, which are membrane-bound organelles found within cells that help break down and recycle various biological molecules. Beta-glucosidase is involved in the breakdown of glycolipids and gangliosides, which are complex lipids that contain sugar molecules.

Deficiencies in beta-glucosidase activity can lead to certain genetic disorders, such as Gaucher disease, in which there is an accumulation of glucocerebrosidase, a type of glycolipid, within the lysosomes. This can result in various symptoms, including enlargement of the liver and spleen, anemia, and bone pain.

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.

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.

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.

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.

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.

Trichoderma is a genus of fungi that are commonly found in soil, decaying wood, and other organic matter. While there are many different species of Trichoderma, some of them have been studied for their potential use in various medical and industrial applications. For example, certain Trichoderma species have been shown to have antimicrobial properties and can be used to control plant diseases. Other species are being investigated for their ability to produce enzymes and other compounds that may have industrial or medicinal uses.

However, it's important to note that not all Trichoderma species are beneficial, and some of them can cause infections in humans, particularly in individuals with weakened immune systems. These infections can be difficult to diagnose and treat, as they often involve multiple organ systems and may require aggressive antifungal therapy.

In summary, Trichoderma is a genus of fungi that can have both beneficial and harmful effects on human health, depending on the specific species involved and the context in which they are encountered.

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.

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.

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.

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.

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.

Epoxide hydrolases are a group of enzymes that catalyze the hydrolysis of epoxides, which are molecules containing a three-membered ring consisting of two carbon atoms and one oxygen atom. This reaction results in the formation of diols, which are molecules containing two hydroxyl groups (-OH).

Epoxide hydrolases play an important role in the detoxification of xenobiotics (foreign substances) and the metabolism of endogenous compounds. They help to convert toxic epoxides into less harmful products, which can then be excreted from the body.

There are two main types of epoxide hydrolases: microsomal epoxide hydrolase (mEH) and soluble epoxide hydrolase (sEH). mEH is primarily responsible for metabolizing xenobiotics, while sEH plays a role in the metabolism of endogenous compounds such as arachidonic acid.

Impaired function or inhibition of epoxide hydrolases has been linked to various diseases, including cancer, cardiovascular disease, and neurological disorders. Therefore, these enzymes are considered important targets for the development of drugs and therapies aimed at treating these conditions.

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.

Bacteroides are a genus of gram-negative, anaerobic, rod-shaped bacteria that are normally present in the human gastrointestinal tract. They are part of the normal gut microbiota and play an important role in breaking down complex carbohydrates and other substances in the gut. However, some species of Bacteroides can cause opportunistic infections, particularly in individuals with weakened immune systems or when they spread to other parts of the body. They are resistant to many commonly used antibiotics, making infections caused by these bacteria difficult to treat.

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.

A cell wall is a rigid layer found surrounding the plasma membrane of plant cells, fungi, and many types of bacteria. It provides structural support and protection to the cell, maintains cell shape, and acts as a barrier against external factors such as chemicals and mechanical stress. The composition of the cell wall varies among different species; for example, in plants, it is primarily made up of cellulose, hemicellulose, and pectin, while in bacteria, it is composed of peptidoglycan.

Biocatalysis is the use of living organisms or their components, such as enzymes, to accelerate chemical reactions. In other words, it is the process by which biological systems, including cells, tissues, and organs, catalyze chemical transformations. Biocatalysts, such as enzymes, can increase the rate of a reaction by lowering the activation energy required for the reaction to occur. They are highly specific and efficient, making them valuable tools in various industries, including pharmaceuticals, food and beverage, and biofuels.

In medicine, biocatalysis is used in the production of drugs, such as antibiotics and hormones, as well as in diagnostic tests. Enzymes are also used in medical treatments, such as enzyme replacement therapy for genetic disorders that affect enzyme function. Overall, biocatalysis plays a critical role in many areas of medicine and healthcare.

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.

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.

Digitalis glycosides are a type of cardiac glycoside that are derived from the foxglove plant (Digitalis purpurea) and related species. These compounds have a steroidal structure with a lactone ring attached to the molecule, which is responsible for their positive inotropic effects on the heart.

The two main digitalis glycosides used clinically are digoxin and digitoxin. They work by inhibiting the sodium-potassium pump in cardiac muscle cells, leading to an increase in intracellular calcium levels and a subsequent enhancement of myocardial contractility. This makes them useful in the treatment of heart failure and atrial arrhythmias such as atrial fibrillation.

However, digitalis glycosides have a narrow therapeutic index, meaning that there is only a small difference between their therapeutic and toxic doses. Therefore, they must be administered with caution and patients should be closely monitored for signs of toxicity such as nausea, vomiting, visual disturbances, and cardiac arrhythmias.

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.

Fungi, in the context of medical definitions, are a group of eukaryotic organisms that include microorganisms such as yeasts and molds, as well as the more familiar mushrooms. The study of fungi is known as mycology.

Fungi can exist as unicellular organisms or as multicellular filamentous structures called hyphae. They are heterotrophs, which means they obtain their nutrients by decomposing organic matter or by living as parasites on other organisms. Some fungi can cause various diseases in humans, animals, and plants, known as mycoses. These infections range from superficial, localized skin infections to systemic, life-threatening invasive diseases.

Examples of fungal infections include athlete's foot (tinea pedis), ringworm (dermatophytosis), candidiasis (yeast infection), histoplasmosis, coccidioidomycosis, and aspergillosis. Fungal infections can be challenging to treat due to the limited number of antifungal drugs available and the potential for drug resistance.

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.

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.

Iridoid glycosides are a type of naturally occurring compounds that are found in various plants, including the Lamiaceae (mint) family and the Plantaginaceae (plantain) family. These compounds consist of an iridoid moiety, which is a cyclic molecule derived from the terpene iridodial, linked to a sugar group. Iridoid glycosides have been studied for their potential medicinal properties, including anti-inflammatory, antispasmodic, and analgesic effects. Some examples of plants that contain iridoid glycosides include gardenia, olive, and valerian. It is important to note that while some iridoid glycosides have been found to have medicinal benefits, others may be toxic in high concentrations, so it is essential to use them under the guidance of a healthcare professional.

'Clostridium' is a genus of gram-positive, rod-shaped bacteria that are widely distributed in nature, including in soil, water, and the gastrointestinal tracts of animals and humans. Many species of Clostridium are anaerobic, meaning they can grow and reproduce in environments with little or no oxygen. Some species of Clostridium are capable of producing toxins that can cause serious and sometimes life-threatening illnesses in humans and animals.

Some notable species of Clostridium include:

* Clostridium tetani, which causes tetanus (also known as lockjaw)
* Clostridium botulinum, which produces botulinum toxin, the most potent neurotoxin known and the cause of botulism
* Clostridium difficile, which can cause severe diarrhea and colitis, particularly in people who have recently taken antibiotics
* Clostridium perfringens, which can cause food poisoning and gas gangrene.

It is important to note that not all species of Clostridium are harmful, and some are even beneficial, such as those used in the production of certain fermented foods like sauerkraut and natto. However, due to their ability to produce toxins and cause illness, it is important to handle and dispose of materials contaminated with Clostridium species carefully, especially in healthcare settings.

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.

Carboxylic ester hydrolases are a class of enzymes that catalyze the hydrolysis of ester bonds in carboxylic acid esters, producing alcohols and carboxylates. This group includes several subclasses of enzymes such as esterases, lipases, and thioesterases. These enzymes play important roles in various biological processes, including metabolism, detoxification, and signal transduction. They are widely used in industrial applications, such as the production of biodiesel, pharmaceuticals, and food ingredients.

Digitoxin is a cardiac glycoside drug that is derived from the foxglove plant (Digitalis lanata). It is used in the treatment of various heart conditions, particularly congestive heart failure and certain types of arrhythmias. Digitoxin works by increasing the force of heart muscle contractions and slowing the heart rate, which helps to improve the efficiency of the heart's pumping action.

Like other cardiac glycosides, digitoxin inhibits the sodium-potassium pump in heart muscle cells, leading to an increase in intracellular calcium levels and a strengthening of heart muscle contractions. However, digitoxin has a longer half-life than other cardiac glycosides such as digoxin, which means that it stays in the body for a longer period of time and may require less frequent dosing.

Digitoxin is available in tablet form and is typically prescribed at a low dose, with regular monitoring of blood levels to ensure safe and effective use. Common side effects of digitoxin include nausea, vomiting, diarrhea, and dizziness. In rare cases, it can cause more serious side effects such as arrhythmias or toxicity, which may require hospitalization and treatment with medications or other interventions.

'Bacillus' is a genus of rod-shaped, gram-positive bacteria that are commonly found in soil, water, and the gastrointestinal tracts of animals. Many species of Bacillus are capable of forming endospores, which are highly resistant to heat, radiation, and chemicals, allowing them to survive for long periods in harsh environments. The most well-known species of Bacillus is B. anthracis, which causes anthrax in animals and humans. Other species of Bacillus have industrial or agricultural importance, such as B. subtilis, which is used in the production of enzymes and antibiotics.

A bacterial genome is the complete set of genetic material, including both DNA and RNA, found within a single bacterium. It contains all the hereditary information necessary for the bacterium to grow, reproduce, and survive in its environment. The bacterial genome typically includes circular chromosomes, as well as plasmids, which are smaller, circular DNA molecules that can carry additional genes. These genes encode various functional elements such as enzymes, structural proteins, and regulatory sequences that determine the bacterium's characteristics and behavior.

Bacterial genomes vary widely in size, ranging from around 130 kilobases (kb) in Mycoplasma genitalium to over 14 megabases (Mb) in Sorangium cellulosum. The complete sequencing and analysis of bacterial genomes have provided valuable insights into the biology, evolution, and pathogenicity of bacteria, enabling researchers to better understand their roles in various diseases and potential applications in biotechnology.

Iridoids are a type of naturally occurring compounds that are widely distributed in the plant kingdom. They are characterized by the presence of a cyclopentanoid structure fused to a monoterpene unit. Iridoids have a wide range of biological activities, including anti-inflammatory, analgesic, and antioxidant effects. Some iridoids also have potential therapeutic benefits in the treatment of various diseases, such as cancer and neurodegenerative disorders.

In a medical context, iridoids may be mentioned in relation to their presence in certain medicinal plants or herbs used in traditional medicine, or in research investigating their potential pharmacological properties. However, it is important to note that the use of iridoid-containing plants or supplements should only be done under the guidance of a qualified healthcare professional, as with any medical treatment.

Glucosides are chemical compounds that consist of a glycosidic bond between a sugar molecule (typically glucose) and another non-sugar molecule, which can be an alcohol, phenol, or steroid. They occur naturally in various plants and some microorganisms.

Glucosides are not medical terms per se, but they do have significance in pharmacology and toxicology because some of them may release the sugar portion upon hydrolysis, yielding aglycone, which can have physiological effects when ingested or absorbed into the body. Some glucosides are used as medications or dietary supplements due to their therapeutic properties, while others can be toxic if consumed in large quantities.

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.

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.

A multigene family is a group of genetically related genes that share a common ancestry and have similar sequences or structures. These genes are arranged in clusters on a chromosome and often encode proteins with similar functions. They can arise through various mechanisms, including gene duplication, recombination, and transposition. Multigene families play crucial roles in many biological processes, such as development, immunity, and metabolism. Examples of multigene families include the globin genes involved in oxygen transport, the immune system's major histocompatibility complex (MHC) genes, and the cytochrome P450 genes associated with drug metabolism.

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.

Aerial parts of plants refer to the above-ground portions of a plant, including leaves, stems, flowers, and fruits. These parts are often used in medicine, either in their entirety or as isolated extracts, to take advantage of their medicinal properties. The specific components of aerial parts that are used in medicine can vary depending on the plant species and the desired therapeutic effects. For example, the leaves of some plants may contain active compounds that have anti-inflammatory or analgesic properties, while the flowers of others may be rich in antioxidants or compounds with sedative effects. In general, aerial parts of plants are used in herbal medicine to treat a wide range of conditions, including respiratory, digestive, and nervous system disorders, as well as skin conditions and infections.

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.

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.

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.

'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.

Fast Atom Bombardment (FAB) Mass Spectrometry is a technique used for determining the mass of ions in a sample. In FAB-MS, the sample is mixed with a matrix material and then bombarded with a beam of fast atoms, usually xenon or cesium. This bombardment leads to the formation of ions from the sample which can then be detected and measured using a mass analyzer. The resulting mass spectrum provides information about the molecular weight and structure of the sample molecules. FAB-MS is particularly useful for the analysis of large, thermally labile, or polar molecules that may not ionize well by other methods.

A plant extract is a preparation containing chemical constituents that have been extracted from a plant using a solvent. The resulting extract may contain a single compound or a mixture of several compounds, depending on the extraction process and the specific plant material used. These extracts are often used in various industries including pharmaceuticals, nutraceuticals, cosmetics, and food and beverage, due to their potential therapeutic or beneficial properties. The composition of plant extracts can vary widely, and it is important to ensure their quality, safety, and efficacy before use in any application.

Cardenolides are a type of steroid compound that are found in certain plants and animals. These compounds have a characteristic structure that includes a five-membered lactone ring, which is attached to a steroid nucleus. Cardenolides are well known for their toxicity to many organisms, including humans, and they have been used for both medicinal and poisonous purposes.

One of the most famous cardenolides is digitoxin, which is derived from the foxglove plant (Digitalis purpurea). Digitoxin has been used as a medication to treat heart conditions such as congestive heart failure, as it can help to strengthen heart contractions and regulate heart rhythm. However, because of its narrow therapeutic index and potential for toxicity, digitoxin is not commonly used today.

Other cardenolides include ouabain, which is found in the seeds of the African plant Acokanthera ouabaio, and bufadienolides, which are found in the skin and parotid glands of toads. These compounds have also been studied for their potential medicinal uses, but they are not widely used in clinical practice due to their toxicity.

It is important to note that cardenolides can be highly toxic to humans and animals, and exposure to these compounds can cause a range of symptoms including nausea, vomiting, diarrhea, seizures, and even death. As such, it is essential to use caution when handling or coming into contact with plants or animals that contain cardenolides.

