Coenzyme a transferases. Medical search

Small molecules that are required for the catalytic function of ENZYMES. Many VITAMINS are coenzymes.

Transferases are enzymes transferring a group, for example, the methyl group or a glycosyl group, from one compound (generally regarded as donor) to another compound (generally regarded as acceptor). The classification is based on the scheme "donor:acceptor group transferase". (Enzyme Nomenclature, 1992) EC 2.

A transferase that catalyzes the addition of aliphatic, aromatic, or heterocyclic FREE RADICALS as well as EPOXIDES and arene oxides to GLUTATHIONE. Addition takes place at the SULFUR. It also catalyzes the reduction of polyol nitrate by glutathione to polyol and nitrite.

A somewhat heterogeneous class of enzymes that catalyze the transfer of alkyl or related groups (excluding methyl groups). EC 2.5.

Enzymes which transfer coenzyme A moieties from acyl- or acetyl-CoA to various carboxylic acceptors forming a thiol ester. Enzymes in this group are instrumental in ketone body metabolism and utilization of acetoacetate in mitochondria. EC 2.8.3.

A lipid-soluble benzoquinone which is involved in ELECTRON TRANSPORT in mitochondrial preparations. The compound occurs in the majority of aerobic organisms, from bacteria to higher plants and animals.

Acetyl CoA participates in the biosynthesis of fatty acids and sterols, in the oxidation of fatty acids and in the metabolism of many amino acids. It also acts as a biological acetylating agent.

Enzymes that catalyze the formation of acyl-CoA derivatives. EC 6.2.1.

A class of enzymes that transfers substituted phosphate groups. EC 2.7.8.

A non-template-directed DNA polymerase normally found in vertebrate thymus and bone marrow. It catalyzes the elongation of oligo- or polydeoxynucleotide chains and is widely used as a tool in the differential diagnosis of acute leukemias in man. EC 2.7.7.31.

Enzymes that catalyze the reversible reduction of alpha-carboxyl group of 3-hydroxy-3-methylglutaryl-coenzyme A to yield MEVALONIC ACID.

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 rate dynamics in chemical or physical systems.

A sulfhydryl compound used to prevent urothelial toxicity by inactivating metabolites from ANTINEOPLASTIC AGENTS, such as IFOSFAMIDE or CYCLOPHOSPHAMIDE.

Enzymes from the transferase class that catalyze the transfer of acyl groups from donor to acceptor, forming either esters or amides. (From Enzyme Nomenclature 1992) EC 2.3.

A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.

A coenzyme composed of ribosylnicotinamide 5'-diphosphate coupled to adenosine 5'-phosphate by pyrophosphate linkage. It is found widely in nature and is involved in numerous enzymatic reactions in which it serves as an electron carrier by being alternately oxidized (NAD+) and reduced (NADH). (Dorland, 27th ed)

Acyltransferases that use AMINO ACYL TRNA as the amino acid donor in formation of a peptide bond. There are ribosomal and non-ribosomal peptidyltransferases.

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.

Enzymes that catalyze the transfer of N-acetylglucosamine from a nucleoside diphosphate N-acetylglucosamine to an acceptor molecule which is frequently another carbohydrate. EC 2.4.1.-.

A butyryl-beta-alanine that can also be viewed as pantoic acid complexed with BETA ALANINE. It is incorporated into COENZYME A and protects cells against peroxidative damage by increasing the level of GLUTATHIONE.

Enzymes that transfer the ADP-RIBOSE group of NAD or NADP to proteins or other small molecules. Transfer of ADP-ribose to water (i.e., hydrolysis) is catalyzed by the NADASES. The mono(ADP-ribose)transferases transfer a single ADP-ribose. POLY(ADP-RIBOSE) POLYMERASES transfer multiple units of ADP-ribose to protein targets, building POLY ADENOSINE DIPHOSPHATE RIBOSE in linear or branched chains.

An enzyme that catalyzes the synthesis of geranylgeranyl diphosphate from trans, trans-farnesyl diphosphate and isopentenyl diphosphate.

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 large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.

An intermediate in the pathway of coenzyme A formation in mammalian liver and some microorganisms.

The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.

A phylum of ARCHAEA comprising at least seven classes: Methanobacteria, Methanococci, Halobacteria (extreme halophiles), Archaeoglobi (sulfate-reducing species), Methanopyri, and the thermophiles: Thermoplasmata, and Thermococci.

The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.

A class of enzymes that transfers nucleotidyl residues. EC 2.7.7.

An enzyme that catalyzes the dehydration of 1,2-propanediol to propionaldehyde. EC 4.2.1.28.

The parts of a macromolecule that directly participate in its specific combination with another molecule.

A post-translational modification of proteins by the attachment of an isoprenoid to the C-terminal cysteine residue. The isoprenoids used, farnesyl diphosphate or geranylgeranyl diphosphate, are derived from the same biochemical pathway that produces cholesterol.

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.

A skin irritant that may cause dermatitis of both primary and allergic types. Contact sensitization with DNCB has been used as a measure of cellular immunity. DNCB is also used as a reagent for the detection and determination of pyridine compounds.

Nicotinamide adenine dinucleotide phosphate. A coenzyme composed of ribosylnicotinamide 5'-phosphate (NMN) coupled by pyrophosphate linkage to the 5'-phosphate adenosine 2',5'-bisphosphate. It serves as an electron carrier in a number of reactions, being alternately oxidized (NADP+) and reduced (NADPH). (Dorland, 27th ed)

Compounds that inhibit HMG-CoA reductases. They have been shown to directly lower cholesterol synthesis.

A species of halophilic archaea whose organisms are nonmotile. Habitats include freshwater and marine mud, animal-waste lagoons, and the rumens of ungulates.

Enzymes that catalyze the transfer of galactose from a nucleoside diphosphate galactose to an acceptor molecule which is frequently another carbohydrate. EC 2.4.1.-.

Enzymes that catalyze the transfer of N-acetylgalactosamine from a nucleoside diphosphate N-acetylgalactosamine to an acceptor molecule which is frequently another carbohydrate. EC 2.4.1.-.

A fatty acid coenzyme derivative which plays a key role in fatty acid oxidation and biosynthesis.

A subclass of enzymes which includes all dehydrogenases acting on primary and secondary alcohols as well as hemiacetals. They are further classified according to the acceptor which can be NAD+ or NADP+ (subclass 1.1.1), cytochrome (1.1.2), oxygen (1.1.3), quinone (1.1.5), or another acceptor (1.1.99).

A fungal metabolite isolated from cultures of Aspergillus terreus. The compound is a potent anticholesteremic agent. It inhibits 3-hydroxy-3-methylglutaryl coenzyme A reductase (HYDROXYMETHYLGLUTARYL COA REDUCTASES), which is the rate-limiting enzyme in cholesterol biosynthesis. It also stimulates the production of low-density lipoprotein receptors in the liver.

An enzyme that catalyzes the formation of CoA derivatives from ATP, acetate, and CoA to form AMP, pyrophosphate, and acetyl CoA. It acts also on propionates and acrylates. EC 6.2.1.1.

Nutritional factor found in milk, eggs, malted barley, liver, kidney, heart, and leafy vegetables. The richest natural source is yeast. It occurs in the free form only in the retina of the eye, in whey, and in urine; its principal forms in tissues and cells are as FLAVIN MONONUCLEOTIDE and FLAVIN-ADENINE DINUCLEOTIDE.

A subclass of enzymes of the transferase class that catalyze the transfer of a methyl group from one compound to another. (Dorland, 28th ed) EC 2.1.1.

Structurally related forms of an enzyme. Each isoenzyme has the same mechanism and classification, but differs in its chemical, physical, or immunological characteristics.

A coenzyme A derivative which plays a key role in the fatty acid synthesis in the cytoplasmic and microsomal systems.

The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.

The class of all enzymes catalyzing oxidoreduction reactions. The substrate that is oxidized is regarded as a hydrogen donor. The systematic name is based on donor:acceptor oxidoreductase. The recommended name will be dehydrogenase, wherever this is possible; as an alternative, reductase can be used. Oxidase is only used in cases where O2 is the acceptor. (Enzyme Nomenclature, 1992, p9)

An enzyme, sometimes called GGT, with a key role in the synthesis and degradation of GLUTATHIONE; (GSH, a tripeptide that protects cells from many toxins). It catalyzes the transfer of the gamma-glutamyl moiety to an acceptor amino acid.

Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.

A genus of anaerobic, rod-shaped METHANOBACTERIACEAE. Its organisms are nonmotile and use ammonia as the sole source of nitrogen. These methanogens are found in aquatic sediments, soil, sewage, and the gastrointestinal tract of animals.

Proteins found in any species of bacterium.

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.

Phosphoric or pyrophosphoric acid esters of polyisoprenoids.

A chemical reaction in which an electron is transferred from one molecule to another. The electron-donating molecule is the reducing agent or reductant; the electron-accepting molecule is the oxidizing agent or oxidant. Reducing and oxidizing agents function as conjugate reductant-oxidant pairs or redox pairs (Lehninger, Principles of Biochemistry, 1982, p471).

Enzymes catalyzing the transfer of an acetyl group, usually from acetyl coenzyme A, to another compound. EC 2.3.1.

Enzymes that catalyze the incorporation of deoxyribonucleotides into a chain of DNA. EC 2.7.7.-.

Enzymes which transfer sulfur atoms to various acceptor molecules. EC 2.8.1.

Proteins prepared by recombinant DNA technology.

Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.

Enzymes that catalyze the transfer of hexose groups. EC 2.4.1.-.

Enzymes of the transferase class that catalyze the transfer of a pentose group from one compound to another.

The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.

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)

Derivatives of ACETIC ACID. Included under this heading are a broad variety of acid forms, salts, esters, and amides that contain the carboxymethane structure.

Liquid chromatographic techniques which feature high inlet pressures, high sensitivity, and high speed.

An enzyme that catalyzes the synthesis of UDPgalactose from UTP and galactose-1-phosphate. It is present in low levels in fetal and infant liver, but increases with age, thereby enabling galactosemic infants who survive to develop the capacity to metabolize galactose. EC 2.7.7.10.

This is the active form of VITAMIN B 6 serving as a coenzyme for synthesis of amino acids, neurotransmitters (serotonin, norepinephrine), sphingolipids, aminolevulinic acid. During transamination of amino acids, pyridoxal phosphate is transiently converted into pyridoxamine phosphate (PYRIDOXAMINE).

The sum of the weight of all the atoms in a molecule.

Specific hydroxymethylglutaryl CoA reductases that utilize the cofactor NAD. In liver enzymes of this class are involved in cholesterol biosynthesis.

An enzyme that catalyzes the conversion of methylmalonyl-CoA to succinyl-CoA by transfer of the carbonyl group. It requires a cobamide coenzyme. A block in this enzymatic conversion leads to the metabolic disease, methylmalonic aciduria. EC 5.4.99.2.

A tripeptide with many roles in cells. It conjugates to drugs to make them more soluble for excretion, is a cofactor for some enzymes, is involved in protein disulfide bond rearrangement and reduces peroxides.

A derivative of LOVASTATIN and potent competitive inhibitor of 3-hydroxy-3-methylglutaryl coenzyme A reductase (HYDROXYMETHYLGLUTARYL COA REDUCTASES), which is the rate-limiting enzyme in cholesterol biosynthesis. It may also interfere with steroid hormone production. Due to the induction of hepatic LDL RECEPTORS, it increases breakdown of LDL CHOLESTEROL.

The functional hereditary units of BACTERIA.

The N-acetyl derivative of glucosamine.

The simplest saturated hydrocarbon. It is a colorless, flammable gas, slightly soluble in water. It is one of the chief constituents of natural gas and is formed in the decomposition of organic matter. (Grant & Hackh's Chemical Dictionary, 5th ed)

Closed vesicles of fragmented endoplasmic reticulum created when liver cells or tissue are disrupted by homogenization. They may be smooth or rough.

Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.

A cobalt-containing coordination compound produced by intestinal micro-organisms and found also in soil and water. Higher plants do not concentrate vitamin B 12 from the soil and so are a poor source of the substance as compared with animal tissues. INTRINSIC FACTOR is important for the assimilation of vitamin B 12.

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.

Oxidoreductases that are specific for ALDEHYDES.

Genetically engineered MUTAGENESIS at a specific site in the DNA molecule that introduces a base substitution, or an insertion or deletion.

The region of an enzyme that interacts with its substrate to cause the enzymatic reaction.

An enzyme that catalyzes the formation of acetoacetyl-CoA from two molecules of ACETYL COA. Some enzymes called thiolase or thiolase-I have referred to this activity or to the activity of ACETYL-COA C-ACYLTRANSFERASE.

A family of enzymes accepting a wide range of substrates, including phenols, alcohols, amines, and fatty acids. They function as drug-metabolizing enzymes that catalyze the conjugation of UDPglucuronic acid to a variety of endogenous and exogenous compounds. EC 2.4.1.17.

Cyclic TETRAPYRROLES based on the corrin skeleton.

An enzyme that catalyzes the formation of cholesterol esters by the direct transfer of the fatty acid group from a fatty acyl CoA derivative. This enzyme has been found in the adrenal gland, gonads, liver, intestinal mucosa, and aorta of many mammalian species. EC 2.3.1.26.

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).

Enzymes that catalyze the transfer of glucose from a nucleoside diphosphate glucose to an acceptor molecule which is frequently another carbohydrate. EC 2.4.1.-.

An enzyme that catalyzes the synthesis of acetylphosphate from acetyl-CoA and inorganic phosphate. Acetylphosphate serves as a high-energy phosphate compound. EC 2.3.1.8.

The relationship between the chemical structure of a compound and its biological or pharmacological activity. Compounds are often classed together because they have structural characteristics in common including shape, size, stereochemical arrangement, and distribution of functional groups.

A test used to determine whether or not complementation (compensation in the form of dominance) will occur in a cell with a given mutant phenotype when another mutant genome, encoding the same mutant phenotype, is introduced into that cell.

Enzymes of the transferase class that catalyze the conversion of L-aspartate and 2-ketoglutarate to oxaloacetate and L-glutamate. EC 2.6.1.1.

A condensation product of riboflavin and adenosine diphosphate. The coenzyme of various aerobic dehydrogenases, e.g., D-amino acid oxidase and L-amino acid oxidase. (Lehninger, Principles of Biochemistry, 1982, p972)

The study of crystal structure using X-RAY DIFFRACTION techniques. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)

Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control of gene action in enzyme synthesis.