Secondary protein structure refers to the local spatial arrangement of amino acid chains in a protein, typically described as regular repeating patterns held together by hydrogen bonds. The two most common types of secondary structures are the alpha-helix (α-helix) and the beta-pleated sheet (β-sheet). In an α-helix, the polypeptide chain twists around itself in a helical shape, with each backbone atom forming a hydrogen bond with the fourth amino acid residue along the chain. This forms a rigid rod-like structure that is resistant to bending or twisting forces. In β-sheets, adjacent segments of the polypeptide chain run parallel or antiparallel to each other and are connected by hydrogen bonds, forming a pleated sheet-like arrangement. These secondary structures provide the foundation for the formation of tertiary and quaternary protein structures, which determine the overall three-dimensional shape and function of the protein.

Triterpenes are a type of natural compound that are composed of six isoprene units and have the molecular formula C30H48. They are synthesized through the mevalonate pathway in plants, fungi, and some insects, and can be found in a wide variety of natural sources, including fruits, vegetables, and medicinal plants.

Triterpenes have diverse structures and biological activities, including anti-inflammatory, antiviral, and cytotoxic effects. Some triterpenes are also used in traditional medicine, such as glycyrrhizin from licorice root and betulinic acid from the bark of birch trees.

Triterpenes can be further classified into various subgroups based on their carbon skeletons, including squalene, lanostane, dammarane, and ursane derivatives. Some triterpenes are also modified through various biochemical reactions to form saponins, steroids, and other compounds with important biological activities.

Flavonols are a type of flavonoid, which is a class of plant and fungal metabolites. They are characterized by the presence of a 3-hydroxyflavone skeleton. Flavonols are found in a variety of plants and are known for their antioxidant properties. Some common dietary sources of flavonols include onions, kale, broccoli, apples, tea, and red wine. They have been studied for their potential health benefits, including reducing the risk of chronic diseases such as cancer and cardiovascular disease. Flavonols are also known to have anti-inflammatory, neuroprotective, and antimicrobial properties.

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.

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.

Glucuronidase is an enzyme that catalyzes the hydrolysis of glucuronic acid from various substrates, including molecules that have been conjugated with glucuronic acid as part of the detoxification process in the body. This enzyme plays a role in the breakdown and elimination of certain drugs, toxins, and endogenous compounds, such as bilirubin. It is found in various tissues and organisms, including humans, bacteria, and insects. In clinical contexts, glucuronidase activity may be measured to assess liver function or to identify the presence of certain bacterial infections.

Acid phosphatase is a type of enzyme that is found in various tissues and organs throughout the body, including the prostate gland, red blood cells, bone, liver, spleen, and kidneys. This enzyme plays a role in several biological processes, such as bone metabolism and the breakdown of molecules like nucleotides and proteins.

Acid phosphatase is classified based on its optimum pH level for activity. Acid phosphatases have an optimal activity at acidic pH levels (below 7.0), while alkaline phosphatases have an optimal activity at basic or alkaline pH levels (above 7.0).

In clinical settings, measuring the level of acid phosphatase in the blood can be useful as a tumor marker for prostate cancer. Elevated acid phosphatase levels may indicate the presence of metastatic prostate cancer or disease progression. However, it is important to note that acid phosphatase is not specific to prostate cancer and can also be elevated in other conditions, such as bone diseases, liver disorders, and some benign conditions. Therefore, acid phosphatase should be interpreted in conjunction with other diagnostic tests and clinical findings for a more accurate diagnosis.

Iridoid glucosides are a type of plant-based compounds that are characterized by their iridoid structure, which is a cyclic organic compound containing a cyclopentane ring fused to a six-membered unsaturated carbocycle. These compounds are often found in plants as glycosides, meaning they are combined with a sugar molecule such as glucose.

Iridoid glucosides have been identified in a variety of plant families, including the Lamiaceae (mint family), Scrophulariaceae (figwort family), and Rubiaceae (coffee family). Some examples of iridoid glucosides include geniposide, which is found in the fruit of the gardenia plant, and aucubin, which is found in the leaves of the eucommia tree.

Iridoid glucosides have been studied for their potential medicinal properties, including anti-inflammatory, antioxidant, and antimicrobial effects. However, more research is needed to fully understand their mechanisms of action and potential therapeutic uses.

Hexosaminidases are a group of enzymes that play a crucial role in the breakdown of complex carbohydrates, specifically glycoproteins and glycolipids, in the human body. These enzymes are responsible for cleaving the terminal N-acetyl-D-glucosamine (GlcNAc) residues from these molecules during the process of glycosidase digestion.

There are several types of hexosaminidases, including Hexosaminidase A and Hexosaminidase B, which are encoded by different genes and have distinct functions. Deficiencies in these enzymes can lead to serious genetic disorders, such as Tay-Sachs disease and Sandhoff disease, respectively. These conditions are characterized by the accumulation of undigested glycolipids and glycoproteins in various tissues, leading to progressive neurological deterioration and other symptoms.

Pregnanes are a class of steroid hormones and steroids that contain a pregnane nucleus, which is a steroid core with a carbon skeleton consisting of 21 carbons. This structure includes four fused rings, labeled A through D, and is derived from cholesterol.

Pregnanes are important precursors for the synthesis of various steroid hormones in the body, including progesterone, which plays a crucial role in maintaining pregnancy and regulating the menstrual cycle. Other examples of pregnanes include cortisol, a stress hormone produced by the adrenal gland, and aldosterone, a hormone that helps regulate electrolyte balance and blood pressure.

It's worth noting that pregnanes can also refer to synthetic compounds that contain this steroid nucleus and are used in various medical and research contexts.

Molecular structure, in the context of biochemistry and molecular biology, refers to the arrangement and organization of atoms and chemical bonds within a molecule. It describes the three-dimensional layout of the constituent elements, including their spatial relationships, bond lengths, and angles. Understanding molecular structure is crucial for elucidating the functions and reactivities of biological macromolecules such as proteins, nucleic acids, lipids, and carbohydrates. Various experimental techniques, like X-ray crystallography, nuclear magnetic resonance (NMR) spectroscopy, and cryo-electron microscopy (cryo-EM), are employed to determine molecular structures at atomic resolution, providing valuable insights into their biological roles and potential therapeutic targets.

Digoxin is a medication that belongs to a class of drugs called cardiac glycosides. It is used to treat various heart conditions, such as heart failure and atrial fibrillation, by helping the heart beat stronger and more regularly. Digoxin works by inhibiting the sodium-potassium pump in heart muscle cells, which leads to an increase in intracellular calcium and a strengthening of heart contractions. It is important to monitor digoxin levels closely, as too much can lead to toxicity and serious side effects.

Beta-Mannosidase is an enzyme that breaks down complex carbohydrates known as glycoproteins. It does this by catalyzing the hydrolysis of beta-mannosidic linkages, which are specific types of chemical bonds that connect mannose sugars within glycoproteins.

This enzyme plays an important role in the normal functioning of the body, particularly in the breakdown and recycling of glycoproteins. A deficiency in beta-mannosidase activity can lead to a rare genetic disorder known as beta-Mannosidosis, which is characterized by the accumulation of mannose-rich oligosaccharides in various tissues and organs, leading to progressive neurological deterioration and other symptoms.

"Cimicifuga" is a genus of plants commonly known as black cohosh or bugbane. It belongs to the family Ranunculaceae and is native to North America. The plant has been used in traditional medicine for treating various health conditions, such as menopausal symptoms, menstrual cramps, and inflammation. However, it's essential to consult a healthcare professional before using any herbal remedies for medical purposes.

Rutin is a flavonoid, a type of plant pigment that is found in various plants and foods including citrus fruits, buckwheat, and asparagus. It has antioxidant properties and is known to help strengthen blood vessels and reduce inflammation. In medical terms, rutin may be mentioned in the context of discussing treatments for conditions related to these effects, such as varicose veins or hemorrhoids. However, it's important to note that while rutin has potential health benefits, more research is needed to fully understand its effects and proper dosages.

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.

Ouabain is defined as a cardiac glycoside, a type of steroid, that is found in the seeds and roots of certain plants native to Africa. It is used in medicine as a digitalis-like agent to increase the force of heart contractions and slow the heart rate, particularly in the treatment of congestive heart failure and atrial fibrillation. Ouabain functions by inhibiting the sodium-potassium pump (Na+/K+-ATPase) in the cell membrane, leading to an increase in intracellular sodium and calcium ions, which ultimately enhances cardiac muscle contractility. It is also known as g-strophanthin or ouabaine.

N-Acetylmuramoyl-L-alanine Amidase (also known as NAM Amidase or MurNAc-LAA Amidase) is an enzyme that plays a crucial role in the bacterial cell wall metabolism. It is responsible for cleaving the amide bond between N-acetylmuramic acid (NAM) and L-alanine (L-Ala) in the peptidoglycan, which is a major component of the bacterial cell wall.

The enzyme's systematic name is N-acetylmuramoyl-L-alanine amidase, but it can also be referred to as:

* N-acetylmuramic acid lyase
* Peptidoglycan N-acetylmuramoylhydrolase
* N-acetylmuramoyl-L-alanine glycohydrolase
* N-acetylmuramoyl-L-alanine amidohydrolase

N-Acetylmuramoyl-L-alanine Amidase is an essential enzyme for bacterial cell division and morphogenesis, as it facilitates the separation of daughter cells by cleaving peptidoglycan crosslinks. This enzyme has been studied extensively due to its potential as a target for developing new antibiotics that can selectively inhibit bacterial cell wall biosynthesis without affecting human cells.

Peptide hydrolases, also known as proteases or peptidases, are a group of enzymes that catalyze the hydrolysis of peptide bonds in proteins and peptides. They play a crucial role in various biological processes such as protein degradation, digestion, cell signaling, and regulation of various physiological functions. Based on their catalytic mechanism and the specificity for the peptide bond, they are classified into several types, including serine proteases, cysteine proteases, aspartic proteases, and metalloproteases. These enzymes have important clinical applications in the diagnosis and treatment of various diseases, such as cancer, viral infections, and inflammatory disorders.

A rhizome is not typically used as a medical term, but it is a term borrowed from botany that has been adopted in some areas of medicine, particularly in psychiatry and psychotherapy.

In its original botanical sense, a rhizome is a horizontal stem of a plant that grows underground, often sending out roots and shoots from its nodes. This growth pattern is contrasted with that of a root system, which grows downward, and a stem system, which grows upward.

In psychiatry and psychotherapy, the term "rhizome" has been used as a metaphor to describe a non-hierarchical and decentralized approach to understanding mental processes and subjectivity. The rhizome model emphasizes the complexity, multiplicity, and interconnectedness of these processes, and rejects simplistic or reductionist explanations that focus on a single cause or origin. Instead, it encourages a more holistic and dynamic view of mental life, one that is open to multiple perspectives and interpretations.

It's important to note that the use of the term "rhizome" in this context is metaphorical and not medical in the strict sense. It is a way of thinking about mental processes and subjectivity that has been influenced by poststructuralist and feminist theories, among others.

Acetylglucosaminidase (ACG) is an enzyme that catalyzes the hydrolysis of N-acetyl-beta-D-glucosaminides, which are found in glycoproteins and glycolipids. This enzyme plays a crucial role in the degradation and recycling of these complex carbohydrates within the body.

Deficiency or malfunction of Acetylglucosaminidase can lead to various genetic disorders, such as mucolipidosis II (I-cell disease) and mucolipidosis III (pseudo-Hurler polydystrophy), which are characterized by the accumulation of glycoproteins and glycolipids in lysosomes, resulting in cellular dysfunction and progressive damage to multiple organs.

Alpha-L-Fucosidase is an enzyme that catalyzes the hydrolysis of the terminal alpha-L-fucose residues from glycoproteins, glycolipids, and other substrates. This enzyme plays a crucial role in the degradation and recycling of complex carbohydrates found on the surface of cells and in various biological fluids. Deficiencies in alpha-L-fucosidase activity can lead to genetic disorders such as fucosidosis, which is characterized by the accumulation of fucose-containing glycoproteins and glycolipids in various tissues and organs, resulting in progressive neurological deterioration and other systemic manifestations.

Ranunculaceae is a family of flowering plants, also known as the buttercup family. It includes over 2,000 species distributed across 58 genera. The plants in this family are characterized by their showy, often brightly colored flowers and typically have numerous stamens and carpels. Many members of Ranunculaceae contain toxic compounds, which can be irritants or even poisonous if ingested. Examples of plants in this family include buttercups, delphiniums, monkshood, and columbines.

Stevia is not a medical term, but a common name for a natural sweetener derived from the leaves of the Stevia rebaudiana plant. Here's a definition related to its use as a sweetener:

Stevia: A natural non-nutritive sweetener and sugar substitute derived from the leaves of the Stevia rebaudiana plant, which is native to South America. The sweetening compounds in stevia are called steviol glycosides, which have up to 350 times the sweetness of sucrose (table sugar) but contain minimal calories and do not raise blood sugar levels. Stevia extracts are often used as a sugar substitute in food and beverages, including drinks, desserts, and baked goods. It is also available in powdered or liquid forms for general use as a sweetener.

Mucolipidoses are a group of inherited metabolic disorders characterized by the accumulation of complex carbohydrates (muco-) and fatty substances (lipids) in various tissues and cells (-oses). This is due to deficiency in enzymes that help break down these substances within lysosomes, which are organelles responsible for recycling and breaking down waste materials inside the cell.

There are four main types of mucolipidoses (I, II, III, and IV), each resulting from specific genetic mutations affecting different enzymes or proteins involved in the lysosomal degradation pathway. The symptoms, severity, and age of onset can vary widely among these types, ranging from mild to severe and including developmental delays, bone abnormalities, vision and hearing loss, heart problems, and coarse facial features.

Mucolipidoses are typically inherited in an autosomal recessive manner, meaning that an individual must inherit two copies of the mutated gene (one from each parent) to develop the condition. However, mucolipidosis II is caused by X-linked inheritance, where a single copy of the mutated gene on the X chromosome is enough to cause the disorder.

Early diagnosis and management of mucolipidoses can help improve quality of life and slow disease progression. Treatment options include physical therapy, occupational therapy, speech therapy, medications for symptom management, and in some cases, enzyme replacement therapy or bone marrow transplantation.

Saponins are a type of naturally occurring chemical compound found in various plants, including soapwords, ginseng, and many others. They are known for their foaming properties, similar to that of soap, which gives them their name "saponin" derived from the Latin word "sapo" meaning soap.

Medically, saponins have been studied for their potential health benefits, including their ability to lower cholesterol levels, reduce inflammation, and boost the immune system. However, they can also have toxic effects in high concentrations, causing gastrointestinal disturbances and potentially damaging red blood cells.

Saponins are typically found in the cell walls of plants and can be extracted through various methods for use in pharmaceuticals, food additives, and cosmetics.

Glucosidases are a group of enzymes that catalyze the hydrolysis of glycosidic bonds, specifically at the non-reducing end of an oligo- or poly saccharide, releasing a single sugar molecule, such as glucose. They play important roles in various biological processes, including digestion of carbohydrates and the breakdown of complex glycans in glycoproteins and glycolipids.

In the context of digestion, glucosidases are produced by the pancreas and intestinal brush border cells to help break down dietary polysaccharides (e.g., starch) into monosaccharides (glucose), which can then be absorbed by the body for energy production or storage.

There are several types of glucosidases, including:

1. α-Glucosidase: This enzyme is responsible for cleaving α-(1→4) and α-(1→6) glycosidic bonds in oligosaccharides and disaccharides, such as maltose, maltotriose, and isomaltose.
2. β-Glucosidase: This enzyme hydrolyzes β-(1→4) glycosidic bonds in cellobiose and other oligosaccharides derived from plant cell walls.
3. Lactase (β-Galactosidase): Although not a glucosidase itself, lactase is often included in this group because it hydrolyzes the β-(1→4) glycosidic bond between glucose and galactose in lactose, yielding free glucose and galactose.

Deficiencies or inhibition of these enzymes can lead to various medical conditions, such as congenital sucrase-isomaltase deficiency (an α-glucosidase deficiency), lactose intolerance (a lactase deficiency), and Gaucher's disease (a β-glucocerebrosidase deficiency).

Thiol esters are chemical compounds that contain a sulfur atom (from a mercapto group, -SH) linked to a carbonyl group (a carbon double-bonded to an oxygen atom, -CO-) through an ester bond. Thiolester hydrolases are enzymes that catalyze the hydrolysis of thiol esters, breaking down these compounds into a carboxylic acid and a thiol (a compound containing a mercapto group).

In biological systems, thiolester bonds play important roles in various metabolic pathways. For example, acetyl-CoA, a crucial molecule in energy metabolism, is a thiol ester that forms between coenzyme A and an acetyl group. Thiolester hydrolases help regulate the formation and breakdown of these thiol esters, allowing cells to control various biochemical reactions.

Examples of thiolester hydrolases include:

1. CoA thioesterases (CoATEs): These enzymes hydrolyze thiol esters between coenzyme A and fatty acids, releasing free coenzyme A and a fatty acid. This process is essential for fatty acid metabolism.
2. Acetyl-CoA hydrolase: This enzyme specifically breaks down the thiol ester bond in acetyl-CoA, releasing acetic acid and coenzyme A.
3. Thioesterases involved in non-ribosomal peptide synthesis (NRPS): These enzymes hydrolyze thiol esters during the biosynthesis of complex peptides, allowing for the formation of unique amino acid sequences and structures.

Understanding the function and regulation of thiolester hydrolases can provide valuable insights into various metabolic processes and potential therapeutic targets in disease treatment.

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.

Kaempferol is not a medical term, but a chemical compound. It is a type of flavonoid, a class of plant pigments that are known for their antioxidant properties. Kaempferol can be found in various plants and foods such as tea, broccoli, kale, spinach, grapes, and some types of berries.

Medically, kaempferol has been studied for its potential health benefits due to its antioxidant, anti-inflammatory, and anti-cancer properties. However, more research is needed to confirm these effects and determine the appropriate dosages for medical use. It's important to note that consuming foods rich in kaempferol as part of a balanced diet is generally considered safe and beneficial for health.

I'm sorry for any confusion, but "Spirostans" is not a recognized term in medical terminology. It seems like it might be a reference to a specific chemical compound or class of compounds, possibly related to steroids, based on the prefix "spiro-" and the suffix "-stan." However, I cannot provide a precise definition without more context.

If you're referring to a specific medical or scientific concept, could you please provide more information or check the spelling? I'm here to help, and I want to make sure I give you the most accurate and helpful response possible.

Beta-N-Acetylhexosaminidases are a group of enzymes that play a role in the breakdown and recycling of complex carbohydrates in the body. Specifically, they help to break down gangliosides, which are a type of molecule found in cell membranes.

There are several different isoforms of beta-N-Acetylhexosaminidases, including A, B, and S. These isoforms are formed by different combinations of subunits, which can affect their activity and substrate specificity.

Mutations in the genes that encode for these enzymes can lead to a variety of genetic disorders, including Tay-Sachs disease and Sandhoff disease. These conditions are characterized by an accumulation of gangliosides in the brain, which can cause progressive neurological deterioration and death.

Treatment for these conditions typically involves managing symptoms and providing supportive care, as there is currently no cure. Enzyme replacement therapy has been explored as a potential treatment option, but its effectiveness varies depending on the specific disorder and the age of the patient.

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.

Quercetin is a type of flavonoid antioxidant that is found in plant foods, including leafy greens, tomatoes, berries, and broccoli. It has been studied for its potential health benefits, such as reducing inflammation, protecting against damage to cells, and helping to reduce the risk of heart disease and cancer. Quercetin is also known for its ability to stabilize mast cells and prevent the release of histamine, making it a popular natural remedy for allergies. It is available in supplement form, but it is always recommended to consult with a healthcare provider before starting any new supplement regimen.

"Asclepias" is a genus of plants in the dogbane family (Apocynaceae). It includes several species commonly known as milkweeds. These plants are native to North America and are known for their milky sap and clusters of pink, yellow, or white flowers. Some species of Asclepias are important host plants for the monarch butterfly, which lays its eggs on the leaves and uses the sap to fuel its migration.

Galactosidases are a group of enzymes that catalyze the hydrolysis of galactose-containing sugars, specifically at the beta-glycosidic bond. There are several types of galactosidases, including:

1. Beta-galactosidase: This is the most well-known type of galactosidase and it catalyzes the hydrolysis of lactose into glucose and galactose. It has important roles in various biological processes, such as lactose metabolism in animals and cell wall biosynthesis in plants.
2. Alpha-galactosidase: This enzyme catalyzes the hydrolysis of alpha-galactosides, which are found in certain plant-derived foods like legumes. A deficiency in this enzyme can lead to a genetic disorder called Fabry disease.
3. N-acetyl-beta-glucosaminidase: This enzyme is also known as hexosaminidase and it catalyzes the hydrolysis of N-acetyl-beta-D-glucosamine residues from glycoproteins, glycolipids, and other complex carbohydrates.

Galactosidases are widely used in various industrial applications, such as food processing, biotechnology, and biofuel production. They also have potential therapeutic uses, such as in the treatment of lysosomal storage disorders like Fabry disease.

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.

Cellulose 1,4-beta-Cellobiosidase is an enzyme that catalyzes the hydrolysis of cellulose, a complex carbohydrate and the main structural component of plant cell walls, into simpler sugars. Specifically, this enzyme breaks down cellulose by cleaving the 1,4-beta-glycosidic bonds between the cellobiose units that make up the cellulose polymer, releasing individual cellobiose molecules (disaccharides consisting of two glucose molecules). This enzyme is also known as cellobiohydrolase or beta-1,4-D-glucan cellobiohydrolase. It plays a crucial role in the natural breakdown of plant material and is widely used in various industrial applications, such as biofuel production and pulp and paper manufacturing.

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.

Diterpenes, kaurane refers to a class of diterpenoids with a unique chemical structure called a kaurane skeleton. Diterpenes are a type of terpene, which are natural compounds derived from isoprene units. Kaurane diterpenes are characterized by a particular carbon skeleton consisting of five six-membered rings, including four cyclohexane rings and one cyclopentane ring.

Kaurane diterpenes can be found in various plants, including those used in traditional medicine. Some kaurane diterpenes have been reported to possess biological activities, such as anti-inflammatory, antiviral, and cytotoxic effects. However, more research is needed to fully understand their therapeutic potential and safety profile.

Flavanones are a type of flavonoid, which is a class of plant pigments widely found in fruits, vegetables, and other plants. Flavanones are known for their antioxidant properties and potential health benefits. They are typically found in citrus fruits such as oranges, lemons, and grapefruits. Some common flavanones include hesperetin, naringenin, and eriodictyol. These compounds have been studied for their potential effects on cardiovascular health, cancer prevention, and neuroprotection, although more research is needed to fully understand their mechanisms of action and therapeutic potential.

Medicinal plants are defined as those plants that contain naturally occurring chemical compounds which can be used for therapeutic purposes, either directly or indirectly. These plants have been used for centuries in various traditional systems of medicine, such as Ayurveda, Chinese medicine, and Native American medicine, to prevent or treat various health conditions.

Medicinal plants contain a wide variety of bioactive compounds, including alkaloids, flavonoids, tannins, terpenes, and saponins, among others. These compounds have been found to possess various pharmacological properties, such as anti-inflammatory, analgesic, antimicrobial, antioxidant, and anticancer activities.

Medicinal plants can be used in various forms, including whole plant material, extracts, essential oils, and isolated compounds. They can be administered through different routes, such as oral, topical, or respiratory, depending on the desired therapeutic effect.

It is important to note that while medicinal plants have been used safely and effectively for centuries, they should be used with caution and under the guidance of a healthcare professional. Some medicinal plants can interact with prescription medications or have adverse effects if used inappropriately.

Scrophulariaceae is a family of plants commonly known as the Figwort or Snapdragon family. It was once a large and diverse group, but many of its members have been reclassified into different families in recent years based on molecular evidence. The family still includes a number of well-known garden plants such as foxgloves (Digitalis), snapdragons (Antirrhinum), and penstemons (Penstemon).

The plants in Scrophulariaceae are typically herbaceous, although some are shrubs or small trees. They are characterized by their two-lipped flowers, with the upper lip usually forming a hood and the lower lip often having three lobes. The stamens and style are often enclosed within the flower and only emerge when it is fully open.

Scrophulariaceae has been reported to contain various chemical compounds with potential medicinal properties, such as cardiac glycosides in Digitalis species, which have been used to treat heart conditions. However, it's important to note that the use of these plants for medicinal purposes should only be done under the guidance and supervision of a qualified healthcare professional, as they can also contain toxic compounds that may cause harm if not used correctly.

Alpha-glucosidases are a group of enzymes that break down complex carbohydrates into simpler sugars, such as glucose, by hydrolyzing the alpha-1,4 and alpha-1,6 glycosidic bonds in oligosaccharides, disaccharides, and polysaccharides. These enzymes are located on the brush border of the small intestine and play a crucial role in carbohydrate digestion and absorption.

Inhibitors of alpha-glucosidases, such as acarbose and miglitol, are used in the treatment of type 2 diabetes to slow down the digestion and absorption of carbohydrates, which helps to reduce postprandial glucose levels and improve glycemic control.

Acid anhydride hydrolases are a class of enzymes that catalyze the hydrolysis (breakdown) of acid anhydrides, which are chemical compounds formed by the reaction between two carboxylic acids. This reaction results in the formation of a molecule of water and the release of a new carboxylic acid.

Acid anhydride hydrolases play important roles in various biological processes, including the metabolism of lipids, carbohydrates, and amino acids. They are also involved in the regulation of intracellular pH and the detoxification of xenobiotics (foreign substances).

Examples of acid anhydride hydrolases include esterases, lipases, and phosphatases. These enzymes have different substrate specificities and catalytic mechanisms, but they all share the ability to hydrolyze acid anhydrides.

The term "acid anhydride hydrolase" is often used interchangeably with "esterase," although not all esterases are capable of hydrolyzing acid anhydrides.

Sodium-Potassium-Exchanging ATPase (also known as Na+/K+ ATPase) is a type of active transporter found in the cell membrane of many types of cells. It plays a crucial role in maintaining the electrochemical gradient and membrane potential of animal cells by pumping sodium ions (Na+) out of the cell and potassium ions (K+) into the cell, using energy derived from ATP hydrolysis.

This transporter is composed of two main subunits: a catalytic α-subunit that contains the binding sites for Na+, K+, and ATP, and a regulatory β-subunit that helps in the proper targeting and functioning of the pump. The Na+/K+ ATPase plays a critical role in various physiological processes, including nerve impulse transmission, muscle contraction, and kidney function.

In summary, Sodium-Potassium-Exchanging ATPase is an essential membrane protein that uses energy from ATP to transport sodium and potassium ions across the cell membrane, thereby maintaining ionic gradients and membrane potentials necessary for normal cellular function.

Arylsulfatases are a group of enzymes that play a role in the breakdown and recycling of complex molecules in the body. Specifically, they catalyze the hydrolysis of sulfate ester bonds in certain types of large sugar molecules called glycosaminoglycans (GAGs).

There are several different types of arylsulfatases, each of which targets a specific type of sulfate ester bond. For example, arylsulfatase A is responsible for breaking down sulfate esters in a GAG called cerebroside sulfate, while arylsulfatase B targets a different GAG called dermatan sulfate.

Deficiencies in certain arylsulfatases can lead to genetic disorders. For example, a deficiency in arylsulfatase A can cause metachromatic leukodystrophy, a progressive neurological disorder that affects the nervous system and causes a range of symptoms including muscle weakness, developmental delays, and cognitive decline. Similarly, a deficiency in arylsulfatase B can lead to Maroteaux-Lamy syndrome, a rare genetic disorder that affects the skeleton, eyes, ears, heart, and other organs.