Organic, monobasic acids derived from hydrocarbons by the equivalent of oxidation of a methyl group to an alcohol, aldehyde, and then acid. Fatty acids are saturated and unsaturated (FATTY ACIDS, UNSATURATED). (Grant & Hackh's Chemical Dictionary, 5th ed)

An enzyme that catalyzes the conversion of L-glutamate and water to 2-oxoglutarate and NH3 in the presence of NAD+. (From Enzyme Nomenclature, 1992) EC 1.4.1.2.

RNA sequences that serve as templates for protein synthesis. Bacterial mRNAs are generally primary transcripts in that they do not require post-transcriptional processing. Eukaryotic mRNA is synthesized in the nucleus and must be exported to the cytoplasm for translation. Most eukaryotic mRNAs have a sequence of polyadenylic acid at the 3' end, referred to as the poly(A) tail. The function of this tail is not known for certain, but it may play a role in the export of mature mRNA from the nucleus as well as in helping stabilize some mRNA molecules by retarding their degradation in the cytoplasm.

A zinc-containing enzyme which oxidizes primary and secondary alcohols or hemiacetals in the presence of NAD. In alcoholic fermentation, it catalyzes the final step of reducing an aldehyde to an alcohol in the presence of NADH and hydrogen.

The sequence of carbohydrates within POLYSACCHARIDES; GLYCOPROTEINS; and GLYCOLIPIDS.

Enzymes of the isomerase class that catalyze the transfer of acyl-, phospho-, amino- or other groups from one position within a molecule to another. EC 5.4.

The extent to which an enzyme retains its structural conformation or its activity when subjected to storage, isolation, and purification or various other physical or chemical manipulations, including proteolytic enzymes and heat.

The chemical or biochemical addition of carbohydrate or glycosyl groups to other chemicals, especially peptides or proteins. Glycosyl transferases are used in this biochemical reaction.

Established cell cultures that have the potential to propagate indefinitely.

An enzyme that catalyzes the transfer of UMP from UDPglucose to galactose 1-phosphate, forming UDPgalactose and glucose 1-phosphate. Deficiency in this enzyme is the major cause of GALACTOSEMIA. EC 2.7.7.12.

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 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 principal sterol of all higher animals, distributed in body tissues, especially the brain and spinal cord, and in animal fats and oils.

Consists of a polypeptide chain and 4'-phosphopantetheine linked to a serine residue by a phosphodiester bond. Acyl groups are bound as thiol esters to the pantothenyl group. Acyl carrier protein is involved in every step of fatty acid synthesis by the cytoplasmic system.

Enzymes that catalyze the cleavage of a carbon-carbon bond of a 3-hydroxy acid. (Dorland, 28th ed) EC 4.1.3.

An antitumor antibiotic produced by Streptomyces sparsogenes. It inhibits protein synthesis in 70S and 80S ribosomal systems.

An enzyme that catalyzes the synthesis of hydroxymethylglutaryl-CoA from acetyl-CoA and acetoacetyl-CoA. This is a key enzyme in steroid biosynthesis. This enzyme was formerly listed as EC 4.1.3.5.

The protein components of enzyme complexes (HOLOENZYMES). An apoenzyme is the holoenzyme minus any cofactors (ENZYME COFACTORS) or prosthetic groups required for the enzymatic function.

A species of the genus SACCHAROMYCES, family Saccharomycetaceae, order Saccharomycetales, known as "baker's" or "brewer's" yeast. The dried form is used as a dietary supplement.

An enzyme that catalyzes the conversion of 5-phosphoribosyl-1-pyrophosphate and hypoxanthine, guanine, or 6-mercaptopurine to the corresponding 5'-mononucleotides and pyrophosphate. The enzyme is important in purine biosynthesis as well as central nervous system functions. Complete lack of enzyme activity is associated with the LESCH-NYHAN SYNDROME, while partial deficiency results in overproduction of uric acid. EC 2.4.2.8.

Determination of the spectra of ultraviolet absorption by specific molecules in gases or liquids, for example Cl2, SO2, NO2, CS2, ozone, mercury vapor, and various unsaturated compounds. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)

Enzymes that catalyze the transfer of mannose from a nucleoside diphosphate mannose to an acceptor molecule which is frequently another carbohydrate. The group includes EC 2.4.1.32, EC 2.4.1.48, EC 2.4.1.54, and EC 2.4.1.57.

Compounds or agents that combine with an enzyme in such a manner as to prevent the normal substrate-enzyme combination and the catalytic reaction.

A rather large group of enzymes comprising not only those transferring phosphate but also diphosphate, nucleotidyl residues, and others. These have also been subdivided according to the acceptor group. (From Enzyme Nomenclature, 1992) EC 2.7.

An enzyme that catalyzes the deamination of ethanolamine to acetaldehyde. EC 4.3.1.7.

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.

Semiautonomous, self-reproducing organelles that occur in the cytoplasm of all cells of most, but not all, eukaryotes. Each mitochondrion is surrounded by a double limiting membrane. The inner membrane is highly invaginated, and its projections are called cristae. Mitochondria are the sites of the reactions of oxidative phosphorylation, which result in the formation of ATP. They contain distinctive RIBOSOMES, transfer RNAs (RNA, TRANSFER); AMINO ACYL T RNA SYNTHETASES; and elongation and termination factors. Mitochondria depend upon genes within the nucleus of the cells in which they reside for many essential messenger RNAs (RNA, MESSENGER). Mitochondria are believed to have arisen from aerobic bacteria that established a symbiotic relationship with primitive protoeukaryotes. (King & Stansfield, A Dictionary of Genetics, 4th ed)

Enzymes that catalyze the addition of a carboxyl group to a compound (carboxylases) or the removal of a carboxyl group from a compound (decarboxylases). EC 4.1.1.

An enzyme that catalyzes reversibly the transfer of phosphoethanolamine from CDP-ethanolamine to diacylglycerol to yield phosphatidylethanolamine (cephalin) and CMP. The enzyme is found in the endoplasmic reticulum. EC 2.7.8.1.

Intracellular fluid from the cytoplasm after removal of ORGANELLES and other insoluble cytoplasmic components.

Chromatography on non-ionic gels without regard to the mechanism of solute discrimination.

Short sequences (generally about 10 base pairs) of DNA that are complementary to sequences of messenger RNA and allow reverse transcriptases to start copying the adjacent sequences of mRNA. Primers are used extensively in genetic and molecular biology techniques.

A genus of anaerobic, irregular spheroid-shaped METHANOSARCINALES whose organisms are nonmotile. Endospores are not formed. These archaea derive energy via formation of methane from acetate, methanol, mono-, di-, and trimethylamine, and possibly, carbon monoxide. Organisms are isolated from freshwater and marine environments.

Derivatives of adipic acid. Included under this heading are a broad variety of acid forms, salts, esters, and amides that contain a 1,6-carboxy terminated aliphatic structure.

Compounds containing the -SH radical.

Enzyme that catalyzes the final step of fatty acid oxidation in which ACETYL COA is released and the CoA ester of a fatty acid two carbons shorter is formed.

A group of enzymes that catalyze the transfer of carboxyl- or carbamoyl- groups. EC 2.1.3.

A class of enzymes that catalyze geometric or structural changes within a molecule to form a single product. The reactions do not involve a net change in the concentrations of compounds other than the substrate and the product.(from Dorland, 28th ed) EC 5.

An enzyme that, in the pathway of cholesterol biosynthesis, catalyzes the condensation of isopentenyl pyrophosphate and dimethylallylpyrophosphate to yield pyrophosphate and geranylpyrophosphate. The enzyme then catalyzes the condensation of the latter compound with another molecule of isopentenyl pyrophosphate to yield pyrophosphate and farnesylpyrophosphate. EC 2.5.1.1.

Theoretical representations that simulate the behavior or activity of chemical processes or phenomena; includes the use of mathematical equations, computers, and other electronic equipment.

Artifactual vesicles formed from the endoplasmic reticulum when cells are disrupted. They are isolated by differential centrifugation and are composed of three structural features: rough vesicles, smooth vesicles, and ribosomes. Numerous enzyme activities are associated with the microsomal fraction. (Glick, Glossary of Biochemistry and Molecular Biology, 1990; from Rieger et al., Glossary of Genetics: Classical and Molecular, 5th ed)

Derivatives of SUCCINIC ACID. Included under this heading are a broad variety of acid forms, salts, esters, and amides that contain a 1,4-carboxy terminated aliphatic structure.

Extrachromosomal, usually CIRCULAR DNA molecules that are self-replicating and transferable from one organism to another. They are found in a variety of bacterial, archaeal, fungal, algal, and plant species. They are used in GENETIC ENGINEERING as CLONING VECTORS.

Enzymes that catalyze the first step leading to the oxidation of succinic acid by the reversible formation of succinyl-CoA from succinate and CoA with the concomitant cleavage of ATP to ADP (EC 6.2.1.5) or GTP to GDP (EC 6.2.1.4) and orthophosphate. Itaconate can act instead of succinate and ITP instead of GTP.EC 6.2.1.-.

Serves as the biological precursor of insect chitin, of muramic acid in bacterial cell walls, and of sialic acids in mammalian glycoproteins.

Genetically identical individuals developed from brother and sister matings which have been carried out for twenty or more generations or by parent x offspring matings carried out with certain restrictions. This also includes animals with a long history of closed colony breeding.

Hydroxycinnamic acid and its derivatives. Act as activators of the indoleacetic acid oxidizing system, thereby producing a decrease in the endogenous level of bound indoleacetic acid in plants.

Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins.

A nucleoside diphosphate sugar which serves as a source of N-acetylgalactosamine for glycoproteins, sulfatides and cerebrosides.

7-carbon saturated monocarboxylic acids.

Systems of enzymes which function sequentially by catalyzing consecutive reactions linked by common metabolic intermediates. They may involve simply a transfer of water molecules or hydrogen atoms and may be associated with large supramolecular structures such as MITOCHONDRIA or RIBOSOMES.

The addition of an organic acid radical into a molecule.

Salts and derivatives of acetoacetic acid.

An increase in the rate of synthesis of an enzyme due to the presence of an inducer which acts to derepress the gene responsible for enzyme synthesis.

The facilitation of biochemical reactions with the aid of naturally occurring catalysts such as ENZYMES.

Derivatives of BUTYRIC ACID that include a double bond between carbon 2 and 3 of the aliphatic structure. Included under this heading are a broad variety of acid forms, salts, esters, and amides that include the aminobutryrate structure.

Conversion of an inactive form of an enzyme to one possessing metabolic activity. It includes 1, activation by ions (activators); 2, activation by cofactors (coenzymes); and 3, conversion of an enzyme precursor (proenzyme or zymogen) to an active enzyme.

A clear, colorless, viscous organic solvent and diluent used in pharmaceutical preparations.

Cells propagated in vitro in special media conducive to their growth. Cultured cells are used to study developmental, morphologic, metabolic, physiologic, and genetic processes, among others.

Separation technique in which the stationary phase consists of ion exchange resins. The resins contain loosely held small ions that easily exchange places with other small ions of like charge present in solutions washed over the resins.

The biosynthesis of RNA carried out on a template of DNA. The biosynthesis of DNA from an RNA template is called REVERSE TRANSCRIPTION.

An essential amino acid that is required for the production of HISTAMINE.

A genus of gram-negative, aerobic, rod-shaped bacteria found in wet soil containing decaying organic material and in water. Cells tend to be pleomorphic if grown on media containing succinate or coccoid if grown in the presence of an alcohol as the sole carbon source. (From Bergey's Manual of Determinative Bacteriology, 9th ed)

Domesticated bovine animals of the genus Bos, usually kept on a farm or ranch and used for the production of meat or dairy products or for heavy labor.

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)

Multicomponent ribonucleoprotein structures found in the CYTOPLASM of all cells, and in MITOCHONDRIA, and PLASTIDS. They function in PROTEIN BIOSYNTHESIS via GENETIC TRANSLATION.

An in situ method for detecting areas of DNA which are nicked during APOPTOSIS. Terminal deoxynucleotidyl transferase is used to add labeled dUTP, in a template-independent manner, to the 3 prime OH ends of either single- or double-stranded DNA. The terminal deoxynucleotidyl transferase nick end labeling, or TUNEL, assay labels apoptosis on a single-cell level, making it more sensitive than agarose gel electrophoresis for analysis of DNA FRAGMENTATION.

The property of objects that determines the direction of heat flow when they are placed in direct thermal contact. The temperature is the energy of microscopic motions (vibrational and translational) of the particles of atoms.

A group of inherited enzyme deficiencies which feature elevations of GALACTOSE in the blood. This condition may be associated with deficiencies of GALACTOKINASE; UDPGLUCOSE-HEXOSE-1-PHOSPHATE URIDYLYLTRANSFERASE; or UDPGLUCOSE 4-EPIMERASE. The classic form is caused by UDPglucose-Hexose-1-Phosphate Uridylyltransferase deficiency, and presents in infancy with FAILURE TO THRIVE; VOMITING; and INTRACRANIAL HYPERTENSION. Affected individuals also may develop MENTAL RETARDATION; JAUNDICE; hepatosplenomegaly; ovarian failure (PRIMARY OVARIAN INSUFFICIENCY); and cataracts. (From Menkes, Textbook of Child Neurology, 5th ed, pp61-3)

Derivatives of propionic acid. Included under this heading are a broad variety of acid forms, salts, esters, and amides that contain the carboxyethane structure.

A carboxylating enzyme that catalyzes the conversion of ATP, acetyl-CoA, and HCO3- to ADP, orthophosphate, and malonyl-CoA. It is a biotinyl-protein that also catalyzes transcarboxylation. The plant enzyme also carboxylates propanoyl-CoA and butanoyl-CoA (From Enzyme Nomenclature, 1992) EC 6.4.1.2.

A genus of green nonsulfur bacteria in the family Chloroflexaceae. They are photosynthetic, thermophilic, filamentous gliding bacteria found in hot springs.

An adenine nucleotide containing three phosphate groups esterified to the sugar moiety. In addition to its crucial roles in metabolism adenosine triphosphate is a neurotransmitter.

The art or process of comparing photometrically the relative intensities of the light in different parts of the spectrum.