I'm sorry for any confusion, but "Norisoprenoids" is not a widely recognized or established term in medicine or medical chemistry. It appears to be a term used primarily in the field of plant metabolism and natural products chemistry, referring to a class of compounds that are derived from the degradation of carotenoids (a type of isoprenoid) and have lost one or more methyl groups.

If you're asking about this term in a different context or if there's specific medical relevance you have in mind, could you please provide more details? I'd be happy to help further if I can.

Flavonoids are a type of plant compounds with antioxidant properties that are beneficial to health. They are found in various fruits, vegetables, grains, and wine. Flavonoids have been studied for their potential to prevent chronic diseases such as heart disease and cancer due to their ability to reduce inflammation and oxidative stress.

There are several subclasses of flavonoids, including:

1. Flavanols: Found in tea, chocolate, grapes, and berries. They have been shown to improve blood flow and lower blood pressure.
2. Flavones: Found in parsley, celery, and citrus fruits. They have anti-inflammatory and antioxidant properties.
3. Flavanonols: Found in citrus fruits, onions, and tea. They have been shown to improve blood flow and reduce inflammation.
4. Isoflavones: Found in soybeans and legumes. They have estrogen-like effects and may help prevent hormone-related cancers.
5. Anthocyanidins: Found in berries, grapes, and other fruits. They have antioxidant properties and may help improve vision and memory.

It is important to note that while flavonoids have potential health benefits, they should not be used as a substitute for medical treatment or a healthy lifestyle. It is always best to consult with a healthcare professional before starting any new supplement regimen.

Disaccharidases are a group of enzymes found in the brush border of the small intestine. They play an essential role in digesting complex carbohydrates into simpler sugars, which can then be absorbed into the bloodstream. The three main disaccharidases are:

1. Maltase-glucoamylase: This enzyme breaks down maltose (a disaccharide formed from two glucose molecules) and maltotriose (a trisaccharide formed from three glucose molecules) into individual glucose units.
2. Sucrase: This enzyme is responsible for breaking down sucrose (table sugar, a disaccharide composed of one glucose and one fructose molecule) into its component monosaccharides, glucose and fructose.
3. Lactase: This enzyme breaks down lactose (a disaccharide formed from one glucose and one galactose molecule) into its component monosaccharides, glucose and galactose.

Deficiencies in these disaccharidases can lead to various digestive disorders, such as lactose intolerance (due to lactase deficiency), sucrase-isomaltase deficiency, or congenital sucrase-isomaltase deficiency (CSID). These conditions can cause symptoms like bloating, diarrhea, and abdominal cramps after consuming foods containing the specific disaccharide.

Disaccharides are a type of carbohydrate that is made up of two monosaccharide units bonded together. Monosaccharides are simple sugars, such as glucose, fructose, or galactose. When two monosaccharides are joined together through a condensation reaction, they form a disaccharide.

The most common disaccharides include:

* Sucrose (table sugar), which is composed of one glucose molecule and one fructose molecule.
* Lactose (milk sugar), which is composed of one glucose molecule and one galactose molecule.
* Maltose (malt sugar), which is composed of two glucose molecules.

Disaccharides are broken down into their component monosaccharides during digestion by enzymes called disaccharidases, which are located in the brush border of the small intestine. These enzymes catalyze the hydrolysis of the glycosidic bond that links the two monosaccharides together, releasing them to be absorbed into the bloodstream and used for energy.

Disorders of disaccharide digestion and absorption can lead to various symptoms, such as bloating, diarrhea, and abdominal pain. For example, lactose intolerance is a common condition in which individuals lack sufficient levels of the enzyme lactase, leading to an inability to properly digest lactose and resulting in gastrointestinal symptoms.

Rhodiola (Rhodiola rosea), also known as golden root or roseroot, is an herb that grows in the wild Arctic regions of Europe and Asia. It has been used in traditional medicine in Russia and Scandinavia for centuries to increase stamina, strength, and mental capacity, and to help cope with cold climates and high altitudes.

Rhodiola rosea contains several chemical compounds, including rosavins and salidroside, which are believed to have adaptogenic properties, meaning they may help the body better respond to physical, chemical, and environmental stress. Some studies suggest that rhodiola may help reduce fatigue, improve mental performance, and boost the immune system, but more research is needed to confirm these effects and determine optimal dosages.

It's important to note that while some supplements containing rhodiola rosea are available over-the-counter, they are not regulated by the Food and Drug Administration (FDA) in the same way as prescription drugs, so it's important to talk to a healthcare provider before taking them. Additionally, rhodiola may interact with certain medications or have side effects, so it's important to use it under the guidance of a healthcare professional.

I believe there may be a slight misunderstanding in your question. "Plant leaves" are not a medical term, but rather a general biological term referring to a specific organ found in plants.

Leaves are organs that are typically flat and broad, and they are the primary site of photosynthesis in most plants. They are usually green due to the presence of chlorophyll, which is essential for capturing sunlight and converting it into chemical energy through photosynthesis.

While leaves do not have a direct medical definition, understanding their structure and function can be important in various medical fields, such as pharmacognosy (the study of medicinal plants) or environmental health. For example, certain plant leaves may contain bioactive compounds that have therapeutic potential, while others may produce allergens or toxins that can impact human health.

Pyrophosphatases are enzymes that catalyze the hydrolysis or cleavage of pyrophosphate (PPi) into two inorganic phosphate (Pi) molecules. This reaction is essential for many biochemical processes, such as energy metabolism and biosynthesis pathways, where pyrophosphate is generated as a byproduct. By removing the pyrophosphate, pyrophosphatases help drive these reactions forward and maintain the thermodynamic equilibrium.

There are several types of pyrophosphatases found in various organisms and cellular compartments, including:

1. Inorganic Pyrophosphatase (PPiase): This enzyme is widely distributed across all kingdoms of life and is responsible for hydrolyzing inorganic pyrophosphate into two phosphates. It plays a crucial role in maintaining the cellular energy balance by ensuring that the reverse reaction, the formation of pyrophosphate from two phosphates, does not occur spontaneously.
2. Nucleotide Pyrophosphatases: These enzymes hydrolyze the pyrophosphate bond in nucleoside triphosphates (NTPs) and deoxynucleoside triphosphates (dNTPs), converting them into nucleoside monophosphates (NMPs) or deoxynucleoside monophosphates (dNMPs). This reaction is important for regulating the levels of NTPs and dNTPs in cells, which are necessary for DNA and RNA synthesis.
3. ATPases and GTPases: These enzymes belong to a larger family of P-loop NTPases that use the energy released from pyrophosphate bond hydrolysis to perform mechanical work or transport ions across membranes. Examples include the F1F0-ATP synthase, which synthesizes ATP using a proton gradient, and various molecular motors like myosin, kinesin, and dynein, which move along cytoskeletal filaments.

Overall, pyrophosphatases are essential for maintaining cellular homeostasis by regulating the levels of nucleotides and providing energy for various cellular processes.

High-performance liquid chromatography (HPLC) is a type of chromatography that separates and analyzes compounds based on their interactions with a stationary phase and a mobile phase under high pressure. The mobile phase, which can be a gas or liquid, carries the sample mixture through a column containing the stationary phase.

In HPLC, the mobile phase is a liquid, and it is pumped through the column at high pressures (up to several hundred atmospheres) to achieve faster separation times and better resolution than other types of liquid chromatography. The stationary phase can be a solid or a liquid supported on a solid, and it interacts differently with each component in the sample mixture, causing them to separate as they travel through the column.

HPLC is widely used in analytical chemistry, pharmaceuticals, biotechnology, and other fields to separate, identify, and quantify compounds present in complex mixtures. It can be used to analyze a wide range of substances, including drugs, hormones, vitamins, pigments, flavors, and pollutants. HPLC is also used in the preparation of pure samples for further study or use.

Cathepsins are a type of proteolytic enzymes, which are found in lysosomes and are responsible for breaking down proteins inside the cell. They are classified as papain-like cysteine proteases and play important roles in various physiological processes, including tissue remodeling, antigen presentation, and apoptosis (programmed cell death). There are several different types of cathepsins, including cathepsin B, C, D, F, H, K, L, S, V, and X/Z, each with distinct substrate specificities and functions.

Dysregulation of cathepsins has been implicated in various pathological conditions, such as cancer, neurodegenerative diseases, and inflammatory disorders. For example, overexpression or hyperactivation of certain cathepsins has been shown to contribute to tumor invasion and metastasis, while their inhibition has been explored as a potential therapeutic strategy in cancer treatment. Similarly, abnormal levels of cathepsins have been linked to the progression of neurodegenerative diseases like Alzheimer's and Parkinson's, making them attractive targets for drug development.

Amidohydrolases are a class of enzymes that catalyze the hydrolysis of amides and related compounds, resulting in the formation of an acid and an alcohol. This reaction is also known as amide hydrolysis or amide bond cleavage. Amidohydrolases play important roles in various biological processes, including the metabolism of xenobiotics (foreign substances) and endogenous compounds (those naturally produced within an organism).

The term "amidohydrolase" is a broad one that encompasses several specific types of enzymes, such as proteases, esterases, lipases, and nitrilases. These enzymes have different substrate specificities and catalytic mechanisms but share the common ability to hydrolyze amide bonds.

Proteases, for example, are a major group of amidohydrolases that specifically cleave peptide bonds in proteins. They are involved in various physiological processes, such as protein degradation, digestion, and regulation of biological pathways. Esterases and lipases hydrolyze ester bonds in various substrates, including lipids and other organic compounds. Nitrilases convert nitriles into carboxylic acids and ammonia by cleaving the nitrile bond (C≡N) through hydrolysis.

Amidohydrolases are found in various organisms, from bacteria to humans, and have diverse applications in industry, agriculture, and medicine. For instance, they can be used for the production of pharmaceuticals, biofuels, detergents, and other chemicals. Additionally, inhibitors of amidohydrolases can serve as therapeutic agents for treating various diseases, such as cancer, viral infections, and neurodegenerative disorders.

Glycosyltransferases are a group of enzymes that play a crucial role in the synthesis of glycoconjugates, which are complex carbohydrate structures found on the surface of cells and in various biological fluids. These enzymes catalyze the transfer of a sugar moiety from an activated donor molecule to an acceptor molecule, resulting in the formation of a glycosidic bond.

The donor molecule is typically a nucleotide sugar, such as UDP-glucose or CMP-sialic acid, which provides the energy required for the transfer reaction. The acceptor molecule can be a wide range of substrates, including proteins, lipids, and other carbohydrates.

Glycosyltransferases are highly specific in their activity, with each enzyme recognizing a particular donor and acceptor pair. This specificity allows for the precise regulation of glycan structures, which have been shown to play important roles in various biological processes, including cell recognition, signaling, and adhesion.

Defects in glycosyltransferase function can lead to a variety of genetic disorders, such as congenital disorders of glycosylation (CDG), which are characterized by abnormal glycan structures and a wide range of clinical manifestations, including developmental delay, neurological impairment, and multi-organ dysfunction.

Chinese herbal drugs, also known as traditional Chinese medicine (TCM), refer to a system of medicine that has been practiced in China for thousands of years. It is based on the belief that the body's vital energy, called Qi, must be balanced and flowing freely for good health. TCM uses various techniques such as herbal therapy, acupuncture, dietary therapy, and exercise to restore balance and promote healing.

Chinese herbal drugs are usually prescribed in the form of teas, powders, pills, or tinctures and may contain one or a combination of herbs. The herbs used in Chinese medicine are typically derived from plants, minerals, or animal products. Some commonly used Chinese herbs include ginseng, astragalus, licorice root, and cinnamon bark.

It is important to note that the use of Chinese herbal drugs should be under the guidance of a qualified practitioner, as some herbs can interact with prescription medications or have side effects. Additionally, the quality and safety of Chinese herbal products can vary widely depending on the source and manufacturing process.

Molecular conformation, also known as spatial arrangement or configuration, refers to the specific three-dimensional shape and orientation of atoms that make up a molecule. It describes the precise manner in which bonds between atoms are arranged around a molecular framework, taking into account factors such as bond lengths, bond angles, and torsional angles.

Conformational isomers, or conformers, are different spatial arrangements of the same molecule that can interconvert without breaking chemical bonds. These isomers may have varying energies, stability, and reactivity, which can significantly impact a molecule's biological activity and function. Understanding molecular conformation is crucial in fields such as drug design, where small changes in conformation can lead to substantial differences in how a drug interacts with its target.

Esterases are a group of enzymes that catalyze the hydrolysis of ester bonds in esters, producing alcohols and carboxylic acids. They are widely distributed in plants, animals, and microorganisms and play important roles in various biological processes, such as metabolism, digestion, and detoxification.

Esterases can be classified into several types based on their substrate specificity, including carboxylesterases, cholinesterases, lipases, and phosphatases. These enzymes have different structures and mechanisms of action but all share the ability to hydrolyze esters.

Carboxylesterases are the most abundant and diverse group of esterases, with a wide range of substrate specificity. They play important roles in the metabolism of drugs, xenobiotics, and lipids. Cholinesterases, on the other hand, specifically hydrolyze choline esters, such as acetylcholine, which is an important neurotransmitter in the nervous system. Lipases are a type of esterase that preferentially hydrolyzes triglycerides and plays a crucial role in fat digestion and metabolism. Phosphatases are enzymes that remove phosphate groups from various molecules, including esters, and have important functions in signal transduction and other cellular processes.

Esterases can also be used in industrial applications, such as in the production of biodiesel, detergents, and food additives. They are often produced by microbial fermentation or extracted from plants and animals. The use of esterases in biotechnology is an active area of research, with potential applications in biofuel production, bioremediation, and medical diagnostics.

N-Glycosyl hydrolases (or N-glycanases) are a class of enzymes that catalyze the hydrolysis of the glycosidic bond between an N-glycosyl group and an aglycon, which is typically another part of a larger molecule such as a protein or lipid. N-Glycosyl groups refer to carbohydrate moieties attached to an nitrogen atom, usually in the side chain of an amino acid such as asparagine (Asn) in proteins.

N-Glycosyl hydrolases play important roles in various biological processes, including the degradation and processing of glycoproteins, the modification of glycolipids, and the breakdown of complex carbohydrates. These enzymes are widely distributed in nature and have been found in many organisms, from bacteria to humans.

The classification and nomenclature of N-Glycosyl hydrolases are based on the type of glycosidic bond they cleave and the stereochemistry of the reaction they catalyze. They are grouped into different families in the Carbohydrate-Active enZymes (CAZy) database, which provides a comprehensive resource for the study of carbohydrate-active enzymes.

It is worth noting that N-Glycosyl hydrolases can have both beneficial and detrimental effects on human health. For example, they are involved in the normal turnover and degradation of glycoproteins in the body, but they can also contribute to the pathogenesis of certain diseases, such as lysosomal storage disorders, where mutations in N-Glycosyl hydrolases lead to the accumulation of undigested glycoconjugates and cellular damage.

Cathepsin D is a lysosomal aspartic protease that plays a role in intracellular protein degradation and turnover. It is produced as an inactive precursor and is activated by cleavage into two subunits within the acidic environment of the lysosome. Cathepsin D is also known to be secreted by certain cells, where it can contribute to extracellular matrix remodeling and tissue degradation. In addition, abnormal levels or activity of cathepsin D have been implicated in various diseases, including cancer, neurodegenerative disorders, and infectious diseases.

"Piromyces" is not a medical term, but rather it refers to a genus of anamorphic fungi belonging to the family Neocallimastigaceae. These fungi are commonly found in the digestive tracts of various animals, including ruminants and some non-ruminant herbivores, where they play a crucial role in breaking down complex plant material through anaerobic digestion. They are not associated with any human or animal diseases.

I apologize for the confusion, but "Lamiaceae" is not a medical term. It is a taxonomic category in biology, specifically it is a family of flowering plants that includes many familiar herbs such as mint, rosemary, sage, basil, and lavender. These plants are often used in medicine, cooking, and for ornamental purposes. The Lamiaceae family is characterized by their square stems, opposite leaves, and two-lipped flowers.

Acanthaceae is a family of flowering plants that includes around 2,500 species distributed across 220-400 genera. These plants are primarily found in tropical and subtropical regions, with some extending into temperate zones. The family is characterized by the presence of stiff, spiny bracts, which are often colorful and modified to attract pollinators.

The plants in Acanthaceae can vary widely in form, from herbaceous annuals and perennials to shrubs and trees. They have simple or opposite leaves that may be entire or lobed. The flowers are typically bisexual, with a two-lipped calyx and corolla, and four stamens.

Some well-known members of Acanthaceae include the garden plants Shrimp Plant (Justicia brandegeeana) and Whorled Tubelet (Lepidagathis formosa), as well as the medicinal plant Indian Snakeroot (Rauvolfia serpentina).

In a medical context, some species of Acanthaceae have been used in traditional medicine for various purposes, such as treating skin conditions, fevers, and gastrointestinal disorders. However, it is important to note that the use of these plants should be done with caution and under the guidance of a qualified healthcare professional, as they can also contain toxic compounds.

Acetylesterase is an enzyme that catalyzes the hydrolysis of acetyl esters into alcohol and acetic acid. This enzyme plays a role in the metabolism of various xenobiotics, including drugs and environmental toxins, by removing acetyl groups from these compounds. Acetylesterase is found in many tissues, including the liver, intestine, and blood. It belongs to the class of enzymes known as hydrolases, which act on ester bonds.

Cistanche is a genus of plants in the family Orobanchaceae, also known as the broomrape family. It includes several species that are native to Asia and the Mediterranean region. One commonly used species is Cistanche deserticola, which is known in traditional Chinese medicine as Rou Cong Rong. This plant is a parasitic desert shrub that grows by tapping into the roots of other plants for nutrients.

In traditional Chinese medicine, extracts from the dried root of Cistanche deserticola are used to treat various conditions, such as impotence, constipation, and kidney deficiency. However, it's important to note that while some studies suggest potential health benefits of Cistanche, more research is needed to confirm its effectiveness and safety.

As with any supplement or medication, consult a healthcare professional before using Cistanche extract or any other products derived from this plant.

A plant root is not a medical term per se, but it is a term from botany, which is the study of plants. However, I can certainly provide a definition for you.

Plant roots are the underground organs of a plant that typically grow downward into the soil. They serve several important functions, including:

1. Anchorage: Roots help to stabilize the plant and keep it upright in the ground.
2. Absorption: Roots absorb water and nutrients from the soil, which are essential for the plant's growth and development.
3. Conduction: Roots conduct water and nutrients up to the above-ground parts of the plant, such as the stem and leaves.
4. Vegetative reproduction: Some plants can reproduce vegetatively through their roots, producing new plants from root fragments or specialized structures called rhizomes or tubers.

Roots are composed of several different tissues, including the epidermis, cortex, endodermis, and vascular tissue. The epidermis is the outermost layer of the root, which secretes a waxy substance called suberin that helps to prevent water loss. The cortex is the middle layer of the root, which contains cells that store carbohydrates and other nutrients. The endodermis is a thin layer of cells that surrounds the vascular tissue and regulates the movement of water and solutes into and out of the root. The vascular tissue consists of xylem and phloem, which transport water and nutrients throughout the plant.

'Aspergillus niger' is a species of fungi that belongs to the genus Aspergillus. It is a ubiquitous microorganism that can be found in various environments, including soil, decaying vegetation, and indoor air. 'Aspergillus niger' is a black-colored mold that produces spores that are easily dispersed in the air.

This fungus is well known for its ability to produce a variety of enzymes and metabolites, some of which have industrial applications. For example, it is used in the production of citric acid, which is widely used as a food additive and preservative.

However, 'Aspergillus niger' can also cause health problems in humans, particularly in individuals with weakened immune systems or underlying lung conditions. It can cause allergic reactions, respiratory symptoms, and invasive aspergillosis, a serious infection that can spread to other organs in the body.

In addition, 'Aspergillus niger' can produce mycotoxins, which are toxic compounds that can contaminate food and feed and cause various health effects in humans and animals. Therefore, it is important to prevent the growth and proliferation of this fungus in indoor environments and food production facilities.

Thin-layer chromatography (TLC) is a type of chromatography used to separate, identify, and quantify the components of a mixture. In TLC, the sample is applied as a small spot onto a thin layer of adsorbent material, such as silica gel or alumina, which is coated on a flat, rigid support like a glass plate. The plate is then placed in a developing chamber containing a mobile phase, typically a mixture of solvents.

As the mobile phase moves up the plate by capillary action, it interacts with the stationary phase and the components of the sample. Different components of the mixture travel at different rates due to their varying interactions with the stationary and mobile phases, resulting in distinct spots on the plate. The distance each component travels can be measured and compared to known standards to identify and quantify the components of the mixture.

TLC is a simple, rapid, and cost-effective technique that is widely used in various fields, including forensics, pharmaceuticals, and research laboratories. It allows for the separation and analysis of complex mixtures with high resolution and sensitivity, making it an essential tool in many analytical applications.

Monocrotophos is not typically defined in medical terms, but it is a pesticide that can have medical implications. It's a type of organophosphate insecticide that works by inhibiting the enzyme acetylcholinesterase, leading to an overaccumulation of the neurotransmitter acetylcholine and resulting in symptoms such as muscle twitching, nausea, vomiting, diarrhea, sweating, and, at high exposures, seizures and respiratory failure. Chronic exposure can lead to neurological problems and an increased risk of certain cancers.

Convolvulaceae is a family of flowering plants, also known as the bindweed or morning glory family. It includes both annual and perennial vines, herbs, and shrubs, with over 1,650 species spread across around 60 genera. The plants in this family are characterized by their twining stems and funnel-shaped flowers. Some of the well-known members of Convolvulaceae include the sweet potato (Ipomoea batatas), morning glory (Ipomoea spp.), and bindweed (Convolvulus spp.).

Many species in this family contain ergoline alkaloids, which can have hallucinogenic effects. Some indigenous cultures have used these plants for their psychoactive properties in religious or spiritual ceremonies. However, it's important to note that some of these alkaloids can be toxic and even fatal if ingested in large quantities.

In a medical context, certain species of Convolvulaceae may be relevant due to their potential toxicity or as weeds that can cause problems in agriculture. For example, field bindweed (Convolvulus arvensis) is a notorious agricultural weed that can reduce crop yields and increase the difficulty of farming.

Spectrophotometry, Infrared is a scientific analytical technique used to measure the absorption or transmission of infrared light by a sample. It involves the use of an infrared spectrophotometer, which directs infrared radiation through a sample and measures the intensity of the radiation that is transmitted or absorbed by the sample at different wavelengths within the infrared region of the electromagnetic spectrum.

Infrared spectroscopy can be used to identify and quantify functional groups and chemical bonds present in a sample, as well as to study the molecular structure and composition of materials. The resulting infrared spectrum provides a unique "fingerprint" of the sample, which can be compared with reference spectra to aid in identification and characterization.

Infrared spectrophotometry is widely used in various fields such as chemistry, biology, pharmaceuticals, forensics, and materials science for qualitative and quantitative analysis of samples.

Chitinase is an enzyme that breaks down chitin, a complex carbohydrate and a major component of the exoskeletons of arthropods, the cell walls of fungi, and the microfilamentous matrices of many invertebrates. Chitinases are found in various organisms, including bacteria, fungi, plants, and animals. In humans, chitinases are involved in immune responses to certain pathogens and have been implicated in the pathogenesis of several inflammatory diseases, such as asthma and chronic obstructive pulmonary disease (COPD).

Rubiaceae is not a medical term, but a taxonomic category in botany. It refers to the family of flowering plants that includes more than 13,500 species, distributed across approximately 600 genera. Some well-known members of this family include coffee (Coffea arabica), gardenias (Gardenia jasminoides), and madder (Rubia tinctorum).

In a medical context, certain plants from the Rubiaceae family have been used in traditional medicine for various purposes. For example:

* Coffee (Coffea arabica) beans are used to prepare caffeinated beverages that can help with alertness and concentration.
* Gardenia fruits and flowers have been used in traditional Chinese medicine to treat anxiety, insomnia, and inflammation.
* Madder root (Rubia tinctorum) has been used as a dye and in traditional medicine to treat skin conditions and digestive disorders.

However, it's important to note that the medicinal use of plants from this family should be based on scientific evidence and under the guidance of healthcare professionals, as some of these plants can have side effects or interact with medications.

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.

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.

Xylan Endo-1,3-beta-Xylosidase is an enzyme that breaks down xylan, which is a major component of hemicellulose in plant cell walls. This enzyme specifically catalyzes the hydrolysis of 1,3-beta-D-xylosidic linkages in xylans, resulting in the release of xylose units from the xylan backbone. It is involved in the process of breaking down plant material for various industrial applications and in the natural decomposition of plants by microorganisms.

In a medical context, "resins, plant" refer to the sticky, often aromatic substances produced by certain plants. These resins are typically composed of a mixture of volatile oils, terpenes, and rosin acids. They may be present in various parts of the plant, including leaves, stems, and roots, and are often found in specialized structures such as glands or ducts.

Plant resins have been used for centuries in traditional medicine and other applications. Some resins have antimicrobial, anti-inflammatory, or analgesic properties and have been used to treat a variety of ailments, including skin conditions, respiratory infections, and pain.

Examples of plant resins with medicinal uses include:

* Frankincense (Boswellia spp.) resin has been used in traditional medicine to treat inflammation, arthritis, and asthma.
* Myrrh (Commiphora spp.) resin has been used as an antiseptic, astringent, and anti-inflammatory agent.
* Pine resin has been used topically for its antimicrobial and anti-inflammatory properties.

It's important to note that while some plant resins have demonstrated medicinal benefits, they should be used with caution and under the guidance of a healthcare professional. Some resins can have adverse effects or interact with medications, and it's essential to ensure their safe and effective use.

I'm sorry for any confusion, but "Gardenia" is not a medical term. It is the name of a genus of flowering plants in the coffee family, Rubiaceae. These plants are native to tropical and subtropical regions of Africa, Southern Asia, and Australia. The flowers of some Gardenia species are used in perfumes and traditional medicines due to their fragrance. If you have any questions about a specific medical term or concept, please let me know and I would be happy to help.

Glucan Endo-1,3-beta-D-Glucosidase is an enzyme that catalyzes the hydrolysis of 1,3-beta-D-glycosyl links in glucans, which are polysaccharides composed of D-glucose units joined by beta-linkages. This enzyme specifically cleaves internal beta-1,3 bonds, resulting in the production of shorter glucan chains with reducing and non-reducing ends.

Glucan Endo-1,3-beta-D-Glucosidase is found in various organisms, including bacteria, fungi, and higher plants. It has attracted significant interest in biotechnological applications due to its potential role in the degradation of cell walls in pathogenic fungi and its ability to generate bioactive glucooligosaccharides with potential health benefits.

In medical contexts, Glucan Endo-1,3-beta-D-Glucosidase has been studied for its potential role in the treatment of fungal infections, as well as its diagnostic value in detecting and measuring specific types of glucans in biological samples.

Stereoisomerism is a type of isomerism (structural arrangement of atoms) in which molecules have the same molecular formula and sequence of bonded atoms, but differ in the three-dimensional orientation of their atoms in space. This occurs when the molecule contains asymmetric carbon atoms or other rigid structures that prevent free rotation, leading to distinct spatial arrangements of groups of atoms around a central point. Stereoisomers can have different chemical and physical properties, such as optical activity, boiling points, and reactivities, due to differences in their shape and the way they interact with other molecules.

There are two main types of stereoisomerism: enantiomers (mirror-image isomers) and diastereomers (non-mirror-image isomers). Enantiomers are pairs of stereoisomers that are mirror images of each other, but cannot be superimposed on one another. Diastereomers, on the other hand, are non-mirror-image stereoisomers that have different physical and chemical properties.

Stereoisomerism is an important concept in chemistry and biology, as it can affect the biological activity of molecules, such as drugs and natural products. For example, some enantiomers of a drug may be active, while others are inactive or even toxic. Therefore, understanding stereoisomerism is crucial for designing and synthesizing effective and safe drugs.