A family of anaerobic, coccoid to rod-shaped METHANOBACTERIALES. Cell membranes are composed mainly of polyisoprenoid hydrocarbons ether-linked to glycerol. Its organisms are found in anaerobic habitats throughout nature.

Any of the processes by which cytoplasmic or intercellular factors influence the differential control of gene action in bacteria.

Enzymes that catalyze the synthesis of FATTY ACIDS from acetyl-CoA and malonyl-CoA derivatives.

Proteins found in any species of archaeon.

A coenzyme for a number of oxidative enzymes including NADH DEHYDROGENASE. It is the principal form in which RIBOFLAVIN is found in cells and tissues.

A thiol-containing non-essential amino acid that is oxidized to form CYSTINE.

A subclass of enzymes of the transferase class that catalyze the transfer of an amino group from a donor (generally an amino acid) to an acceptor (generally a 2-keto acid). Most of these enzymes are pyridoxyl phosphate proteins. (Dorland, 28th ed) EC 2.6.1.

A deoxyribonucleotide polymer that is the primary genetic material of all cells. Eukaryotic and prokaryotic organisms normally contain DNA in a double-stranded state, yet several important biological processes transiently involve single-stranded regions. DNA, which consists of a polysugar-phosphate backbone possessing projections of purines (adenine and guanine) and pyrimidines (thymine and cytosine), forms a double helix that is held together by hydrogen bonds between these purines and pyrimidines (adenine to thymine and guanine to cytosine).

One of the mechanisms by which CELL DEATH occurs (compare with NECROSIS and AUTOPHAGOCYTOSIS). Apoptosis is the mechanism responsible for the physiological deletion of cells and appears to be intrinsically programmed. It is characterized by distinctive morphologic changes in the nucleus and cytoplasm, chromatin cleavage at regularly spaced sites, and the endonucleolytic cleavage of genomic DNA; (DNA FRAGMENTATION); at internucleosomal sites. This mode of cell death serves as a balance to mitosis in regulating the size of animal tissues and in mediating pathologic processes associated with tumor growth.

Enzymes that catalyze the transfer of hydroxymethyl or formyl groups. EC 2.1.2.

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 group of oxidoreductases that act on NADH or NADPH. In general, enzymes using NADH or NADPH to reduce a substrate are classified according to the reverse reaction, in which NAD+ or NADP+ is formally regarded as an acceptor. This subclass includes only those enzymes in which some other redox carrier is the acceptor. (Enzyme Nomenclature, 1992, p100) EC 1.6.

Steroids with a hydroxyl group at C-3 and most of the skeleton of cholestane. Additional carbon atoms may be present in the side chain. (IUPAC Steroid Nomenclature, 1987)

A subfamily in the family MURIDAE, comprising the hamsters. Four of the more common genera are Cricetus, CRICETULUS; MESOCRICETUS; and PHODOPUS.

Enzymes that catalyze the breakage of a carbon-oxygen bond leading to unsaturated products via the removal of water. EC 4.2.1.

Ligases that catalyze the joining of adjacent AMINO ACIDS by the formation of carbon-nitrogen bonds between their carboxylic acid groups and amine groups.

A multistage process that includes cloning, physical mapping, subcloning, determination of the DNA SEQUENCE, and information analysis.

Elements of limited time intervals, contributing to particular results or situations.

A chromatographic technique that utilizes the ability of biological molecules to bind to certain ligands specifically and reversibly. It is used in protein biochemistry. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)

Biological catalysts and their cofactors.

Any of various enzymatically catalyzed post-translational modifications of PEPTIDES or PROTEINS in the cell of origin. These modifications include carboxylation; HYDROXYLATION; ACETYLATION; PHOSPHORYLATION; METHYLATION; GLYCOSYLATION; ubiquitination; oxidation; proteolysis; and crosslinking and result in changes in molecular weight and electrophoretic motility.

The restriction of a characteristic behavior, anatomical structure or physical system, such as immune response; metabolic response, or gene or gene variant to the members of one species. It refers to that property which differentiates one species from another but it is also used for phylogenetic levels higher or lower than the species.

A basic science concerned with the composition, structure, and properties of matter; and the reactions that occur between substances and the associated energy exchange.

A functional 4-hydroxysalicylate/hydroxyquinol degradative pathway gene cluster is linked to the initial dibenzo-p-dioxin pathway genes in Sphingomonas sp. strain RW1. (1/146)

The bacterium Sphingomonas sp. strain RW1 is able to use dibenzo-p-dioxin, dibenzofuran, and several hydroxylated derivatives as sole sources of carbon and energy. We have determined and analyzed the nucleic acid sequence of a 9,997-bp HindIII fragment downstream of cistrons dxnA1A2, which encode the dioxygenase component of the initial dioxygenase system of the corresponding catabolic pathways. This fragment contains 10 colinear open reading frames (ORFs), apparently organized in one compact operon. The enzymatic activities of some proteins encoded by these genes were analyzed in the strain RW1 and, after hyperexpression, in Escherichia coli. The first three ORFs of the locus, designated dxnC, ORF2, and fdx3, specify a protein with a low homology to bacterial siderophore receptors, a polypeptide representing no significant homology to known proteins, and a putative ferredoxin, respectively. dxnD encodes a 69-kDa phenol monooxygenase-like protein with activity for the turnover of 4-hydroxysalicylate, and dxnE codes for a 37-kDa protein whose sequence and activity are similar to those of known maleylacetate reductases. The following gene, dxnF, encodes a 33-kDa intradiol dioxygenase which efficiently cleaves hydroxyquinol, yielding maleylacetate, the ketoform of 3-hydroxy-cis,cis-muconate. The heteromeric protein encoded by dxnGH is a 3-oxoadipate succinyl coenzyme A (succinyl-CoA) transferase, whereas dxnI specifies a protein exhibiting marked homology to acetyl-CoA acetyltransferases (thiolases). The last ORF of the sequenced fragment codes for a putative transposase. DxnD, DxnF, DxnE, DxnGH, and DxnI (the activities of most of them have also been detected in strain RW1) thus form a complete 4-hydroxysalicylate/hydroxyquinol degradative pathway. A route for the mineralization of the growth substrates 3-hydroxydibenzofuran and 2-hydroxydibenzo-p-dioxin in Sphingomonas sp. strain RW1 thus suggests itself. (+info)

Oxygen exchange between acetate and the catalytic glutamate residue in glutaconate CoA-transferase from Acidaminococcus fermentans. Implications for the mechanism of CoA-ester hydrolysis. (2/146)

The exchange of oxygen atoms between acetate, glutaryl-CoA, and the catalytic glutamate residue in glutaconate CoA-transferase from Acidaminococcus fermentans was analyzed using [(18)O(2)]acetate together with matrix-assisted laser desorption/ionization time of flight mass spectrometry of an appropriate undecapeptide. The exchange reaction was shown to be site-specific, reversible, and required both glutaryl-CoA and [(18)O(2)]acetate. The observed exchange is in agreement with the formation of a mixed anhydride intermediate between the enzyme and acetate. In contrast, with a mutant enzyme, which was converted to a thiol ester hydrolyase by replacement of the catalytic glutamate residue by aspartate, no (18)O uptake from H(2)(18)O into the carboxylate was detectable. This result is in accord with a mechanism in which the carboxylate of aspartate acts as a general base in activating a water molecule for hydrolysis of the thiol ester intermediate. This mechanism is further supported by the finding of a significant hydrolyase activity of the wild-type enzyme using acetyl-CoA as substrate, whereas glutaryl-CoA is not hydrolyzed. The small acetate molecule in the substrate binding pocket may activate a water molecule for hydrolysis of the nearby enzyme-CoA thiol ester. (+info)

Regulation and adaptation of glucose metabolism of the parasitic protist Leishmania donovani at the enzyme and mRNA levels. (3/146)

Adaptation of the glucose metabolism of Leishmania donovani promastigotes (insect stage) was investigated by simultaneously measuring metabolic rates, enzyme activities, message levels, and cellular parameters under various conditions. Chemostats were used to adapt cells to different growth rates with growth rate-limiting or excess glucose concentrations. L. donovani catabolized glucose to CO(2), succinate, acetate, and pyruvate in ratios that depended on growth rate and glucose availability. Rates of glucose consumption were a linear function of growth rate and were twice as high in excess glucose-grown cells as in glucose-limited organisms. The major end product was CO(2), but organic end products were also formed in ratios that varied strongly with growth conditions. The specific activities of the 14 metabolic enzymes measured varied by factors of 3 to 17. Two groups of enzymes adapted specific activities in parallel, but there was no correlation between the groups. The activities of only one group correlated with specific rates of glucose metabolism. Total RNA content per cellular protein varied by a factor of 6 and showed a linear relationship with the rate of glucose consumption. There was no correlation between steady-state message levels and activities of the corresponding enzymes, suggesting regulation at the posttranscriptional level. A comparison of the adaptation of energy metabolism in L. donovani and other species suggests that the energy metabolism of L. donovani is inefficient but is well suited to the environmental challenges that it encounters during residence in the sandfly, its insect vector. (+info)

Protection of mice against brucellosis by vaccination with Brucella melitensis WR201(16MDeltapurEK). (4/146)

Human brucellosis can be acquired from infected animal tissues by ingestion, inhalation, or contamination of the conjunctiva or traumatized skin by infected animal products. A vaccine to protect humans from occupational exposure or from zoonotic infection in areas where the disease is endemic would reduce an important cause of morbidity worldwide. Vaccines currently used in animals are unsuitable for human use. We tested a live, attenuated, purine-auxotrophic mutant strain of Brucella melitensis, WR201, for its ability to elicit cellular and humoral immune responses and to protect mice against intranasal challenge with B. melitensis 16M. Mice inoculated intraperitoneally with WR201 made serum antibody to lipopolysaccharide and non-O-polysaccharide antigens. Splenocytes from immunized animals released interleukin-2 (IL-2), gamma interferon, and IL-10 when cultured with Brucella antigens. Immunization led to protection from disseminated infection but had only a slight effect on clearance of the challenge inoculum from the lungs. These studies suggest that WR201 should be further investigated as a vaccine to prevent human brucellosis. (+info)

Isolation and characterization of a haploid germ cell-specific novel complementary deoxyribonucleic acid; testis-specific homologue of succinyl CoA:3-Oxo acid CoA transferase. (5/146)

We have isolated a cDNA clone encoding a mouse haploid germ cell-specific protein from a subtracted cDNA library. Sequence analysis of the cDNA revealed high homology with pig and human heart succinyl CoA:3-oxo acid CoA transferase (EC 2.8.3.5), which is a key enzyme for energy metabolism of ketone bodies. The deduced protein consists of 520 amino acid residues, including glutamate 344, known to be the catalytic residue in the active site of pig heart CoA transferase and the expected mitochondrial targeting sequence enriched with Arg, Leu, and Ser in the N-terminal region. Thus, we termed this gene scot-t (testis-specific succinyl CoA:3-oxo acid CoA transferase). Northern blot analysis, in situ hybridization, and Western blot analysis demonstrated a unique expression pattern of the mRNA with rapid translation exclusively in late spermatids. The scot-t protein was detected first in elongated spermatids at step 8 or 9 as faint signals and gradually accumulated during spermiogenesis. It was also detected in the midpiece of spermatozoa by immunohistochemistry. The results suggest that the scot-t protein plays important roles in the energy metabolism of spermatozoa. (+info)

Nitration of succinyl-CoA:3-oxoacid CoA-transferase in rats after endotoxin administration. (6/146)

The tyrosine nitration of proteins has been observed in diverse inflammatory conditions and has been linked to the presence of reactive nitrogen species. From many in vitro experiments, it is apparent that tyrosine nitration may alter the function of proteins. A limited number of experiments under in vivo conditions also demonstrate that protein nitration is associated with altered cellular processes. To understand the association of protein nitration with the pathogenic mechanism of the disease, it is essential to identify specific protein targets of nitration with in vivo or intact tissue models. Using anti-nitrotyrosine antibodies, we demonstrated the accumulation of nitrotyrosine in a 52-kDa protein in rat kidney after lipopolysaccharide treatment. The 52-kDa protein was purified and identified with partial sequence as succinyl-CoA:3-oxoacid CoA-transferase (SCOT; EC ). Western blot analysis revealed that the nitration of this mitochondrial enzyme increased in the kidneys and hearts of lipopolysaccharide-treated rats, whereas its catalytic activity decreased. These data suggest that tyrosine nitration may be a mechanism for the inhibition of SCOT activity in inflammatory conditions. SCOT is a key enzyme for ketone body utilization. Thus, tyrosine nitration of the enzyme with sepsis or inflammation may explain the altered metabolism of ketone bodies present in these disorders. (+info)

Succinyl-CoA:(R)-benzylsuccinate CoA-transferase: an enzyme of the anaerobic toluene catabolic pathway in denitrifying bacteria. (7/146)

Anaerobic microbial toluene catabolism is initiated by addition of fumarate to the methyl group of toluene, yielding (R)-benzylsuccinate as first intermediate, which is further metabolized via beta-oxidation to benzoyl-coenzyme A (CoA) and succinyl-CoA. A specific succinyl-CoA:(R)-benzylsuccinate CoA-transferase activating (R)-benzylsuccinate to the CoA-thioester was purified and characterized from Thauera aromatica. The enzyme is fully reversible and forms exclusively the 2-(R)-benzylsuccinyl-CoA isomer. Only some close chemical analogs of the substrates are accepted by the enzyme: succinate was partially replaced by maleate or methylsuccinate, and (R)-benzylsuccinate was replaced by methylsuccinate, benzylmalonate, or phenylsuccinate. In contrast to all other known CoA-transferases, the enzyme consists of two subunits of similar amino acid sequences and similar sizes (44 and 45 kDa) in an alpha(2)beta(2) conformation. Identity of the subunits with the products of the previously identified toluene-induced bbsEF genes was confirmed by determination of the exact masses via electrospray-mass spectrometry. The deduced amino acid sequences resemble those of only two other characterized CoA-transferases, oxalyl-CoA:formate CoA-transferase and (E)-cinnamoyl-CoA:(R)-phenyllactate CoA-transferase, which represent a new family of CoA-transferases. As suggested by kinetic analysis, the reaction mechanism of enzymes of this family apparently involves formation of a ternary complex between the enzyme and the two substrates. (+info)

Diabetes-associated nitration of tyrosine and inactivation of succinyl-CoA:3-oxoacid CoA-transferase. (8/146)

High levels of reactive species of nitrogen and oxygen in diabetes may cause modifications of proteins. Recently, an increase in protein tyrosine nitration was found in several diabetic tissues. To understand whether protein tyrosine nitration is the cause or the result of the associated diabetic complications, it is essential to identify specific proteins vulnerable to nitration with in vivo models of diabetes. In the present study, we have demonstrated that succinyl-CoA:3-oxoacid CoA-transferase (SCOT; EC 2.8.3.5) is susceptible to tyrosine nitration in hearts from streptozotocin-treated rats. After 4 and 8 wk of streptozotocin administration and diabetes progression, SCOT from rat hearts had a 24% and 39% decrease in catalytic activity, respectively. The decrease in SCOT catalytic activity is accompanied by an accumulation of nitrotyrosine in SCOT protein. SCOT is a mitochondrial matrix protein responsible for ketone body utilization. Ketone bodies provide an alternative source of energy during periods of glucose deficiency. Because diabetes results in profound derangements in myocardial substrate utilization, we suggest that SCOT tyrosine nitration is a contributing factor to this impairment in the diabetic heart. (+info)

There are two main types of galactosemia:

1. Classical galactosemia: This is the most severe form of the disorder, and it is characterized by a complete lack of the enzyme galactose-1-phosphate uridylyltransferase (GALT). Without GALT, galactose builds up in the blood and tissues, leading to serious health problems.
2. Dialectical galactosemia: This form of the disorder is less severe than classical galactosemia, and it is characterized by a partial deficiency of GALT. People with dialectical galactosemia may experience some symptoms, but they are typically milder than those experienced by people with classical galactosemia.

Symptoms of galactosemia can include:

* Diarrhea
* Vomiting
* Jaundice (yellowing of the skin and eyes)
* Fatigue
* Poor feeding in infants
* Developmental delays

If left untreated, galactosemia can lead to a range of complications, including:

* Liver disease
* Kidney disease
* Increased risk of infections
* Delayed growth and development

The diagnosis of galactosemia is typically made through a combination of physical examination, medical history, and laboratory tests. Treatment for the disorder typically involves a strict diet that limits or eliminates galactose-containing foods, such as milk and other dairy products. In some cases, medication may also be prescribed to help manage symptoms.

Overall, early diagnosis and treatment of galactosemia are important for preventing or minimizing the risk of complications associated with this condition.

Term: Lesch-Nyhan Syndrome

Definition: A rare X-linked recessive genetic disorder caused by mutations in the HPRT1 gene, resulting in an impaired ability to metabolize uric acid and leading to symptoms such as gout, kidney stones, and other complications.

Etymology: Named after the physicians who first described the condition, Lesch and Nyhan.

Incidence: Approximately 1 in 165,000 male births.

Prevalence: Estimated to affect approximately 1 in 23,000 males worldwide.

Causes: Mutations in the HPRT1 gene, which codes for the enzyme hypoxanthine-guanine phosphoribosyltransferase (HPRT). This enzyme is involved in the metabolism of uric acid.

Symptoms: Gout attacks, kidney stones, joint pain and swelling, urate nephropathy (kidney damage), and other complications.

Diagnosis: Diagnosed through a combination of clinical evaluation, laboratory tests such as blood and urine analysis, and genetic testing to identify HPRT1 gene mutations.

Treatment: Medications to reduce uric acid levels, such as allopurinol or rasburicase, and management of symptoms such as pain and inflammation with nonsteroidal anti-inflammatory drugs (NSAIDs) or colchicine.

Prognosis: The condition is usually diagnosed in childhood, and patients often have a normal life expectancy if properly managed. However, untreated or poorly managed hyperuricemia can lead to complications such as kidney damage and cardiovascular disease.

Inheritance pattern: Autosomal recessive inheritance pattern, meaning that the individual must inherit two copies of the mutated HPRT1 gene (one from each parent) in order to develop the condition.

Other names: Hyperuricemia, gout, Lesch-Nyhan syndrome.

The two main types of lymphoid leukemia are:

1. Acute Lymphoblastic Leukemia (ALL): This type of leukemia is most commonly seen in children, but it can also occur in adults. It is characterized by a rapid increase in the number of immature white blood cells in the blood and bone marrow.
2. Chronic Lymphocytic Leukemia (CLL): This type of leukemia usually affects older adults and is characterized by the gradual buildup of abnormal white blood cells in the blood, bone marrow, and lymph nodes.

Symptoms of lymphoid leukemia include fatigue, fever, night sweats, weight loss, and swollen lymph nodes. Treatment options for lymphoid leukemia can vary depending on the type of cancer and the severity of symptoms, but may include chemotherapy, radiation therapy, or bone marrow transplantation.

There are several methods for diagnosing myringosclerosis, including:

1. Otoscopy: an examination of the outer ear and eardrum using a specialized instrument called an otoscope.
2. Tympanometry: a test that measures the movement of the eardrum and the reflexes of the middle ear muscles.
3. Acoustic reflectometry: a test that uses sound waves to measure the stiffness of the eardrum.
4. Auditory brainstem response (ABR) testing: a test that measures the electrical activity of the hearing nerve in response to sound.

There is no cure for myringosclerosis, but there are several treatment options available, including:

1. Hearing aids: devices that amplify sound and can help improve hearing.
2. Cochlear implants: devices that bypass the damaged part of the ear and directly stimulate the auditory nerve.
3. Surgery: in some cases, surgery may be necessary to remove the affected portion of the eardrum.
4. Medications: certain medications, such as corticosteroids, may be prescribed to help reduce inflammation and improve hearing.

It is important to seek medical attention if you experience any symptoms of myringosclerosis, as early diagnosis and treatment can help improve outcomes.

PKAN typically presents in children during the first few years of life, and is characterized by progressive loss of motor skills, cognitive decline, and vision loss. Affected individuals may also experience seizures, difficulty with speech and communication, and changes in behavior. The disorder is often diagnosed based on a combination of clinical features, genetic testing, and imaging studies such as magnetic resonance imaging (MRI) or positron emission tomography (PET).

The underlying pathology of PKAN involves the accumulation of a toxic protein called aggregated pantothenate kinase, which disrupts normal cellular function and leads to progressive degeneration of brain cells. There is currently no cure for PKAN, and treatment is focused on managing symptoms and slowing disease progression. This may include medications to control seizures and muscle spasticity, physical therapy to maintain mobility and strength, and supportive care to address cognitive and behavioral changes.

PKAN is a rare disorder, and the prevalence is not well-defined. However, it is estimated to affect approximately 1 in 200,000 individuals worldwide. The progression of PKAN can be variable, with some individuals experiencing a rapid decline in cognitive and motor functions, while others may have a more gradual course.

In summary, pantothenate kinase-associated neurodegeneration (PKAN) is a rare genetic disorder that affects the brain and spinal cord, causing progressive loss of motor skills, cognitive decline, and vision loss. There is currently no cure for PKAN, and treatment is focused on managing symptoms and slowing disease progression.

Examples of experimental liver neoplasms include:

1. Hepatocellular carcinoma (HCC): This is the most common type of primary liver cancer and can be induced experimentally by injecting carcinogens such as diethylnitrosamine (DEN) or dimethylbenz(a)anthracene (DMBA) into the liver tissue of animals.
2. Cholangiocarcinoma: This type of cancer originates in the bile ducts within the liver and can be induced experimentally by injecting chemical carcinogens such as DEN or DMBA into the bile ducts of animals.
3. Hepatoblastoma: This is a rare type of liver cancer that primarily affects children and can be induced experimentally by administering chemotherapy drugs to newborn mice or rats.
4. Metastatic tumors: These are tumors that originate in other parts of the body and spread to the liver through the bloodstream or lymphatic system. Experimental models of metastatic tumors can be studied by injecting cancer cells into the liver tissue of animals.

The study of experimental liver neoplasms is important for understanding the underlying mechanisms of liver cancer development and progression, as well as identifying potential therapeutic targets for the treatment of this disease. Animal models can be used to test the efficacy of new drugs or therapies before they are tested in humans, which can help to accelerate the development of new treatments for liver cancer.

1) They share similarities with humans: Many animal species share similar biological and physiological characteristics with humans, making them useful for studying human diseases. For example, mice and rats are often used to study diseases such as diabetes, heart disease, and cancer because they have similar metabolic and cardiovascular systems to humans.

2) They can be genetically manipulated: Animal disease models can be genetically engineered to develop specific diseases or to model human genetic disorders. This allows researchers to study the progression of the disease and test potential treatments in a controlled environment.

3) They can be used to test drugs and therapies: Before new drugs or therapies are tested in humans, they are often first tested in animal models of disease. This allows researchers to assess the safety and efficacy of the treatment before moving on to human clinical trials.

4) They can provide insights into disease mechanisms: Studying disease models in animals can provide valuable insights into the underlying mechanisms of a particular disease. This information can then be used to develop new treatments or improve existing ones.

5) Reduces the need for human testing: Using animal disease models reduces the need for human testing, which can be time-consuming, expensive, and ethically challenging. However, it is important to note that animal models are not perfect substitutes for human subjects, and results obtained from animal studies may not always translate to humans.

6) They can be used to study infectious diseases: Animal disease models can be used to study infectious diseases such as HIV, TB, and malaria. These models allow researchers to understand how the disease is transmitted, how it progresses, and how it responds to treatment.

7) They can be used to study complex diseases: Animal disease models can be used to study complex diseases such as cancer, diabetes, and heart disease. These models allow researchers to understand the underlying mechanisms of the disease and test potential treatments.

8) They are cost-effective: Animal disease models are often less expensive than human clinical trials, making them a cost-effective way to conduct research.

9) They can be used to study drug delivery: Animal disease models can be used to study drug delivery and pharmacokinetics, which is important for developing new drugs and drug delivery systems.

10) They can be used to study aging: Animal disease models can be used to study the aging process and age-related diseases such as Alzheimer's and Parkinson's. This allows researchers to understand how aging contributes to disease and develop potential treatments.

Examples of inborn errors of metabolism include:

1. Phenylketonuria (PKU): A disorder that affects the body's ability to break down the amino acid phenylalanine, leading to a buildup of this substance in the blood and brain.
2. Hypothyroidism: A condition in which the thyroid gland does not produce enough thyroid hormones, leading to developmental delays, intellectual disability, and other health problems.
3. Maple syrup urine disease (MSUD): A disorder that affects the body's ability to break down certain amino acids, leading to a buildup of these substances in the blood and urine.
4. Glycogen storage diseases: A group of disorders that affect the body's ability to store and use glycogen, a form of carbohydrate energy.
5. Mucopolysaccharidoses (MPS): A group of disorders that affect the body's ability to produce and break down certain sugars, leading to a buildup of these substances in the body.
6. Citrullinemia: A disorder that affects the body's ability to break down the amino acid citrulline, leading to a buildup of this substance in the blood and urine.
7. Homocystinuria: A disorder that affects the body's ability to break down certain amino acids, leading to a buildup of these substances in the blood and urine.
8. Tyrosinemia: A disorder that affects the body's ability to break down the amino acid tyrosine, leading to a buildup of this substance in the blood and liver.

Inborn errors of metabolism can be diagnosed through a combination of physical examination, medical history, and laboratory tests such as blood and urine tests. Treatment for these disorders varies depending on the specific condition and may include dietary changes, medication, and other therapies. Early detection and treatment can help manage symptoms and prevent complications.

Diagnosis of monieziasis typically involves a combination of physical examination, medical history, and laboratory tests such as fecal examination or endoscopy. Treatment typically involves the use of anthelmintic medications to kill the parasites, and supportive care to manage symptoms such as pain and diarrhea. In severe cases, hospitalization may be necessary to monitor and treat complications.

Prevention of monieziasis primarily involves good hygiene practices such as washing hands before eating or preparing food, avoiding close contact with individuals who have the infection, and avoiding consumption of undercooked or raw meat. In areas where the parasite is common, regular deworming programs can also help to reduce the risk of infection.

The prognosis for monieziasis is generally good if treatment is prompt and effective. However, complications such as intestinal obstruction, perforation, or abscesses can occur if left untreated, and can be life-threatening. It is important to seek medical attention if symptoms persist or worsen over time.

Overall, monieziasis is a rare but potentially serious condition that requires prompt diagnosis and treatment to prevent complications and ensure a good outcome.

There are several types of inborn errors of amino acid metabolism, including:

1. Phenylketonuria (PKU): This is the most common inborn error of amino acid metabolism and is caused by a deficiency of the enzyme phenylalanine hydroxylase. This enzyme is needed to break down the amino acid phenylalanine, which is found in many protein-containing foods. If phenylalanine is not properly broken down, it can build up in the blood and brain and cause serious health problems.
2. Maple syrup urine disease (MSUD): This is a rare genetic disorder that affects the breakdown of the amino acids leucine, isoleucine, and valine. These amino acids are important for growth and development, but if they are not properly broken down, they can build up in the blood and cause serious health problems.
3. Homocystinuria: This is a rare genetic disorder that affects the breakdown of the amino acid methionine. Methionine is important for the body's production of proteins and other compounds, but if it is not properly broken down, it can build up in the blood and cause serious health problems.
4. Arginase deficiency: This is a rare genetic disorder that affects the breakdown of the amino acid arginine. Arginine is important for the body's production of nitric oxide, a compound that helps to relax blood vessels and improve blood flow.
5. Citrullinemia: This is a rare genetic disorder that affects the breakdown of the amino acid citrulline. Citrulline is important for the body's production of proteins and other compounds, but if it is not properly broken down, it can build up in the blood and cause serious health problems.
6. Tyrosinemia: This is a rare genetic disorder that affects the breakdown of the amino acid tyrosine. Tyrosine is important for the body's production of proteins and other compounds, but if it is not properly broken down, it can build up in the blood and cause serious health problems.
7. Maple syrup urine disease (MSUD): This is a rare genetic disorder that affects the breakdown of the amino acids leucine, isoleucine, and valine. These amino acids are important for growth and development, but if they are not properly broken down, they can build up in the blood and cause serious health problems.
8. PKU (phenylketonuria): This is a rare genetic disorder that affects the breakdown of the amino acid phenylalanine. Phenylalanine is important for the body's production of proteins and other compounds, but if it is not properly broken down, it can build up in the blood and cause serious health problems.
9. Methionine adenosyltransferase (MAT) deficiency: This is a rare genetic disorder that affects the breakdown of the amino acid methionine. Methionine is important for the body's production of proteins and other compounds, but if it is not properly broken down, it can build up in the blood and cause serious health problems.
10. Homocystinuria: This is a rare genetic disorder that affects the breakdown of the amino acid homocysteine. Homocysteine is important for the body's production of proteins and other compounds, but if it is not properly broken down, it can build up in the blood and cause serious health problems.