"Cornus" is a genus name that refers to a group of plants commonly known as dogwoods. These plants belong to the family Cornaceae and are native to the temperate regions of the Northern Hemisphere. There are around 30-60 species in this genus, depending on the classification system used.

Dogwoods are deciduous or evergreen shrubs or small trees that typically have opposite, simple leaves and showy flowers. The flowers are often surrounded by large, modified bracts that can be white, pink, or yellow. The fruit of dogwoods is a small, fleshy drupe that contains one to four seeds.

Some species of Cornus have medicinal properties. For example, the bark of Cornus florida (flowering dogwood) and Cornus mas (Cornelian cherry) has been used in traditional medicine to treat fever, diarrhea, and other ailments. However, it is important to note that the use of these plants for medicinal purposes should be done under the guidance of a qualified healthcare professional, as they can also have toxic effects if not used properly.

"Psidium" is a scientific name for a genus of plants that include several species of tropical trees and shrubs, the most well-known of which is "Psidium guajava," or the common guava. These plants are native to Central and South America and are now grown in many tropical and subtropical regions around the world.

The fruits of these plants are also commonly referred to as "guavas" and are popular for their sweet, tangy flavor and high nutritional content. They are rich in vitamin C, dietary fiber, and antioxidants, making them a valuable addition to a healthy diet.

In medical or scientific contexts, the term "Psidium" may be used to refer specifically to the genus of plants or more broadly to any plant or fruit within that genus.

'Cynanchum' is a genus of plants in the family Apocynaceae, also known as Milkweed or Dogbane family. These plants are primarily found in tropical and subtropical regions around the world. Some species of Cynanchum have medicinal uses, including treatments for skin conditions, inflammation, and pain relief. However, it's important to note that some species may contain toxic compounds and should only be used under the guidance of a medical professional.

Naphthacenes are hydrocarbon compounds that consist of a naphthalene ring fused to two additional benzene rings. They belong to the class of polycyclic aromatic hydrocarbons (PAHs) and have been studied for their potential carcinogenic properties. Naphthacenes can be found in various environmental sources, including air pollution from vehicle emissions and cigarette smoke. However, it's important to note that specific medical definitions related to diseases or conditions are not typically associated with naphthacenes.