It is important to note that these disorders are rare and affect a small percentage of the population. However, they can be serious and potentially life-threatening, so it is important to be aware of them and seek medical attention if symptoms persist or worsen over time.

A vitamin B6 deficiency happens when the body does not get enough of this essential nutrient. Vitamin B6 is needed for many bodily functions, such as making new blood cells, keeping the nervous system healthy, and helping to convert food into energy.

The symptoms of a vitamin B6 deficiency can range from mild to severe and may include:

1. Fatigue or weakness: A lack of vitamin B6 can cause tiredness, weakness, and a general feeling of being unwell.
2. Irritability or depression: Vitamin B6 plays a role in the production of neurotransmitters, such as serotonin and dopamine, which are important for mood regulation. A deficiency can lead to feelings of irritability, anxiety, and depression.
3. Nausea and vomiting: Vitamin B6 helps with the absorption of nutrients from food, so a deficiency can cause nausea and vomiting.
4. Skin problems: Vitamin B6 is important for the health of the skin, and a deficiency can lead to conditions such as acne, eczema, and dermatitis.
5. Weight loss: A vitamin B6 deficiency can make it harder to gain weight or maintain weight loss.

Causes of Vitamin B6 Deficiency:

1. Poor diet: A diet that is low in vitamin B6 can lead to a deficiency. Foods rich in vitamin B6 include meat, fish, poultry, whole grains, and leafy green vegetables.
2. Malabsorption: Certain medical conditions, such as celiac disease or inflammatory bowel disease, can make it harder for the body to absorb vitamin B6 from food.
3. Pregnancy and breastfeeding: Women who are pregnant or breastfeeding have a higher need for vitamin B6 and may be more likely to develop a deficiency if they do not consume enough of this nutrient.
4. Alcoholism: Heavy alcohol consumption can interfere with the absorption of vitamin B6, leading to a deficiency.
5. Certain medications: Some medications, such as antidepressants and anti-inflammatory drugs, can interfere with the absorption of vitamin B6.

Signs and Symptoms of Vitamin B6 Deficiency:

1. Depression or anxiety
2. Fatigue or weakness
3. Irritability or mood swings
4. Skin problems, such as acne or eczema
5. Nausea and vomiting
6. Weight loss or difficulty gaining weight
7. Difficulty walking or maintaining balance
8. Headaches or migraines
9. Muscle weakness or cramps
10. Seizures or convulsions (in severe cases)

Treatment of Vitamin B6 Deficiency:

1. Dietary changes: Increasing the intake of vitamin B6-rich foods, such as lean meats, whole grains, and vegetables, can help treat a deficiency.
2. Supplements: Taking a vitamin B6 supplement can help treat a deficiency. The recommended daily dose is 1.3-2.0 mg per day for adults.
3. Addressing underlying causes: If the deficiency is caused by an underlying medical condition, such as celiac disease or alcoholism, treating the condition can help resolve the deficiency.
4. Vitamin B complex supplements: Taking a vitamin B complex supplement that contains all eight B vitamins can help ensure that the body is getting enough of this essential nutrient.

In conclusion, vitamin B6 is an essential nutrient that plays a crucial role in many bodily functions. Deficiency in this vitamin can lead to a range of health problems, from mild discomforts like fatigue and nausea to more severe conditions like seizures and convulsions. Treatment of a deficiency typically involves dietary changes, supplements, and addressing any underlying medical conditions. It is important to seek medical advice if symptoms persist or worsen over time.

There are several types of hypercholesterolemia, including:

1. Familial hypercholesterolemia: This is an inherited condition that causes high levels of low-density lipoprotein (LDL) cholesterol, also known as "bad" cholesterol, in the blood.
2. Non-familial hypercholesterolemia: This type of hypercholesterolemia is not inherited and can be caused by a variety of factors, such as a high-fat diet, lack of exercise, obesity, and certain medical conditions, such as hypothyroidism or polycystic ovary syndrome (PCOS).
3. Mixed hypercholesterolemia: This type of hypercholesterolemia is characterized by high levels of both LDL and high-density lipoprotein (HDL) cholesterol in the blood.

The diagnosis of hypercholesterolemia is typically made based on a physical examination, medical history, and laboratory tests, such as a lipid profile, which measures the levels of different types of cholesterol and triglycerides in the blood. Treatment for hypercholesterolemia usually involves lifestyle changes, such as a healthy diet and regular exercise, and may also include medication, such as statins, to lower cholesterol levels.

Crigler-Najjar syndrome is a rare genetic disorder that affects the liver and causes it to be unable to break down bilirubin, a yellow pigment found in the blood. This results in a buildup of bilirubin in the blood and can lead to jaundice, which is characterized by a yellowish tint to the skin and whites of the eyes.

There are two types of Crigler-Najjar syndrome: type 1 and type 2. Type 1 is caused by a deficiency of the enzyme glucuronyltransferase, which is necessary for the breakdown of bilirubin. Type 2 is caused by a deficiency of the enzyme UDP-glucuronosyltransferase. Both types can be inherited from one's parents or can be acquired through mutations that occur spontaneously.

Symptoms of Crigler-Najjar syndrome include jaundice, yellowing of the skin and whites of the eyes, dark urine, itching all over the body, and a higher risk of liver disease. Treatment for Crigler-Najjar syndrome typically involves managing the symptoms and preventing complications. This may include phototherapy to help break down bilirubin, medications to reduce jaundice, and careful monitoring of the liver function. In severe cases, a liver transplant may be necessary.

Overall, Crigler-Najjar syndrome is a rare and potentially serious genetic disorder that affects the liver's ability to break down bilirubin. With proper management and care, individuals with this condition can lead relatively normal lives.

Body weight is an important health indicator, as it can affect an individual's risk for certain medical conditions, such as obesity, diabetes, and cardiovascular disease. Maintaining a healthy body weight is essential for overall health and well-being, and there are many ways to do so, including a balanced diet, regular exercise, and other lifestyle changes.

There are several ways to measure body weight, including:

1. Scale: This is the most common method of measuring body weight, and it involves standing on a scale that displays the individual's weight in kg or lb.
2. Body fat calipers: These are used to measure body fat percentage by pinching the skin at specific points on the body.
3. Skinfold measurements: This method involves measuring the thickness of the skin folds at specific points on the body to estimate body fat percentage.
4. Bioelectrical impedance analysis (BIA): This is a non-invasive method that uses electrical impulses to measure body fat percentage.
5. Dual-energy X-ray absorptiometry (DXA): This is a more accurate method of measuring body composition, including bone density and body fat percentage.

It's important to note that body weight can fluctuate throughout the day due to factors such as water retention, so it's best to measure body weight at the same time each day for the most accurate results. Additionally, it's important to use a reliable scale or measuring tool to ensure accurate measurements.

Mitochondrial encephalomyopathies can be classified into several types based on the specific symptoms and the location of the mutations in the mitochondrial DNA. Some of the most common forms of these disorders include:

1. MELAS syndrome (mitochondrial myopathy, encephalopathy, lactic acidosis, and stroke-like episodes): This is a rare condition that affects the brain, muscles, and other organs. It is characterized by recurrent stroke-like episodes, seizures, and muscle weakness.
2. Kearns-Sayre syndrome: This is a rare genetic disorder that affects the nervous system and the muscles. It is characterized by progressive weakness and paralysis of the muscles, as well as vision loss and cognitive impairment.
3. Chronic progressive external ophthalmoplegia (CPEO): This is a rare disorder that affects the muscles of the eyes and the extraocular system. It is characterized by progressive weakness of the eye muscles, which can lead to droopy eyelids, double vision, and other vision problems.
4. Mitochondrial DNA depletion syndrome: This is a group of disorders that are caused by a decrease in the amount of mitochondrial DNA. These disorders can affect various parts of the body, including the brain, muscles, and other organs. They can cause a wide range of symptoms, including muscle weakness, seizures, and vision loss.
5. Myoclonic dystonia: This is a rare genetic disorder that affects the muscles and the nervous system. It is characterized by muscle stiffness, spasms, and myoclonus (involuntary jerky movements).
6. Neuronal ceroid lipofuscinoses (NCL): These are a group of rare genetic disorders that affect the brain and the nervous system. They can cause progressive loss of cognitive and motor functions, as well as vision loss and seizures.
7. Spinocerebellar ataxia: This is a group of rare genetic disorders that affect the cerebellum and the spinal cord. They can cause progressive weakness, coordination problems, and other movement disorders.
8. Friedreich's ataxia: This is a rare genetic disorder that affects the nervous system and the muscles. It is characterized by progressive loss of coordination and balance, as well as muscle weakness and wasting.
9. Charcot-Marie-Tooth disease: This is a group of rare genetic disorders that affect the peripheral nerves. They can cause muscle weakness, numbness or tingling in the hands and feet, and other problems with movement and sensation.
10. Progressive supranuclear palsy: This is a rare genetic disorder that affects the brain and the nervous system. It is characterized by progressive loss of movement control, as well as dementia and behavioral changes.

It is important to note that this list is not exhaustive and there may be other rare movement disorders that are not included here. If you suspect that you or a loved one may have a rare movement disorder, it is important to consult with a healthcare professional for proper diagnosis and treatment.

Mitochondrial diseases can affect anyone, regardless of age or gender, and they can be caused by mutations in either the mitochondrial DNA (mtDNA) or the nuclear DNA (nDNA). These mutations can be inherited from one's parents or acquired during embryonic development.

Some of the most common symptoms of mitochondrial diseases include:

1. Muscle weakness and wasting
2. Seizures
3. Cognitive impairment
4. Vision loss
5. Hearing loss
6. Heart problems
7. Neurological disorders
8. Gastrointestinal issues
9. Liver and kidney dysfunction

Some examples of mitochondrial diseases include:

1. MELAS syndrome (Mitochondrial Myopathy, Encephalopathy, Lactic Acidosis, and Stroke-like episodes)
2. Kearns-Sayre syndrome (a rare progressive disorder that affects the nervous system and other organs)
3. Chronic progressive external ophthalmoplegia (CPEO), which is characterized by weakness of the extraocular muscles and vision loss
4. Mitochondrial DNA depletion syndrome, which can cause a wide range of symptoms including seizures, developmental delays, and muscle weakness.
5. Mitochondrial myopathy, encephalomyopathy, lactic acidosis, and stroke-like episodes (MELAS)
6. Leigh syndrome, which is a rare genetic disorder that affects the brain and spinal cord.
7. LHON (Leber's Hereditary Optic Neuropathy), which is a rare form of vision loss that can lead to blindness in one or both eyes.
8. Mitochondrial DNA mutation, which can cause a wide range of symptoms including seizures, developmental delays, and muscle weakness.
9. Mitochondrial myopathy, encephalomyopathy, lactic acidosis, and stroke-like episodes (MELAS)
10. Kearns-Sayre syndrome, which is a rare progressive disorder that affects the nervous system and other organs.

It's important to note that this is not an exhaustive list and there are many more mitochondrial diseases and disorders that can affect individuals. Additionally, while these diseases are rare, they can have a significant impact on the quality of life of those affected and their families.

Causes and risk factors:

1. Poor diet: A diet that is deficient in riboflavin can lead to a deficiency. Common culprits include a lack of dairy products, eggs, and leafy green vegetables.
2. Malabsorption: Certain medical conditions, such as celiac disease, Crohn's disease, and pancreatic insufficiency, can lead to malabsorption of riboflavin and other nutrients.
3. Alcoholism: Alcohol can interfere with the absorption of riboflavin and other B vitamins.
4. Pregnancy and lactation: Pregnant and breastfeeding women have a higher demand for riboflavin, and may be at risk for deficiency if their diet does not provide enough.
5. Genetic disorders: Certain genetic disorders, such as fibroblastosis, can lead to riboflavin deficiency.

Symptoms of riboflavin deficiency can include:

1. Cracks in the corners of the mouth (cheilosis)
2. Redness and swelling of the tongue
3. Dry, itchy skin
4. Fatigue
5. Headaches
6. Dizziness
7. Muscle weakness
8. Seizures (in severe cases)

Diagnosis of riboflavin deficiency is typically made based on a combination of symptoms, physical examination findings, and laboratory tests. Treatment involves supplementation with riboflavin, which can help to resolve symptoms and prevent complications.

In summary, riboflavin deficiency is a condition where the body does not have enough riboflavin, leading to a range of symptoms and potential health complications. It is important for individuals at risk for deficiency to be aware of the signs and symptoms, and to seek medical attention if they suspect they may have a deficiency.

1. Muscular dystrophy: A group of genetic disorders characterized by progressive muscle weakness and degeneration.
2. Myopathy: A condition where the muscles become damaged or diseased, leading to muscle weakness and wasting.
3. Fibromyalgia: A chronic condition characterized by widespread pain, fatigue, and muscle stiffness.
4. Rhabdomyolysis: A condition where the muscle tissue is damaged, leading to the release of myoglobin into the bloodstream and potentially causing kidney damage.
5. Polymyositis/dermatomyositis: Inflammatory conditions that affect the muscles and skin.
6. Muscle strain: A common injury caused by overstretching or tearing of muscle fibers.
7. Cervical dystonia: A movement disorder characterized by involuntary contractions of the neck muscles.
8. Myasthenia gravis: An autoimmune disorder that affects the nerve-muscle connection, leading to muscle weakness and fatigue.
9. Oculopharyngeal myopathy: A condition characterized by weakness of the muscles used for swallowing and eye movements.
10. Inclusion body myositis: An inflammatory condition that affects the muscles, leading to progressive muscle weakness and wasting.

These are just a few examples of the many different types of muscular diseases that can affect individuals. Each condition has its unique set of symptoms, causes, and treatment options. It's important for individuals experiencing muscle weakness or wasting to seek medical attention to receive an accurate diagnosis and appropriate care.

Liver neoplasms, also known as liver tumors or hepatic tumors, are abnormal growths of tissue in the liver. These growths can be benign (non-cancerous) or malignant (cancerous). Malignant liver tumors can be primary, meaning they originate in the liver, or metastatic, meaning they spread to the liver from another part of the body.

There are several types of liver neoplasms, including:

1. Hepatocellular carcinoma (HCC): This is the most common type of primary liver cancer and arises from the main cells of the liver (hepatocytes). HCC is often associated with cirrhosis and can be caused by viral hepatitis or alcohol abuse.
2. Cholangiocarcinoma: This type of cancer arises from the cells lining the bile ducts within the liver (cholangiocytes). Cholangiocarcinoma is rare and often diagnosed at an advanced stage.
3. Hemangiosarcoma: This is a rare type of cancer that originates in the blood vessels of the liver. It is most commonly seen in dogs but can also occur in humans.
4. Fibromas: These are benign tumors that arise from the connective tissue of the liver (fibrocytes). Fibromas are usually small and do not spread to other parts of the body.
5. Adenomas: These are benign tumors that arise from the glandular cells of the liver (hepatocytes). Adenomas are usually small and do not spread to other parts of the body.

The symptoms of liver neoplasms vary depending on their size, location, and whether they are benign or malignant. Common symptoms include abdominal pain, fatigue, weight loss, and jaundice (yellowing of the skin and eyes). Diagnosis is typically made through a combination of imaging tests such as CT scans, MRI scans, and ultrasound, and a biopsy to confirm the presence of cancer cells.

Treatment options for liver neoplasms depend on the type, size, location, and stage of the tumor, as well as the patient's overall health. Surgery may be an option for some patients with small, localized tumors, while others may require chemotherapy or radiation therapy to shrink the tumor before surgery can be performed. In some cases, liver transplantation may be necessary.

Prognosis for liver neoplasms varies depending on the type and stage of the cancer. In general, early detection and treatment improve the prognosis, while advanced-stage disease is associated with a poorer prognosis.

There are several different types of leukemia, including:

1. Acute Lymphoblastic Leukemia (ALL): This is the most common type of leukemia in children, but it can also occur in adults. It is characterized by an overproduction of immature white blood cells called lymphoblasts.
2. Acute Myeloid Leukemia (AML): This type of leukemia affects the bone marrow's ability to produce red blood cells, platelets, and other white blood cells. It can occur at any age but is most common in adults.
3. Chronic Lymphocytic Leukemia (CLL): This type of leukemia affects older adults and is characterized by the slow growth of abnormal white blood cells called lymphocytes.
4. Chronic Myeloid Leukemia (CML): This type of leukemia is caused by a genetic mutation in a gene called BCR-ABL. It can occur at any age but is most common in adults.
5. Hairy Cell Leukemia: This is a rare type of leukemia that affects older adults and is characterized by the presence of abnormal white blood cells called hairy cells.
6. Myelodysplastic Syndrome (MDS): This is a group of disorders that occur when the bone marrow is unable to produce healthy blood cells. It can lead to leukemia if left untreated.

Treatment for leukemia depends on the type and severity of the disease, but may include chemotherapy, radiation therapy, targeted therapy, or stem cell transplantation.

... (CoA-transferases) are transferase enzymes that catalyze the transfer of a coenzyme A group from an ... The CoA-transferases have been divided into six families (Cat1, OXCT1, Gct, MdcA, Frc, CitF) based on their amino acid ... These enzymes are found in all three domains of life (bacteria, eukaryotes, archaea). As a group, the CoA transferases catalyze ...

https://en.wikipedia.org/wiki/Coenzyme_A_transferases

Other names in common use include 3-oxoacid coenzyme A-transferase, 3-ketoacid CoA-transferase, 3-ketoacid coenzyme A ... succinyl coenzyme A-acetoacetyl coenzyme A-transferase, and succinyl-CoA transferase. This enzyme participates in 3 metabolic ... transferase, 3-oxo-CoA transferase, 3-oxoacid CoA dehydrogenase, acetoacetate succinyl-CoA transferase, acetoacetyl coenzyme A- ... Preparation and properties of coenzyme A transferase". J. Biol. Chem. 221 (1): 15-31. PMID 13345795. Portal: Biology v t e ( ...

https://en.wikipedia.org/wiki/3-oxoacid_CoA-transferase

Transferases are involved in myriad reactions in the cell. Three examples of these reactions are the activity of coenzyme A ( ... "Group" would be the functional group transferred as a result of transferase activity. The donor is often a coenzyme. Some of ... Terminal transferases are transferases that can be used to label DNA or to produce plasmid vectors. It accomplishes both of ... The A and B transferases are the foundation of the human ABO blood group system. Both A and B transferases are ...

https://en.wikipedia.org/wiki/Transferase

Genes on human chromosome 12, Transferases). ... Coenzyme Q10 Deficiency is associated with COQ5. Therefore, to ... Coenzyme Q5, methyltransferase, more commonly known as COQ5, is an enzyme involved in the electron transport chain. COQ5 is ... "COQ5 Gene - Coenzyme Q5, Methyltransferase". GeneCards human gene database. Weizmann Institute of Science. Dai YN, Zhou K, Cao ... COQ5 has the role of catalyst in the C-methylation in the coenzyme Q biosynthesis, on the benzoic ring of CoQ6, the ...

https://en.wikipedia.org/wiki/Coenzyme_Q5,_methyltransferase

The systematic name of this enzyme class is acetyl-CoA:malonate CoA-transferase. This enzyme is also called malonate coenzyme A ... This enzyme belongs to the family of transferases, specifically the CoA-transferases. ... In enzymology, a malonate CoA-transferase (EC 2.8.3.3) is an enzyme that catalyzes the chemical reaction acetyl-CoA + malonate ... Portal: Biology v t e (EC 2.8.3, Enzymes of unknown structure, All stub articles, Transferase stubs). ...

https://en.wikipedia.org/wiki/Malonate_CoA-transferase

Other names in common use include propionate coenzyme A-transferase, propionate-CoA:lactoyl-CoA transferase, propionyl CoA: ... This enzyme belongs to the family of transferases, specifically the CoA-transferases. The systematic name of this enzyme class ... Stadtman ER (1952). "Acyl-coenzyme A synthesis by phosphotransacetylase and coenzyme A transphorase". Fed. Proc. 11: 291. ... acetate CoA transferase, and propionyl-CoA transferase. This enzyme participates in 3 metabolic pathways: pyruvate metabolism, ...

https://en.wikipedia.org/wiki/Propionate_CoA-transferase

Other names in common use include formyl-coenzyme A transferase, and formyl-CoA oxalate CoA-transferase. As of late 2007, 4 ... Baetz AL, Allison MJ (1990). "Purification and characterization of formyl-coenzyme A transferase from Oxalobacter formigenes". ... This enzyme belongs to the family of transferases, specifically the CoA-transferases. The systematic name of this enzyme class ... "DNA sequencing and expression of the formyl coenzyme A transferase gene, frc, from Oxalobacter formigenes". J. Bacteriol. 179 ( ...

https://en.wikipedia.org/wiki/Formyl-CoA_transferase

"Transcriptional and functional analysis of oxalyl-coenzyme A (CoA) decarboxylase and formyl-CoA transferase genes from ... Oxalate-CoA ligase Formyl-CoA transferase Oxalate CoA-transferase Baetz AL, Allison MJ (July 1990). "Purification and ... No FAD binding is observed in oxalyl-CoA decarboxylase, but an excess of coenzyme A in the crystal structure has led to the ... characterization of formyl-coenzyme A transferase from Oxalobacter formigenes". Journal of Bacteriology. 172 (7): 3537-40. doi: ...

https://en.wikipedia.org/wiki/Oxalyl-CoA_decarboxylase

"Coenzyme A transferase family I (IPR004165) < InterPro < EMBL-EBI". www.ebi.ac.uk. Retrieved 2016-07-22. Orii KE, Fukao T, Song ... protein and messenger RNA levels of succinyl-coenzyme A (CoA):3-ketoacid CoA transferase and mitochondrial and cytosolic ... 3-oxoacid CoA transferase deficiency. This gene encodes a member of the 3-oxoacid CoA-transferase gene family. The encoded ... 3-oxoacid CoA-transferase 1 (OXCT1) is an enzyme that in humans is encoded by the OXCT1 gene. It is also known as succinyl-CoA- ...

https://en.wikipedia.org/wiki/OXCT1

Other names in common use include acetate coenzyme A-transferase, butyryl CoA:acetate CoA transferase, butyryl coenzyme A ... This enzyme belongs to the family of transferases, specifically the CoA-transferases. The systematic name of this enzyme class ... succinyl-coenzyme A (CoA) transferase and 3-oxoadipyl-CoA thiolase". J. Bacteriol. 184 (1): 207-15. doi:10.1128/JB.184.1.207- ... succinyl-coenzyme A (CoA) transferase and 3-oxoadipyl-CoA thiolase". J. Bacteriol. 184 (1): 216-23. doi:10.1128/JB.184.1.216- ...

https://en.wikipedia.org/wiki/Acetate_CoA-transferase

Transferases, Anaerobic digestion, All stub articles, Transferase stubs). ... It does so by combining the hydrogen donor coenzyme B and the methyl donor coenzyme M. Via this enzyme, most of the natural gas ... In enzymology, coenzyme-B sulfoethylthiotransferase, also known as methyl-coenzyme M reductase (MCR) or most systematically as ... Ellermann J, Rospert S, Thauer RK, Bokranz M, Klein A, Voges M, Berkessel A (September 1989). "Methyl-coenzyme-M reductase from ...

https://en.wikipedia.org/wiki/Coenzyme-B_sulfoethylthiotransferase

This enzyme is also called hydroxycinnamoyl coenzyme A-quinate transferase. This enzyme participates in phenylpropanoid ... This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl ... The systematic name of this enzyme class is feruloyl-CoA:quinate O-(hydroxycinnamoyl)transferase. ... "Purification and characterization of hydroxycinnamoyl D-glucose Quinate hydroxycinnamoyl transferase in the root of sweet ...

https://en.wikipedia.org/wiki/Quinate_O-hydroxycinnamoyltransferase

2007). "A mutation in para-hydroxybenzoate-polyprenyl transferase (COQ2) causes primary coenzyme Q10 deficiency". Am. J. Hum. ... "Entrez Gene: COQ2 coenzyme Q2 homolog, prenyltransferase (yeast)". Human COQ2 genome location and COQ2 gene details page in the ... 2006). "Coenzyme Q and the regulation of intracellular steady-state levels of superoxide in HL-60 cells". BioFactors. 25 (1-4 ... 2005). "Coenzyme Q2 induced p53-dependent apoptosis". Biochim. Biophys. Acta. 1724 (1-2): 49-58. doi:10.1016/j.bbagen.2005.04. ...

https://en.wikipedia.org/wiki/COQ2

... carnitine palmitoyl transferase, and cholesterol esterification) Propionyl-CoA Butyryl-CoA Myristoyl-CoA Crotonyl-CoA ... Coenzyme A (CoA, SHCoA, CoASH) is a coenzyme, notable for its role in the synthesis and oxidation of fatty acids, and the ... Coenzyme A is one of five crucial coenzymes that are necessary in the reaction mechanism of the citric acid cycle. Its acetyl- ... Coenzyme A is available from various chemical suppliers as the free acid and lithium or sodium salts. The free acid of coenzyme ...

https://en.wikipedia.org/wiki/Coenzyme_A

Other names in common use include 5-hydroxyvalerate CoA-transferase, and 5-hydroxyvalerate coenzyme A transferase. Eikmanns U, ... This enzyme belongs to the family of transferases, specifically the CoA-transferases. The systematic name of this enzyme class ... In enzymology, a 5-hydroxypentanoate CoA-transferase (EC 2.8.3.14) is an enzyme that catalyzes the chemical reaction acetyl-CoA ... Buckel W (1990). "Properties of 5-hydroxyvalerate CoA-transferase from Clostridium aminovalericum". Biol. Chem. Hoppe-Seyler. ...

https://en.wikipedia.org/wiki/5-hydroxypentanoate_CoA-transferase

Coenzyme A: A Coenzyme-B12-dependent Carbon Skeleton Rearrangement". Angewandte Chemie International Edition in English. 27 (8 ... This enzyme belongs to the family of isomerases, specifically those intramolecular transferases transferring other groups. The ... Other names in common use include isobutyryl coenzyme A mutase, and butyryl-CoA:isobutyryl-CoA mutase. It uses ...

https://en.wikipedia.org/wiki/Isobutyryl-CoA_mutase

Other names in common use include succinyl-beta-ketoacyl-CoA transferase, and oxalate coenzyme A-transferase. This enzyme ... This enzyme belongs to the family of transferases, specifically the CoA-transferases. The systematic name of this enzyme class ... In enzymology, an oxalate CoA-transferase (EC 2.8.3.2) is an enzyme that catalyzes the chemical reaction succinyl-CoA + oxalate ...

https://en.wikipedia.org/wiki/Oxalate_CoA-transferase

Other names in common use include 3-oxoadipate coenzyme A-transferase, and 3-oxoadipate succinyl-CoA transferase. This enzyme ... This enzyme belongs to the family of transferases, specifically the CoA-transferases. The systematic name of this enzyme class ... In enzymology, a 3-oxoadipate CoA-transferase (EC 2.8.3.6) is an enzyme that catalyzes the chemical reaction succinyl-CoA + 3- ...

https://en.wikipedia.org/wiki/3-oxoadipate_CoA-transferase

The systematic name of this enzyme class is sinapoyl-CoA:2-hydroxymalonate O-(hydroxycinnamoyl)transferase. Other names in ... Strack D, Ruhoff R, Grawe W (1986). "Hydroxycinnamoyl-Coenzyme-A-tartronate hydroxycinnamoyltransferase in protein preparations ... This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl ... common use include tartronate sinapoyltransferase, and hydroxycinnamoyl-coenzyme-A:tartronate hydroxycinnamoyltransferase. ...

https://en.wikipedia.org/wiki/Tartronate_O-hydroxycinnamoyltransferase

Other names in common use include hydroxymethylglutarate coenzyme A-transferase, and dicarboxyl-CoA:dicarboxylic acid coenzyme ... This enzyme belongs to the family of transferases, specifically the CoA-transferases. The systematic name of this enzyme class ... 3-hydroxy-3-methylglutarate coenzyme A transferase from rat liver". Biochim. Biophys. Acta. 662 (1): 119-24. doi:10.1016/0005- ... Portal: Biology v t e (EC 2.8.3, Enzymes of unknown structure, All stub articles, Transferase stubs). ...