Glycoside hydrolases are classified into EC 3.2.1 as enzymes catalyzing the hydrolysis of O- or S-glycosides. Glycoside ... List of glycoside hydrolase families Clans of glycoside hydrolases Hierarchical classification of the TIM-barrel type glycoside ... Mutant glycoside hydrolases termed glycosynthases have been developed that can achieve the synthesis of glycosides in high ... Glycoside hydrolases (also called glycosidases or glycosyl hydrolases) catalyze the hydrolysis of glycosidic bonds in complex ...
In molecular biology, glycoside hydrolase family 70 is a family of glycoside hydrolases. Glycoside hydrolases EC 3.2.1. are a ... "Glycoside Hydrolase Family 70". CAZypedia.org. Retrieved 2018-03-06. CAZypedia Consortium (December 2018). "Ten years of ... A classification system for glycoside hydrolases, based on sequence similarity, has led to the definition of >100 different ... Davies G, Henrissat B (September 1995). "Structures and mechanisms of glycosyl hydrolases". Structure. 3 (9): 853-9. doi: ...
In molecular biology, glycoside hydrolase family 36 is a family of glycoside hydrolases. Glycoside hydrolases EC 3.2.1. are a ... Glycoside hydrolase family 36 together with family 31 and family 27 alpha-galactosidases form the glycosyl hydrolase clan GH-D ... Glycoside hydrolase family 36 can be subdivided into 11 families, GH36A to GH36K. Henrissat B, Callebaut I, Mornon JP, Fabrega ... Glycoside hydrolase family 36 also includes enzymes with α-N-acetylgalactosaminidase EC 3.2.1.49 and stachyose synthase EC 2.4. ...
In molecular biology, glycoside hydrolase family 108 is a family of glycoside hydrolases. Glycoside hydrolases EC 3.2.1. are a ... Glycoside hydrolase family 108 CAZY GH_108 includes enzymes with lysozyme (N-acetylmuramidase) EC 3.2.1.17 activity. A glutamic ... "Glycoside Hydrolase Family 108". CAZypedia.org. Retrieved 2018-03-06. CAZypedia Consortium (December 2018). "Ten years of ... A classification system for glycoside hydrolases, based on sequence similarity, has led to the definition of >100 different ...
In molecular biology, glycoside hydrolase family 35 is a family of glycoside hydrolases. Glycoside hydrolases EC 3.2.1. are a ... Glycoside hydrolase family 35 CAZY GH_35 comprises enzymes with only one known activity; beta-galactosidase (EC 3.2.1.23). ... "Glycoside Hydrolase Family 35". CAZypedia.org. Retrieved 2018-03-06. CAZypedia Consortium (December 2018). "Ten years of ... A classification system for glycoside hydrolases, based on sequence similarity, has led to the definition of >100 different ...
... is a family of glycoside hydrolases. Glycoside hydrolases EC 3.2.1. are a widespread group of ... Glycoside hydrolase family 1 CAZY GH_1 comprises enzymes with a number of known activities; beta-glucosidase (EC 3.2.1.21); ... "Glycoside Hydrolase Family 1". CAZypedia.org. Retrieved 2018-03-06. CAZypedia Consortium (December 2018). "Ten years of ... A classification system for glycoside hydrolases, based on sequence similarity, has led to the definition of >100 different ...
In molecular biology, glycoside hydrolase family 63 is a family of glycoside hydrolases. Glycoside hydrolases EC 3.2.1. are a ... "Glycoside Hydrolase Family 63". CAZypedia.org. Retrieved 2018-03-06. CAZypedia Consortium (December 2018). "Ten years of ... A classification system for glycoside hydrolases, based on sequence similarity, has led to the definition of >100 different ... Glycosyl hydrolase family 63 (CAZY GH_63) is a family of eukaryotic enzymes. They catalyse the specific cleavage of the non- ...
In molecular biology, glycoside hydrolase family 100 is a family of glycoside hydrolases. Glycoside hydrolases EC 3.2.1. are a ... Glycoside hydrolase family 100 CAZY GH_100 includes enzymes with invertase activity EC 3.2.1.26. Henrissat B, Callebaut I, ... "Glycoside Hydrolase Family 100". CAZypedia.org. Retrieved 2018-03-06. CAZypedia Consortium (December 2018). "Ten years of ... A classification system for glycoside hydrolases, based on sequence similarity, has led to the definition of >100 different ...
In molecular biology, Glycoside hydrolase family 11 is a family of glycoside hydrolases. Glycoside hydrolases EC 3.2.1. are a ... Glycoside hydrolase family 11 CAZY GH_11 comprises enzymes with only one known activity, xylanase (EC 3.2.1.8). These enzymes ... "Glycoside Hydrolase Family 11". CAZypedia.org. Retrieved 2018-03-06. CAZypedia Consortium (December 2018). "Ten years of ... A classification system for glycoside hydrolases, based on sequence similarity, has led to the definition of >100 different ...
In molecular biology, glycoside hydrolase family 39 is a family of glycoside hydrolases. Glycoside hydrolases EC 3.2.1. are a ... Glycoside hydrolase family 39 CAZY GH_39 comprises enzymes with several known activities; alpha-L-iduronidase (EC 3.2.1.76); ... "Glycoside Hydrolase Family 39". CAZypedia.org. Retrieved 2018-03-06. CAZypedia Consortium (December 2018). "Ten years of ... A classification system for glycoside hydrolases, based on sequence similarity, has led to the definition of >100 different ...
In molecular biology, glycoside hydrolase family 66 is a family of glycoside hydrolases. Glycoside hydrolases EC 3.2.1. are a ... Glycoside hydrolase family 66 CAZY GH_66 includes enzymes with cycloisomaltooligosaccharide glucanotransferase EC 2.4.1.248 and ... "Glycoside Hydrolase Family 66". CAZypedia.org. Retrieved 2018-03-06. CAZypedia Consortium (December 2018). "Ten years of ... A classification system for glycoside hydrolases, based on sequence similarity, has led to the definition of >100 different ...
In molecular biology, glycoside hydrolase family 24 is a family of glycoside hydrolases. Glycoside hydrolases EC 3.2.1. are a ... Glycoside hydrolase family 24 CAZY GH_24 comprises enzymes with only one known activity; lysozyme (EC 3.2.1.17). This family ... "Glycoside Hydrolase Family 24". CAZypedia.org. Retrieved 2018-03-06. CAZypedia Consortium (December 2018). "Ten years of ... A classification system for glycoside hydrolases, based on sequence similarity, has led to the definition of >100 different ...
In molecular biology, glycoside hydrolase family 77 is a family of glycoside hydrolases. Glycoside hydrolases EC 3.2.1. are a ... "Glycoside Hydrolase Family 77". CAZypedia.org. Retrieved 2018-03-06. CAZypedia Consortium (December 2018). "Ten years of ... A classification system for glycoside hydrolases, based on sequence similarity, has led to the definition of >100 different ... This article incorporates text from the public domain Pfam and InterPro: IPR003385 Portal: Biology (EC 3.2.1, Glycoside ...
In molecular biology, glycoside hydrolase family 65 is a family of glycoside hydrolases. Glycoside hydrolases EC 3.2.1. are a ... "Glycoside Hydrolase Family 65". CAZypedia.org. Retrieved 2018-03-06. CAZypedia Consortium (December 2018). "Ten years of ... A classification system for glycoside hydrolases, based on sequence similarity, has led to the definition of >100 different ... This family of glycosyl hydrolases (CAZY GH_65) includes vacuolar acid trehalase and maltose phosphorylases. Maltose ...
In molecular biology, Glycoside hydrolase family 18 is a family of glycoside hydrolases. Glycoside hydrolases EC 3.2.1. are a ... "Glycoside Hydrolase Family 18". CAZypedia.org. Retrieved 2018-03-06. CAZypedia Consortium (December 2018). "Ten years of ... A classification system for glycoside hydrolases, based on sequence similarity, has led to the definition of >100 different ... Davies G, Henrissat B (September 1995). "Structures and mechanisms of glycosyl hydrolases". Structure. 3 (9): 853-9. doi: ...
In molecular biology, glycoside hydrolase family 33 is a family of glycoside hydrolases. Glycoside hydrolases EC 3.2.1. are a ... "Glycoside Hydrolase Family 33". CAZypedia.org. Retrieved 2018-03-06. CAZypedia Consortium (December 2018). "Ten years of ... A classification system for glycoside hydrolases, based on sequence similarity, has led to the definition of >100 different ... Portal: Biology (EC 3.2.1, Glycoside hydrolase families, Protein families). ...
In molecular biology, glycoside hydrolase family 7 is a family of glycoside hydrolases EC 3.2.1., which are a widespread group ... Glycoside hydrolase family 7 CAZY GH_7 comprises enzymes with several known activities including endoglucanase (EC 3.2.1.4) and ... "Glycoside Hydrolase Family 7". CAZypedia.org. Retrieved 2018-03-06. CAZypedia Consortium (December 2018). "Ten years of ... A classification system for glycoside hydrolases, based on sequence similarity, has led to the definition of >100 different ...
In molecular biology, glycoside hydrolase family 92 is a family of glycoside hydrolases. Glycoside hydrolases EC 3.2.1. are a ... Glycoside hydrolase family 92 includes enzymes with mannosyl-oligosaccharide α-1,2-mannosidase EC 3.2.1.113, mannosyl- ... "Glycoside Hydrolase Family 92". CAZypedia.org. Retrieved 2018-03-06. CAZypedia Consortium (December 2018). "Ten years of ... A classification system for glycoside hydrolases, based on sequence similarity, has led to the definition of >100 different ...
In molecular biology, glycoside hydrolase family 71 is a family of glycoside hydrolases. Glycoside hydrolases EC 3.2.1. are a ... "Glycoside Hydrolase Family 71". CAZypedia.org. Retrieved 2018-03-06. CAZypedia Consortium (December 2018). "Ten years of ... A classification system for glycoside hydrolases, based on sequence similarity, has led to the definition of >100 different ... Davies G, Henrissat B (September 1995). "Structures and mechanisms of glycosyl hydrolases". Structure. 3 (9): 853-9. doi: ...
In molecular biology, Glycoside hydrolase family 10 is a family of glycoside hydrolases. Glycoside hydrolases EC 3.2.1. are a ... Glycoside hydrolase family 10 CAZY GH_10 comprises enzymes with a number of known activities; xylanase (EC 3.2.1.8); endo-1,3- ... "Glycoside Hydrolase Family 10". CAZypedia.org. Retrieved 2018-03-06. CAZypedia Consortium (December 2018). "Ten years of ... A classification system for glycoside hydrolases, based on sequence similarity, has led to the definition of >100 different ...
In molecular biology, glycoside hydrolase family 78 is a family of glycoside hydrolases. Glycoside hydrolases EC 3.2.1. are a ... Glycoside hydrolase family 78 CAZY GH_78 includes enzymes with α-L-rhamnosidase EC 3.2.1.40 activity. This family includes ... "Glycoside Hydrolase Family 78". CAZypedia.org. Retrieved 2018-03-06. CAZypedia Consortium (December 2018). "Ten years of ... A classification system for glycoside hydrolases, based on sequence similarity, has led to the definition of >100 different ...
In molecular biology, glycoside hydrolase family 44 is a family of glycoside hydrolases. Glycoside hydrolases EC 3.2.1. are a ... Glycoside hydrolase family 44 CAZY GH_44, formerly known as cellulase family J, includes enzymes with endoglucanase EC 3.2.1.4 ... "Glycoside Hydrolase Family 44". CAZypedia.org. Retrieved 2018-03-06. CAZypedia Consortium (December 2018). "Ten years of ... A classification system for glycoside hydrolases, based on sequence similarity, has led to the definition of >100 different ...
... is a family of glycoside hydrolases. It folds into a TIM barrel. Glycoside hydrolases EC 3.2.1. ... y[ _]9 Glycoside hydrolase family 17 CAZY GH_17 comprises enzymes with several known activities; endo-1,3-beta-glucosidase (EC ... "Glycoside Hydrolase Family 17". CAZypedia.org. Retrieved 2018-03-06. CAZypedia Consortium (December 2018). "Ten years of ... A classification system for glycoside hydrolases, based on sequence similarity, has led to the definition of >100 different ...
In molecular biology, glycoside hydrolase family 73 is a family of glycoside hydrolases. Glycoside hydrolases EC 3.2.1. are a ... Glycoside hydrolase family 73 CAZY GH_73 includes peptidoglycan hydrolases with endo-β-N-acetylglucosaminidase specificity. ... "Glycoside Hydrolase Family 73". CAZypedia.org. Retrieved 2018-03-06. CAZypedia Consortium (December 2018). "Ten years of ... A classification system for glycoside hydrolases, based on sequence similarity, has led to the definition of >100 different ...
In molecular biology, glycoside hydrolase family 37 is a family of glycoside hydrolases. Glycoside hydrolases EC 3.2.1. are a ... Glycoside hydrolase family 37 CAZY GH_37 comprises enzymes with only one known activity; trehalase (EC 3.2.1.28). Trehalase is ... "Glycoside Hydrolase Family 3". CAZypedia.org. Retrieved 2018-03-06. CAZypedia Consortium (December 2018). "Ten years of ... A classification system for glycoside hydrolases, based on sequence similarity, has led to the definition of >100 different ...
In molecular biology, glycoside hydrolase family 79 is a family of glycoside hydrolases. Glycoside hydrolases EC 3.2.1. are a ... Glycoside hydrolase family 79 includes endo-beta-N-glucuronidase EC 3.2.1.31 and heparanase (CAZY GH_79). Heparan sulphate ... "Glycoside Hydrolase Family 79". CAZypedia.org. Retrieved 2018-03-06. CAZypedia Consortium (December 2018). "Ten years of ... A classification system for glycoside hydrolases, based on sequence similarity, has led to the definition of >100 different ...
In molecular biology, glycoside hydrolase family 75 is a family of glycoside hydrolases. Glycoside hydrolases EC 3.2.1. are a ... Glycoside hydrolase family 75 CAZY GH_75 includes enzymes with chitosanase EC 3.2.1.132 activity. This family includes several ... "Glycoside Hydrolase Family 75". CAZypedia.org. Retrieved 2018-03-06. CAZypedia Consortium (December 2018). "Ten years of ... A classification system for glycoside hydrolases, based on sequence similarity, has led to the definition of >100 different ...
In molecular biology, glycoside hydrolase family 67 is a family of glycoside hydrolases. Glycoside hydrolases EC 3.2.1. are a ... Glycoside hydrolase family 67 includes alpha-glucuronidases, these are components of an ensemble of enzymes central to the ... "Glycoside Hydrolase Family 67". CAZypedia.org. Retrieved 2018-03-06. CAZypedia Consortium (December 2018). "Ten years of ... A classification system for glycoside hydrolases, based on sequence similarity, has led to the definition of >100 different ...
In molecular biology, glycoside hydrolase family 76 is a family of glycoside hydrolases. Glycoside hydrolases EC 3.2.1. are a ... Glycoside hydrolase family 76 is a family of alpha-1,6-mannanases (EC 3.2.1.101) (CAZY GH_76). Henrissat B, Callebaut I, ... "Glycoside Hydrolase Family 76". CAZypedia.org. Retrieved 2018-03-06. CAZypedia Consortium (December 2018). "Ten years of ... A classification system for glycoside hydrolases, based on sequence similarity, has led to the definition of >100 different ...
In molecular biology, glycoside hydrolase family 52 is a family of glycoside hydrolases. Glycoside hydrolases EC 3.2.1. are a ... Glycoside hydrolase family 52 CAZY GH_52 comprises enzymes with only one known activity; beta-xylosidase (EC 3.2.1.37). ... "Glycoside Hydrolase Family 52". CAZypedia.org. Retrieved 2018-03-06. CAZypedia Consortium (December 2018). "Ten years of ... A classification system for glycoside hydrolases, based on sequence similarity, has led to the definition of >100 different ...
Glycoside hydrolases are classified into EC 3.2.1 as enzymes catalyzing the hydrolysis of O- or S-glycosides. Glycoside ... List of glycoside hydrolase families Clans of glycoside hydrolases Hierarchical classification of the TIM-barrel type glycoside ... Mutant glycoside hydrolases termed glycosynthases have been developed that can achieve the synthesis of glycosides in high ... Glycoside hydrolases (also called glycosidases or glycosyl hydrolases) catalyze the hydrolysis of glycosidic bonds in complex ...
Thermostable GH159 glycoside hydrolase from Caldicellulosiruptor at 1.7 A ... and preliminary structural properties are reported for three glycoside hydrolases of the recently described glycoside hydrolase ... and preliminary structural properties are reported for three glycoside hydrolases of the recently described glycoside hydrolase ... Biochemical and Structural Characterization of Thermostable GH159 Glycoside Hydrolases Exhibiting alpha-L-Arabinofuranosidase ...
Glycoside hydrolases are also referred to as glycosidases. Glycoside hydrolases can catalyze the hydrolysis of O-, N- and S- ... Glycoside hydrolases are enzymes that catalyze the hydrolysis of the glycosidic linkage of glycosides, leading to the formation ... linked glycosides. Classification. Glycoside hydrolases can be classified in many different ways. The following paragraphs list ... Glycoside Hydrolase Firsts. First sterochemistry determination. Cite some reference here, with a short explanation [1].. First ...
Glycoside Hydrolase Family 9. From CAZypedia. Revision as of 13:18, 18 December 2021 by Harry Brumer. (talk , contribs) (Text ... Honda Y, Arai S, Suzuki K, Kitaoka M, and Fushinobu S. (2016). The crystal structure of an inverting glycoside hydrolase family ... Yoshida K and Komae K. (2006). A rice family 9 glycoside hydrolase isozyme with broad substrate specificity for hemicelluloses ... Indeed, as one of the first glycoside hydrolase families classified by hydrophobic cluster analysis, GH9 was previously known ...
The Gram-negative bacterium Azotobacter chroococcum NCIMB 8003 employs a new glycoside hydrolase family 70 4,6-α- ... The Gram-negative bacterium Azotobacter chroococcum NCIMB 8003 employs a new glycoside hydrolase family 70 4,6-α- ...
How to cite: Bonnardel F, Kumar A, Wimmerova M, Lahmann M, Perez S, Varrot A, Lisacek F, Imberty A. Architecture and Evolution of Blade Assembly in β-propeller Lectins. Structure. 2019 May 7;27(5):764-775.e3. doi:10.1016/j.str.2019.02.002. Epub 2019 Mar 7. PMID: 30853410 ...
Plant receptor-like protein activation by a microbial glycoside hydrolase *Yue Sun ...
LPMOs are widespread in Nature and are best known for their synergistic role with glycoside hydrolases in the conversion of ... including glycoside hydrolases (GHs) from families 3, 5, 6, 9, 12, and 48 (i.e., typical cellulases2), in addition to GHs from ... and glycoside hydrolases belonging to families 5 (cellulases/mannanases) and 18 (chitinases). The yellow stars in subclade A3 ...
"Use of Nanostructure-Initiator Mass Spectrometry to Deduce Selectivity of Reaction in Glycoside Hydrolases," Frontiers in ... Improving the annotation of glycoside hydrolase (GH) phylogenetic trees will improve understanding of the function, synergy, ... Mass Spectrometry Deduces Selectivity of Glycoside Hydrolases for Degrading Biomass Polysaccharides. Improving the annotation ...
The genome of Rhodothermus marinus DSM 4253 encodes six glycoside hydrolases (GH) classified under GH family 3 (GH3): RmBgl3A, ... The genome of Rhodothermus marinus DSM 4253 encodes six glycoside hydrolases (GH) classified under GH family 3 (GH3): RmBgl3A, ... Glycoside Hydrolases / chemistry * Glycoside Hydrolases / classification * Glycoside Hydrolases / genetics* * Glycoside ...