https://en.wikipedia.org/wiki/Succinate—hydroxymethylglutarate_CoA-transferase

Dickert S, Pierik AJ, Linder D, Buckel W (2000). "The involvement of coenzyme A esters in the dehydration of (R)-phenyllactate ... This enzyme belongs to the CoA-transferase family. The systematic name of this enzyme class is (E)-cinnamoyl-CoA:(R)- ... In enzymology, a cinnamoyl-CoA:phenyllactate CoA-transferase (EC 2.8.3.17) is an enzyme that catalyzes the chemical reaction (E ... Portal: Biology v t e (EC 2.8.3, Enzymes of unknown structure, All stub articles, Transferase stubs). ...

https://en.wikipedia.org/wiki/Cinnamoyl-CoA:phenyllactate_CoA-transferase

Succinyl-CoA:3-oxoacid CoA transferase catalyzes the transfer of coenzyme A from succinyl-coenzyme A to acetoacetate. It can be ... Succinyl-CoA:3-oxoacid CoA transferase deficiency is an inborn error of ketone body utilization. ...

https://en.wikipedia.org/wiki/Succinyl-CoA:3-oxoacid_CoA_transferase_deficiency

This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl ... Other names in common use include acylglycerol palmitoyltransferase, monoglyceride acyltransferase, acyl coenzyme A- ...

https://en.wikipedia.org/wiki/2-acylglycerol_O-acyltransferase

Tobin MB, Fleming MD, Skatrud PL, Miller JR (1990). "Molecular characterization of the acyl-coenzyme A:isopenicillin N ... This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl ... Other names in common use include acyl-coenzyme A:isopenicillin N acyltransferase, and isopenicillin N:acyl-CoA: ... β-heterodimeric acyl-coenzyme A: isopenicillin N-acyltransferase of Penicillium chrysogenum". FEBS Letters. 319 (1-2): 166-170 ...

https://en.wikipedia.org/wiki/Isopenicillin_N_N-acyltransferase

Other names in common use include butyryl coenzyme A-acetoacetate coenzyme A-transferase, and butyryl-CoA-acetoacetate CoA- ... This enzyme belongs to the family of transferases, specifically the CoA-transferases. The systematic name of this enzyme class ... transferase. Barker HA, Jeng IM, Neff N, Robertson JM, Tam FK, Hosaka S (1978). "Butyryl-CoA:acetoacetate CoA-transferase from ... In enzymology, a butyrate-acetoacetate CoA-transferase (EC 2.8.3.9) is an enzyme that catalyzes the chemical reaction butanoyl- ...

https://en.wikipedia.org/wiki/Butyrate—acetoacetate_CoA-transferase

KENNEDY EP, WEISS SB (1956). "The function of cytidine coenzymes in the biosynthesis of phospholipides". J. Biol. Chem. 222: ... This enzyme belongs to the family of transferases, specifically those transferring non-standard substituted phosphate groups. ... and phosphorylethanolamine-glyceride transferase. This enzyme participates in 3 metabolic pathways: aminophosphonate metabolism ...

https://en.wikipedia.org/wiki/Diacylglycerol_ethanolaminephosphotransferase

... coenzyme M-epoxyalkane ligase, epoxyalkyl:CoM transferase, epoxypropane:coenzyme M transferase, epoxypropyl:CoM transferase, ... coenzyme M transferase, epoxyalkane:CoM transferase, epoxyalkane:2-mercaptoethanesulfonate transferase, ... Coleman NV, Spain JC (September 2003). "Epoxyalkane: coenzyme M transferase in the ethene and vinyl chloride biodegradation ... Allen JR, Clark DD, Krum JG, Ensign SA (July 1999). "A role for coenzyme M (2-mercaptoethanesulfonic acid) in a bacterial ...

https://en.wikipedia.org/wiki/2-hydroxypropyl-CoM_lyase

It is an organic compound containing a coenzyme substructure, which classifies it as a fatty ester lipid molecule. Being a ... Glutaconate CoA-transferase Glutaconyl-CoA decarboxylase "Glutaryl-CoA Dehydrogenase - an overview , ScienceDirect Topics". www ... Thioesters of coenzyme A, All stub articles, Organic compound stubs). ...

https://en.wikipedia.org/wiki/Glutaconyl-CoA

Saylor MH, Mansell RL (1977). "Hydroxycinnamoyl: coenzyme A transferase involved in the biosynthesis of kaempferol-3-(p- ... This enzyme belongs to the family of transferases, to be specific those acyltransferases transferring groups other than ...

https://en.wikipedia.org/wiki/Flavonol-3-O-triglucoside_O-coumaroyltransferase

... substrate specificity and kinetic behavior of Escherichia coli YfdW and Oxalobacter formigenes formyl coenzyme A transferase". ... Studies have shown that homocysteine reacts with SDH's PLP coenzyme to create a complex. This complex is devoid of coenzyme ...

https://en.wikipedia.org/wiki/Serine_dehydratase

The catabolism of the methyl compounds is mediated by methyl transferases to give methyl coenzyme M. The biochemistry of ... April 2003). "Coenzyme B induced coordination of coenzyme M via its thiol group to Ni(I) of F430 in active methyl-coenzyme M ... The mechanism for the conversion of CH 3-S bond into methane involves a ternary complex of methyl coenzyme M and coenzyme B fit ... Coupling of the coenzyme M thiyl radical (RS.) with HS coenzyme B releases a proton and re-reduces Ni(II) by one-electron, ...

https://en.wikipedia.org/wiki/Methanogenesis

The electrons then flow through photosystem I and can then be used to reduce the coenzyme NADP+. This coenzyme can enter the ... Sheehan D, Meade G, Foley VM, Dowd CA (November 2001). "Structure, function and evolution of glutathione transferases: ... These coenzymes are therefore continuously made, consumed and then recycled. One central coenzyme is adenosine triphosphate ( ... This reduced form of the coenzyme is then a substrate for any of the reductases in the cell that need to transfer hydrogen ...

https://en.wikipedia.org/wiki/Metabolism

... syndrome type 2 Cockayne syndrome type 3 Cockayne's syndrome Codas syndrome Codesette syndrome Coeliac disease Coenzyme Q ... Carnevale-Hernandez-Castillo syndrome Carnevale-Krajewska-Fischetto syndrome Carney syndrome Carnitine palmitoyl transferase ...

https://en.wikipedia.org/wiki/List_of_diseases_(C)

Characterization of sequences at the inhibitor and coenzyme binding sites". The Journal of Biological Chemistry. 267 (1): 150- ... Transferase 1.92, Lyase 1.59, Isomerase 1.51, Phosphodiesterase 1.50, Cytochrome p450 0.84, Epigenetic eraser 0.33, Total ...

https://en.wikipedia.org/wiki/Enzyme_inhibitor

... and lecithin retinol acyl transferase. Higa HH, Varki A (1988). "Acetyl-coenzyme A:polysialic acid O-acetyltransferase from K1- ... This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl ...

https://en.wikipedia.org/wiki/Polysialic-acid_O-acetyltransferase

Glutathione S-transferase uses GSH to clean up various metabolites, xenobiotics, and electrophiles to mercapturates for ... "Glutathione synthetase homologs encode alpha-L-glutamate ligases for methanogenic coenzyme F420 and tetrahydrosarcinapterin ... such as H2O2 or Glutathione S-transferases in the detoxification of xenobiotics. Glutathione synthetase is important for a ...

https://en.wikipedia.org/wiki/Glutathione_synthetase

Somack R, Costilow RN (1973). "Purification and properties of a pyridoxal phosphate and coenzyme B 12 dependent D- -ornithine 5 ... This enzyme belongs to the family of isomerases, specifically those intramolecular transferases transferring amino groups. The ... It has 3 cofactors: pyridoxal phosphate, Cobamide coenzyme, and Dithiothreitol. ...

https://en.wikipedia.org/wiki/D-ornithine_4,5-aminomutase

doi:10.1016/0076-6879(71)18327-9. HOAGLAND MB, NOVELLI GD (1954). "Biosynthesis of coenzyme A from phospho-pantetheine and of ... This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups ( ... Wang TP, Kaplan NO (1954). "Kinases for the synthesis of coenzyme A and triphosphopyridine nucleotide". J. Biol. Chem. 206 (1 ... Abiko Y (1970). "Pantothenic acid and coenzyme A:dephospho-CoA pyrophosphorylase and dephospho-CoA kinase as a possible ...

https://en.wikipedia.org/wiki/Dephospho-CoA_kinase

... methylmalonyl Coenzyme A mutase (6p12.3) NHLRC1: NHL repeat containing E3 ubiquitin protein ligase 1 (6p22.3) NOL7: nucleolar ... 6-N-acetylglucosaminyl-transferase (6p24.3) GMDS: GDP-mannose 4,6-dehydratase (6p25.3) HCG4P11: HLA complex group 4 pseudogene ...

https://en.wikipedia.org/wiki/Chromosome_6

Beg ZH, Stonik JA, Brewer HB Jr (1985). "Phosphorylation of hepatic 3-hydroxy-3-methylglutaryl coenzyme A reductase and ... This enzyme belongs to the family of transferases, specifically those transferring a phosphate group to the sidechain oxygen ... Other names in common use include AMP-activated kinase, AMP-activated protein kinase kinase, hydroxymethylglutaryl coenzyme A ... a protein kinase that modulates the enzymic activity of 3-hydroxy-3-methylglutaryl-coenzyme A reductase". Proc. Natl. Acad. Sci ...

https://en.wikipedia.org/wiki/Dephospho-(reductase_kinase)_kinase

"Acyl-coenzyme A binding protein expression alters liver fatty acyl-coenzyme A metabolism". Biochemistry. 44 (30): 10282-97. doi ... Acyl-CoA cholesterol acyl transferase EC 2.3.1.26, more simply referred to as ACAT, also known as sterol O-acyltransferase ( ... This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl ... "Effect of geometry and position of ethylenic bond upon acyl coenzyme A--cholesterol-O-acyltransferase". Biochemistry. 9 (8): ...

https://en.wikipedia.org/wiki/Sterol_O-acyltransferase

CPT-I inhibitors: Etomoxir, Oxfenicine, Perhexiline CPT-I (carnitine palmitoyl transferase) converts fatty acyl-CoA to fatty ... Carnitine biosynthesis inhibitor: Mildronate 3-KAT inhibitors: Trimetazidine 3-KAT (3-ketoacyl-coenzyme A thiolase) inhibitors ...

https://en.wikipedia.org/wiki/Fatty_acid_oxidation_inhibitors

A pseudo 2 fold symmetry of the region surrounding the peptidyl transferase center led to the hypothesis of the Proto-Ribosome ... Ribonucleotide moieties in many coenzymes, such as acetyl-CoA, NADH, FADH, and F420, may be surviving remnants of covalently ... The large subunit of the ribosome includes an rRNA responsible for the peptide bond-forming peptidyl transferase activity of ... Harper & Row White HB (Mar 1976). "Coenzymes as fossils of an earlier metabolic state". Journal of Molecular Evolution. 7 (2): ...

https://en.wikipedia.org/wiki/RNA_world

The thiol from coenzyme A serves as a good leaving group when attacked by a general base to give N-acetylserotonin. N- ... It has been proposed that histidine residue His122 of serotonin N-acetyl transferase is the catalytic residue that deprotonates ...

https://en.wikipedia.org/wiki/Melatonin

Formyl-CoA transferase （EC 2.8.3.16）mediates the exchange of oxalyl and formyl groups on coenzyme A, interconverting formyl-CoA ... Enzymes in this class include oxalate oxidase, oxalate decarboxylase, oxalyl-CoA decarboxylase, and formyl-CoA transferase. ...

https://en.wikipedia.org/wiki/Oxalate_degrading_enzyme

Orotate is covalently linked with phosphoribosyl pyrophosphate (PRPP) by orotate phosphoribysol-transferase yielding orotidine ... Co-enzyme N10-formyl-THF, along with enzyme GAR transformylase, then donates a one-carbon unit to the amino group onto the ...

https://en.wikipedia.org/wiki/Ribonucleotide

Cinnamoyl-Coenzyme A is an intermediate in the phenylpropanoids metabolic pathway. Cinnamoyl-CoA reductase, an enzyme that ... phenyllactate CoA-transferase, an enzyme that catalyzes the chemical reaction (E)-cinnamoyl-CoA + (R)-phenyllactate → (E)- ... Thioesters of coenzyme A, Cinnamate esters, All stub articles, Aromatic compound stubs). ...

https://en.wikipedia.org/wiki/Cinnamoyl-CoA

... or UDP-GlcNAc is a nucleotide sugar and a coenzyme in metabolism. It is used by ... Clostridium novyi type A alpha-toxin is an O-linked N-actetylglucosamine transferase acting on Rho proteins and causing the ... UDP-GlcNAc is extensively involved in intracellular signaling as a substrate for O-linked N-acetylglucosamine transferases ( ...

https://en.wikipedia.org/wiki/Uridine_diphosphate_N-acetylglucosamine

This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The ... "Biosynthesis of the corrin macrocycle of coenzyme B12 in Pseudomonas denitrificans". J. Bacteriol. 175 (22): 7430-40. PMC ...

https://en.wikipedia.org/wiki/Precorrin-6A_synthase_(deacetylating)

2009). "A human vitamin B12 trafficking protein uses glutathione transferase activity for processing alkylcobalamins". J. Biol ... of cobalamins in human lymphocytes in vitro and the influence of nitrous oxide on the synthesis of cobalamin coenzymes". ...

https://en.wikipedia.org/wiki/MMACHC

COQ2 Coenzyme Q10 deficiency; 607426; COQ9 Coenzyme Q10 deficiency; 607426; PDSS1 Coenzyme Q10 deficiency; 607426; PDSS2 Coffin ... 3-oxoacid CoA transferase deficiency; 245050; OXCT1 Sucrase-isomaltase deficiency, congenital; 222900; SI Sudden infant death ... CHUK Coenzyme Q10 deficiency; 607426; APTX Coenzyme Q10 deficiency; 607426; CABC1 Coenzyme Q10 deficiency; 607426; ... TMPRSS6 Isobutyryl-coenzyme A dehydrogenase deficiency; 611283; ACAD8 Isovaleric acidemia; 243500; IVD IVIC syndrome; 147750; ...