Functional diversification of horizontally acquired glycoside hydrolase family 45 (GH45) proteins in Phytophaga beetles ... Functional diversification of horizontally acquired glycoside hydrolase family 45 (GH45) proteins in Phytophaga beetles Busch, ... Recently, it has become clear that some animals encode endogenous cellulases belonging to several glycoside. hydrolase families ... of horizontally acquired glycoside hydrolase family 45 (GH45) proteins in Phytophaga beetles. BMC Evolutionary Biology, 19: 100 ...
Glycoside hydrolase (GH) family members act as virulence factors and regulate plant immune responses during pathogen infection ... The glycoside hydrolase 28 member VdEPG1 is a virulence factor of Verticillium dahliae and interacts with the jasmonic acid ... The glycoside hydrolase 28 member VdEPG1 is a virulence factor of Verticillium dahliae and ...
Six multidomain glycoside hydrolases (GHs), CelA (Athe_1867), CelB (Athe_1859), CelC (Athe_1857), CelD (Athe_1866), CelE (Athe_ ... N2 - Six multidomain glycoside hydrolases (GHs), CelA (Athe_1867), CelB (Athe_1859), CelC (Athe_1857), CelD (Athe_1866), CelE ( ... AB - Six multidomain glycoside hydrolases (GHs), CelA (Athe_1867), CelB (Athe_1859), CelC (Athe_1857), CelD (Athe_1866), CelE ( ... abstract = "Six multidomain glycoside hydrolases (GHs), CelA (Athe_1867), CelB (Athe_1859), CelC (Athe_1857), CelD (Athe_1866 ...
In this study, we found 61 families of glycoside hydrolases (GH) (out of 182 CAZymes) from protein sequences deposited in the ... Fibrolytic bacteria and glycoside hydrolases are abundant in feed efficient cattle. A Log2-fold increase in the abundance of F ... Neves, A.L.A., Yu, J., Suzuki, Y. et al. Accelerated discovery of novel glycoside hydrolases using targeted functional ... Discovery of glycoside hydrolases through phenotype-based selective pressure on the rumen microbial community. Since there is ...
Glycoside Hydrolases GlycosylTransferases Polysaccharide Lyases Carbohydrate Esterases Auxiliary Activities Carbohydrate- ...
Glycoside Hydrolases GlycosylTransferases Polysaccharide Lyases Carbohydrate Esterases Auxiliary Activities Carbohydrate- ...
Probing electrostatic interactions along the reaction pathway of a glycoside hydrolase: Histidine characterization by NMR ... Probing electrostatic interactions along the reaction pathway of a glycoside hydrolase: Histidine characterization by NMR ... Probing electrostatic interactions along the reaction pathway of a glycoside hydrolase: Histidine characterization by NMR ... of the histidine residues are discussed in terms of their structural and functional roles in this model glycoside hydrolase. ...
... multiple glycoside hydrolases from diverse families. We furthermore uncover previously underestimated, and highly complex ...
The Oryza sativa Branching Enzyme 1 (OsBE1) gene, encoding a glycoside hydrolase family 13 protein, was cloned from rice. The ... 3]Wang X C, Yang Z R, Wang M, Meng L Z, Jiang Y W, Han Y H. The BRANCHING ENZYME1 gene, encoding a glycoside hydrolase family ... 2]Wang X C, Xue L, Sun J Q, Zuo J R. The Arabidopsis BE1 gene, encoding a putative glycoside hydrolase localized in plastids, ... Key words: Glycoside hydrolase, Carbohydrate metabolism, OsBE1, Chloroplast, Rice (Oryza sativa L.) ...
T2 - Molecular evolution of glycoside hydrolase genes in the western corn rootworm (Diabrotica virgifera virgifera) (PLoS ONE ( ... Correction: Molecular evolution of glycoside hydrolase genes in the western corn rootworm (Diabrotica virgifera virgifera) ( ... Correction: Molecular evolution of glycoside hydrolase genes in the western corn rootworm (Diabrotica virgifera virgifera) ( ... Correction: Molecular evolution of glycoside hydrolase genes in the western corn rootworm (Diabrotica virgifera virgifera) ( ...
CRYSTAL STRUCTURE OF GLYCOSIDE HYDROLASE FAMILY 3 BETA- GLUCOSIDASE CEL3A FROM THE MODERATELY THERMOPHILIC FUNGUS RASAMSONIA ... CRYSTAL STRUCTURE OF GLYCOSIDE HYDROLASE FAMILY 3 BETA- GLUCOSIDASE CEL3A FROM THE MODERATELY THERMOPHILIC FUNGUS RASAMSONIA ... CRYSTAL STRUCTURE OF GLYCOSIDE HYDROLASE FAMILY 3 BETA- GLUCOSIDASE CEL3A FROM THE MODERATELY THERMOPHILIC FUNGUS RASAMSONIA ...
Biochemical and Structural Analyses of a Bacterial Endo-β-1,2-Glucanase Reveal A New Glycoside Hydrolase Family. 0 ... Biochemical and Structural Analyses of a Bacterial Endo-β-1,2-Glucanase Reveal A New Glycoside Hydrolase Family. Journal of ...
Parrent, JL, James, TY, Vasaitis, R & Taylor, AFS 2009, Friend or foe? Evolutionary history of glycoside hydrolase family 32 ... Friend or foe? Evolutionary history of glycoside hydrolase family 32 genes encoding for sucrolytic activity in fungi and its ... Dive into the research topics of Friend or foe? Evolutionary history of glycoside hydrolase family 32 genes encoding for ... Friend or foe? Evolutionary history of glycoside hydrolase family 32 genes encoding for sucrolytic activity in fungi and its ...
Glycoside hydrolase, family 3, N-terminal domain. The name of this superfamily has been modified since the most recent official ...
Chitinases are glycosyl hydrolases that catalyze the hydrolysis of the β-1,4 linkages in complex carbohydrates and those that ... of glycoside hydrolases. Curr Opin Struct Biol 7:637- 644. https://doi.org/ ... Chitinases are glycosyl hydrolases (GHs) that belong to the GH18 and GH19 families ... Chitinases are glycosyl hydrolases that catalyze the hydrolysis of the β-1,4 linkages in complex carbohydrates and those that ...
IPR017853 Glycoside hydrolase superfamily. Molecular. Reagents less. * All nucleic 24. cDNA 23 ...
Glycoside hydrolase, family 47. ENSTGUP00000013755. Pfam. PF00010. IPR011598. 20. 69. 6.20e-11. Myc-type, basic helix-loop- ...
IPR000322 Glycoside hydrolase family 31, TIM barrel domain. IPR017853 Glycoside hydrolase superfamily ...
Functional genomic analysis of Arabidopsis thaliana glycoside hydrolase family 1 施明哲. Xu Z, Escamilla-Trevino L, Zeng L, ... Functional genomic analysis of Arabidopsis thaliana glycoside hydrolase family 1 Plant Molecular Biology, 55(3), 343-367 ...
  • Glycoside hydrolases (also called glycosidases or glycosyl hydrolases) catalyze the hydrolysis of glycosidic bonds in complex sugars. (wikipedia.org)
  • Glycoside hydrolases are classified into EC 3.2.1 as enzymes catalyzing the hydrolysis of O- or S-glycosides. (wikipedia.org)
  • Glycoside hydrolases can also be classified according to the stereochemical outcome of the hydrolysis reaction: thus they can be classified as either retaining or inverting enzymes. (wikipedia.org)
  • Glycoside hydrolases are enzymes that catalyze the hydrolysis of the glycosidic linkage of glycosides, leading to the formation of a sugar hemiacetal or hemiketal and the corresponding free aglycon. (cazypedia.org)
  • Glycoside hydrolases can catalyze the hydrolysis of O-, N- and S-linked glycosides. (cazypedia.org)
  • Retaining and inverting classification refers to the stereochemical outcome of the hydrolysis reaction catalyzed by the glycoside hydrolase. (cazypedia.org)
  • Chitinases are glycosyl hydrolases that catalyze the hydrolysis of the β-1,4 linkages in complex carbohydrates and those that contain GlcNAc. (researchgate.net)
  • Agarases are glycoside hydrolases that catalyze the hydrolysis of agar. (worthington-biochem.com)
  • β-galactosidase , also called lactase , beta-gal or β-gal , is a glycoside hydrolase enzyme that catalyzes the hydrolysis of β-galactosides into monosaccharides through the breaking of a glycosidic bond . (wikidoc.org)
  • Functional, biochemical, and preliminary structural properties are reported for three glycoside hydrolases of the recently described glycoside hydrolase (GH) family 159. (rcsb.org)
  • Indeed, as one of the first glycoside hydrolase families classified by hydrophobic cluster analysis, GH9 was previously known as "Cellulase Family E" [ 1 , 2 ]. (cazypedia.org)
  • The genome of Rhodothermus marinus DSM 4253 encodes six glycoside hydrolases (GH) classified under GH family 3 (GH3): RmBgl3A, RmBgl3B, RmBgl3C, RmXyl3A, RmXyl3B and RmNag3. (nih.gov)
  • Glycoside hydrolase (GH) family members act as virulence factors and regulate plant immune responses during pathogen infection . (bvsalud.org)
  • 3]Wang X C, Yang Z R, Wang M, Meng L Z, Jiang Y W, Han Y H. The BRANCHING ENZYME1 gene, encoding a glycoside hydrolase family 13 protein, is required for in vitro plant regeneration in Arabidopsis. (chinacrops.org)
  • Photosynthate within plants is transported from source to sink tissues as sucrose, which is hydrolyzed by plant glycosyl hydrolase family 32 enzymes (GH32) into its constituent monosaccharides to meet plant cellular demands. (elsevierpure.com)
  • Based on catalytic domain similarities, β-Agarase II of Pseudoalteromonas atlantica has been designated part of the glycosyl hydrolase 86 (GH86) family. (worthington-biochem.com)
  • Substrate Specificity in Glycoside Hydrolase Family 10. (expasy.org)
  • Glycoside hydrolase from the GH76 family indicates that marine Salegentibacter sp. (mpg.de)
  • Keseluruhan sekuens asam amino menunjukkan tingkat kemiripan yang tinggi (98%) xylanase thermo-alkalistabil dari G. stearothermophilus T-6 yang digolongkan sebagai glycoside hydrolase family 10 (GH10). (biotrop.org)
  • The research focus is within the area "enzymes of extremophilic microorganisms", especially concerning thermostable glycoside hydrolases (including representatives from GH-family 1, 3, 10, 12 and 13). (lu.se)
  • 2016) Construction of the first thermostable β-glucosynthase derived from glycoside hydrolase family 3. (lu.se)
  • Four novel multidomain glycoside hydrolases (GHs) from Caldicellulosiruptor morganii and Caldicellulosiruptor danielii were produced recombinantly in Caldicellulosiruptor bescii and characterized. (ncsu.edu)
  • Six multidomain glycoside hydrolases (GHs), CelA (Athe_1867), CelB (Athe_1859), CelC (Athe_1857), CelD (Athe_1866), CelE (Athe_1865), and CelF (Athe_1860) are encoded in the Caldicellulosiruptor bescii glucan degradation locus (GDL). (princeton.edu)
  • Glycoside hydrolases are also referred to as glycosidases. (cazypedia.org)
  • Any member of the class of enzymes that catalyze the cleavage of the glycosidic linkage of glycosides and the addition of water to the resulting molecules. (bvsalud.org)
  • A classification system for glycosyl hydrolases, based on sequence similarity, has led to the definition of more than 100 different families. (wikipedia.org)
  • Recent progress in glycosidase sequence analysis and 3D structure comparison has allowed the proposal of an extended hierarchical classification of the glycoside hydrolases. (wikipedia.org)
  • Glycoside hydrolases can also be classified as exo or endo acting, dependent upon whether they act at the (usually non-reducing) end or in the middle, respectively, of an oligo/polysaccharide chain. (wikipedia.org)
  • Other β-agarases belong to glycosyl hydrolase families 16 and 50, with all three groups containing a conserved glycoside hydrolase region responsible for catalysis (Fu and Kim 2010). (worthington-biochem.com)
  • One of the important occurrences of glycoside hydrolases in bacteria is the enzyme beta-galactosidase (LacZ), which is involved in regulation of expression of the lac operon in E. coli. (wikipedia.org)
  • In this study, we found 61 families of glycoside hydrolases (GH) (out of 182 CAZymes) from protein sequences deposited in the CAZy database-currently associated with more than 20,324 microbial genomes. (biomedcentral.com)
  • Novel multidomain, multifunctional glycoside hydrolases from highly lignocellulolytic Caldicellulosiruptor species. (ncsu.edu)
  • Recently, it has become clear that some animals encode endogenous cellulases belonging to several glycoside hydrolase families (GHs), including GH45. (mpg.de)
  • In higher organisms glycoside hydrolases are found within the endoplasmic reticulum and Golgi apparatus where they are involved in processing of N-linked glycoproteins, and in the lysosome as enzymes involved in the degradation of carbohydrate structures. (wikipedia.org)
  • 2]Wang X C, Xue L, Sun J Q, Zuo J R. The Arabidopsis BE1 gene, encoding a putative glycoside hydrolase localized in plastids, plays crucial roles during embryogenesis and carbohydrate metabolism. (chinacrops.org)
  • Functional Characterization of the Glycoside Hydrolase Encoding Gene OsBE1 during Chloroplast Development in Oryza sativa [J].Acta Agron Sin, 2014, 40(12): 2090-2097. (chinacrops.org)
  • 3. Rather, MY, Ara KZG, Nordberg Karlsson E, Adlercreutz P. ( 2015 ) Characterization of cyclodextrin glycosyltransferases (CGTases) and their application for synthesis of alkyl glycosides with oligomeric head group. (lu.se)
  • 2015. "Use of Nanostructure-Initiator Mass Spectrometry to Deduce Selectivity of Reaction in Glycoside Hydrolases," Frontiers in Bioengineering and Biotechnology 3 (165), DOI: 10.3389/fbioe.2015.00165 . (berscience.org)
  • The diverse ionization behaviors of the histidine residues are discussed in terms of their structural and functional roles in this model glycoside hydrolase. (ubc.ca)
  • The glycoside hydrolase 28 member VdEPG1 is a virulence factor of Verticillium dahliae and interacts with the jasmonic acid pathway-related gene GhOPR9. (bvsalud.org)
  • exo - and endo - refers to the ability of a glycoside hydrolase to cleave a substrate at the end (most frequently, but not always the non-reducing end) or within the middle of a chain. (cazypedia.org)
  • The glycoside hydrolases are involved in the biosynthesis and degradation of glycogen in the body. (wikipedia.org)
  • Activity screening using a set of para -nitrophenyl ( p NP) glycosides suggested additional arabinosidase activity on substrates with arabinosyl residues, which has not been previously reported for members of GH159. (rcsb.org)
  • 5. Rather, MY, Nordberg Karlsson E, Adlercreutz P. ( 2015 ) Complexation of alkyl glycosides with α-cyclodextrin can have drastically different effects on their conversion by glycoside hydrolases. (lu.se)
  • Glycoside hydrolases are found in essentially all domains of life. (wikipedia.org)
  • Glycoside hydrolases are found in the intestinal tract and in saliva where they degrade complex carbohydrates such as lactose, starch, sucrose and trehalose. (wikipedia.org)
  • Improving the annotation of glycoside hydrolase (GH) phylogenetic trees will improve understanding of the function, synergy, and stability of these enzymes and thereby the creation of biomass-degrading enzymatic cocktails. (berscience.org)
  • Our results demonstrate that CcsZ is in fact an endo -acting cellulase belonging to glycoside hydrolase family 5 (GH-5). (biorxiv.org)
  • Novel acid trehalase belonging to glycoside hydrolase family 37 from Pleurotus sp. (bvsalud.org)
  • A classification system for glycosyl hydrolases, based on sequence similarity, has led to the definition of more than 100 different families. (wikipedia.org)
  • This gene encodes a glycoprotein member of the glycosyl hydrolase 18 family. (nih.gov)
  • N-GLYCOSYL HYDROLASES that catalyze the hydrolysis of the N-glycosidic bond of nucleoside-linked sugars. (nih.gov)
  • One of the important occurrences of glycoside hydrolases in bacteria is the enzyme beta-galactosidase (LacZ), which is involved in regulation of expression of the lac operon in E. coli. (wikipedia.org)
  • The lysozyme family of the glycoside hydrolases (GHs) catalyzes the cleavage of the β-1 → 4-glycosidic linkage connecting the N -acetylmuramic acid (MurNAc) and N -acetyl- d -glucosamine (GlcNAc) saccharides of the (MurNAc-GlcNAc) n polymer (the peptidoglycan) of the cell wall of bacteria. (nature.com)
  • The second part of the thesis focuses on glycoside hydrolases from bacteria that break down oligo- and polysaccharides. (kth.se)
  • Some glycoside hydrolases have broad specificity for hydrolysis of glycosidic bonds, potentially increasing their functional utility and flexibility in physiological and industrial applications. (doe.gov)
  • Any member of the class of enzymes that catalyze the cleavage of the glycosidic linkage of glycosides and the addition of water to the resulting molecules. (bvsalud.org)
  • Glycoside hydrolases cleave the glycosidic linkage between two carbohydrate moieties. (iastate.edu)
  • In one of the studies, a bacterial glycoside hydrolase from the acne bacterium Cutibacterium acnes was characterized. (kth.se)
  • In another study, a glycoside hydrolase from a bacterium living in the moose rumen was characterized. (kth.se)
  • Deficiency in specific lysosomal glycoside hydrolases can lead to a range of lysosomal storage disorders that result in developmental problems or death. (wikipedia.org)
  • Lysozymes, also known as muramidase or N-acetylmuramide glycanhydrolase, are glycoside hydrolases, enzymes (EC 3.2.1.17) that damage bacterial cell walls by catalyzing hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins. (gbiosciences.com)
  • Proteomic analysis of the T. aurantiacus culture supernatant revealed dominant glycoside hydrolases from families 5, 7, 10, and 61, proteins that are key enzymes in commercial cocktails. (biomedcentral.com)
  • Inhibition of the glycoside hydrolase O-GlcNAcase (OGA) prevents the removal of O-linked N -acetyl-d-glucosamine (O-GlcNAc) moieties from intracellular proteins and has emerged as an attractive therapeutic approach to prevent the formation of tau pathology. (nih.gov)
  • We also reveal that both Dictyostelium Cln5 and human CLN5 are glycoside hydrolases, providing the first evidence in any system linking a molecular function to CLN5. (nih.gov)
  • The enzymatic hydrolysis of alpha-mannosides is catalyzed by glycoside hydrolases (GH), termed alpha-mannosidases. (rcsb.org)
  • To test this hypothesis, we subcloned the putative glycoside hydrolase CcsZ and solved the X-ray crystal structure of both apo- and product-bound CcsZ. (biorxiv.org)
  • Glycoside hydrolases are found in the intestinal tract and in saliva where they degrade complex carbohydrates such as lactose, starch, sucrose and trehalose. (wikipedia.org)
  • Since taking up his lectureship at Newcastle in 1985 Harry Gilbert's research has focussed on enzymes, primarily glycoside hydrolases, which attack complex carbohydrates. (royalsociety.org)
  • Glycoside hydrolases (GHs) are enzymes that are able to rearrange the plant cell wall polysaccharides, being developmental- and stress-regulated. (intechopen.com)
  • The cellulolytic blend composed of the glycoside hydrolase (GH) domain GH12/GH5/GH1 allowed the conversion of alkaline-treated lignocellulose into glucose with efficiencies ranging from 14% to 17% upon 48h of reaction and an enzyme loading of 0.05% (w/w). (univr.it)
  • Clinically significant dumping syndrome occurs in approximately 10% of patients after any type of gastric surgery and in up to 50% of patients after laparoscopic Roux-en-Y gastric bypass. (medscape.com)