https://en.wikipedia.org/wiki/List_of_OMIM_disorder_codes

This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl ... Substrate and intracellular localization of bovine acetyl-coenzyme A: N-acetylneuraminate-7- and 8-O-acetyltransferase]". Hoppe ...

https://en.wikipedia.org/wiki/N-acetylneuraminate_7-O(or_9-O)-acetyltransferase

... coenzyme F420-0:L-glutamate ligase EC 6.3.2.32: coenzyme γ-F420-2:α-L-glutamate ligase EC 6.3.2.33: tetrahydrosarcinapterin ... several ubiquitin transferases and finally by EC 2.3.2.27 [ubiquitin transferase RING E3 (calmodulin-selective)] EC 6.3.2.22: ... coenzyme F430 synthetase * *No Wikipedia article EC 6.5.1.1: DNA ligase (ATP) EC 6.5.1.2: DNA ligase (NAD+) EC 6.5.1.3: RNA ... long-chain fatty acid adenylase/transferase FadD23 * EC 6.2.1.58: isophthalate-CoA ligase * EC 6.2.1.59: long-chain fatty acid ...

https://en.wikipedia.org/wiki/List_of_EC_numbers_(EC_6)

Pyruvate is oxidized into acetyl coenzyme A catalyzed by pyruvate:ferredoxin oxidoreductase. Two molecules of carbon dioxide ( ... acetate CoA-transferase pathway, whereas carnivores have butyrate-producing bacterial communities dominated by the butyrate ... coenzyme A → adenosine monophosphate + pyrophosphate + butyryl-CoA As a short-chain fatty acid, butyrate is metabolized by ...

https://en.wikipedia.org/wiki/Butyric_acid

Synthesis Palmitic acid Coenzyme A Coenzyme A CoA Brady, R.N.; DiMari, S.J.; Snell, E.E. (1969). "Biosynthesis of sphingolipid ... This transesterification reaction is catalyzed by carnitine palmitoyl transferase. Palmitoyl-Carnitine may translocate across ... The activation is catalyzed by palmitoyl-coenzyme A synthetase and the reaction proceeds through a two step mechanism, in which ... ISBN 978-1-118-91840-1. Bar-Tana, J.; Rose, G.; Brandes, R.; Shapiro, B. (1973-02-01). "Palmitoyl-coenzyme A synthetase. ...

https://en.wikipedia.org/wiki/Palmitoyl-CoA

Role of acyl-coenzyme A: cholesterol transferase 1 (ACAT1) in retinal neovascularization.. Zaidi, Syed A H; Lemtalsi, Tahira; ... coenzyme A cholesterol transferase 1 (ACAT1). Dyslipidemia and cholesterol accumulation have been strongly implicated in ... Transferases Coenzima A/efeitos adversos Lipídeos/efeitos adversos Camundongos Endogâmicos C57BL Modelos Animais de Doenças ...

https://pesquisa.bvsalud.org/perinatal/resource/pt/mdl-36691048

Enzymes and Coenzymes [D08]. *Enzymes [D08.811]. *Transferases [D08.811.913]. *Phosphotransferases [D08.811.913.696] ...

https://connects.catalyst.harvard.edu/Profiles/display/Concept/Thiamin%20Pyrophosphokinase

acetate CoA-transferase *Synonyms: succinyl-CoA:acetate CoA transferase; butyryl coenzyme A transferase; acetate coenzyme A- ... transferase; butyryl CoA:acetate CoA transferase. *EC number: 2.8.3.8. *Enzyme-specific links *Kyoto *ExPASy *BRENDA *IntEnz * ... Reactions catalyzed by acetate CoA-transferase *Butyryl-CoA -----, Butyrate (reacID# r0012) *3-Hydroxy-5-oxohexanoate -----, 3- ...

http://eawag-bbd.ethz.ch/servlets/pageservlet?ptype=e&ECcode=2.8.3.8

201 ACLY is the transferase that catalyzes the conversion of citrate and coenzyme A to acetyl-CoA during fatty acid metabolism ... 196 Conversion of cytosolic citrate to acetyl-coenzyme A (acetyl-CoA) and oxaloacetate by ACLY is critical for fatty acid ... and that for glutathione S-transferase (GST), which catalyzes the conjugation of GSH to xenobiotic compounds enabling their ... a form of Vitamin B3 and the precursor of the coenzymes nicotinamide adenine dinucleotide (NAD) and nicotinamide adenine ...

https://www.nature.com/articles/s41422-020-0291-z?error=cookies_not_supported

Succinyl-CoA:3-ketoacid CoA transferase deficiency. *Succinyl-CoA:3-oxoacid CoA transferase deficiency, see Succinyl-CoA:3- ... Short-chain acyl-coenzyme A dehydrogenase deficiency, see Short-chain acyl-CoA dehydrogenase deficiency ... Succinyl-CoA:acetoacetate transferase deficiency, see Succinyl-CoA:3-ketoacid CoA transferase deficiency ... Succinyl-CoA 3-oxoacid transferase deficiency, see Succinyl-CoA:3-ketoacid CoA transferase deficiency ...

https://medlineplus.gov/genetics/condition-s/

Enzymes and Coenzymes [D08]. *Enzymes [D08.811]. *Transferases [D08.811.913]. *Phosphotransferases [D08.811.913.696] ...

https://profiles.umassmed.edu/display/115092

Enzymes and Coenzymes [D08] * Enzymes [D08.811] * Transferases [D08.811.913] * Phosphotransferases [D08.811.913.696] * ...

https://meshb.nlm.nih.gov/record/ui?ui=D014541

... mediated by inhibition of 3 hydroxy 3 methyl glutoryl coenzyme A reductase and acyl coenzyme A cholesterol acyl transferase in ...

https://www.scirp.org/journal/PaperInformation.aspx?paperID=8421&

Distribution of herbicide-resistant acetyl-coenzyme A carboxylase alleles in Lolium rigidum across grain cropping areas of ... the carboxyl transferase (CT) domain of the ACCase gene from resistant L. rigidum plants, collected from both random surveys of ... Resistance to the acetyl-coenzyme A carboxylase (ACCase)-inhibiting herbicides in Lolium rigidum is widespread in grain ...

https://weedscience.com/details/Case.aspx?ResistID=5226

glutathione S-transferase alpha 1. multiple interactions. ISO. Palmitoyl Coenzyme A binds to and results in decreased activity ... valproyl-coenzyme A inhibits the reaction [CPT1A protein results in increased metabolism of Palmitoyl Coenzyme A]. CTD. PMID: ... Palmitoyl Coenzyme A results in decreased expression of SHBG mRNA; Palmitoyl Coenzyme A results in decreased expression of SHBG ... Palmitoyl Coenzyme A results in decreased expression of HNF4A mRNA; Palmitoyl Coenzyme A results in decreased expression of ...

https://rgd.mcw.edu/rgdweb/ontology/annot.html?acc_id=CHEBI:15539

acetoacetyl Coenzyme A thiolase. *Acetyl CoA acetyltransferase. *Acetyl CoA transferase like protein ...

https://www.abcam.cn/products/proteins-peptides/recombinant-human-acat2acetyl-coa-acetyltransferase-protein-ab98082.html

Biosynthesis of polylactic acid and its copolymers using evolved propionate CoA transferase and PHA synthase. Yang, T. H., Kim ... Biosynthesis of 2-Hydroxyacid-Containing Polyhydroxyalkanoates by Employing butyryl-CoA Transferases in Metabolically ...

https://pure.ewha.ac.kr/en/persons/si-jae-park/publications/?ordering=title&descending=false

Enzymes and Coenzymes [D08]. *Enzymes [D08.811]. *Transferases [D08.811.913]. *Aldehyde-Ketone Transferases [D08.811.913.200] ...

https://profiles.musc.edu/display/97002/

Enzymes and Coenzymes [D08]. *Enzymes [D08.811]. *Transferases [D08.811.913]. *Nitrogenous Group Transferases [D08.811.913.477] ...

https://profiles.ouhsc.edu/display/21583

Enzymes and Coenzymes [D08]. *Enzymes [D08.811]. *Transferases [D08.811.913]. *Phosphotransferases [D08.811.913.696] ...

https://profiles.uchicago.edu/profiles/display/14090

Acyl-CoA-Transferases CoA Transferases CoA-Transferases Coenzyme A Transferases Transferases, CoA Transferases, Coenzyme A ... Acyl-CoA-Transferases. CoA Transferases. CoA-Transferases. Coenzyme A Transferases. Transferases, CoA. Transferases, Coenzyme A ... Coenzyme A-Transferases Entry term(s). A-Transferases, Coenzyme Acyl CoA Transferases ... Coenzyme A-transferases Entry term(s):. A-Transferases, Coenzyme. Acyl CoA Transferases. ...

https://decs.bvsalud.org/en/ths/resource/?id=23592

probable coenzyme A transferase (NCBI). 138, 189. PA5506. PA5506. hypothetical protein (NCBI). 138, 358. ...

https://networks.systemsbiology.net/pae/gene/PA5510

Acetate utilization and butyryl coenzyme A (CoA): acetate-CoA transferase in butyrate-producing bacteria from the human large ...

https://abdn.pure.elsevier.com/en/publications/?showAdvanced=false&allConcepts=true&inferConcepts=true&originalSearch=&improvedLayoutOrganisationUuid=&format=&ordering=title&descending=false&page=20

Enzymes and Coenzymes [D08] * Enzymes [D08.811] * Transferases [D08.811.913] * One-Carbon Group Transferases [D08.811.913.555] ...

https://meshb-prev.nlm.nih.gov/record/ui?ui=D000076983

Peptidase C45, acyl-coenzyme A:6-aminopenicillanic acid acyl-transferase IPR005079 - 0.0. - ...

https://www.scbi.uma.es/sustainpinedb/unigens/28?tab=ung&ung_id=1205266

Folic acid and vitamin B12 are coenzymes for catechol-O-methyl transferase important in the breakdown of catecholamines. ...

https://annals-general-psychiatry.biomedcentral.com/articles/10.1186/1744-859X-7-13

Enzymes belong to the co enzymes of the following group:. Oxidoreductases. Transferase. ...

https://almardia.qa/en/products/environmental/mykrobak-sew/

A-Transferases, Coenzyme use Coenzyme A-Transferases A-Type Potassium Channel Modulatory Protein 1 use Kv Channel-Interacting ... A-Monacylglycerophosphateacyltransferase, Acyl Coenzyme use 1-Acylglycerol-3-Phosphate O-Acyltransferase A-Particle Element, ... A-sn-1,2-Diacylglycerol Acyltransferase, Palmitoyl-Coenzyme use Diacylglycerol O-Acyltransferase ...

https://decs.bvs.br/I/DeCS2016_Alfab-A.htm

... cobalamin adenosyl transferase (Cbl B), (c and d) cytosolic Cbl metabolism (Cbl C and D), (e and g) methyl transferase Cbl ... The former is required for conversion of L-methylmalonic acid to succinyl coenzyme A (CoA), and the latter acts as a ... cobalamin adenosyl transferase (Cbl B), (c and d) cytosolic Cbl metabolism (Cbl C and D), (e and g) methyl transferase Cbl ... The cobalt atom is reduced in a nicotinamide adenine dinucleotide (NADH)-dependent reaction to yield the active coenzyme. It ...

http://emedicine.medscape.com/article/204930-overview

lactis: Impact of Acidic Conditions on the Transcriptional Levels of the Oxalyl Coenzyme A (CoA) Decarboxylase and Formyl-CoA ...

https://www.thegrainfactory-sg.com/blogs/news/oxalates-in-your-plant-food

... transferase activity;2.23392919970439e-09!GO:0065002;intracellular protein transport across a membrane;2.24538098208788e-09!GO: ... group transfer coenzyme metabolic process;7.72227460727237e-07!GO:0031324;negative regulation of cellular metabolic process; ... transferase activity, transferring alkyl or aryl (other than methyl) groups;0.0160663505894548!GO:0046966;thyroid hormone ... coenzyme metabolic process;2.06106460967692e-12!GO:0051082;unfolded protein binding;2.08707077766852e-12!GO:0006446;regulation ...

https://fantom.gsc.riken.jp/resource_browser/index.php?title=FF:10432-106D9&action=edit

... coenzyme (non-protein organic part). Holoenzyme (active enzyme) Apoenzyme + Coenzyme (protein part) (non-protein part) 9 ... 2. Transferases : Enzymes that catalyse the transfer of functional groups. 3. Hydrolases : Enzymes that bring about hydrolysis ... chemistry of enzymes, ES complex theories, co factors and coenzymesmuti ullah3.1K. visualizações•28. slides ... coenzyme (if any) and the type of the reaction catalysed by the enzyme. ...

https://pt.slideshare.net/sayalipowar/chapter-6pptx-256740567

MUT: methylmalonyl Coenzyme A mutase (6p12.3). *NHLRC1: NHL repeat containing E3 ubiquitin protein ligase 1 (6p22.3) ... GCNT2: N-acetyllactosaminide beta-1,6-N-acetylglucosaminyl-transferase (6p24.3). *GMDS: GDP-mannose 4,6-dehydratase (6p25.3) ...

https://wikidoc.org/index.php/Chromosome_6

compound?CoA: Coenzyme A?COAD: Chronic obstructive airways disease?COD: Cause of death?COG: Closed angle glaucoma?COLD: Chronic ... Compound?COMT : Catecholamine-O-methyl-transferase inhibitors?ConA: Concanavalin A?conc. : Concentrated?COP: Capillary osmotic ... transferase)?GGTP: ?GH: Growth hormone?GHB: Gamma hydroxybutyrate?GHRH: Growth hormone-releasing hormone?GHRIH: Growth hormone ... Hypoxanthineguanine phosphoribosyl transferase?HGV: Hepatitis G virus?HHNKC: Hyperglycemic Hyperosmolar Non-Ketotic Coma?HHV: ...

http://kuwaitpharmacy.com/page/9-About-Us.aspx

Protein Acetyl Cholesterol Encodes Reactions Acid Active Cells Primary coenzyme Q10 deficiency Enzymes Deficiency Molecule Mutations COQ2

System kinetics were influenced by domain dissections, and the FAS phosphopantetheinyl transferase (PPT) monodomain exhibited coenzyme A selectivity for the post-translational activation of the FAS acyl carrier protein (ACP). (nih.gov)
This gene encodes the bifunctional protein coenzyme A synthase (CoAsy) which carries out the last two steps in the biosynthesis of CoA from pantothenic acid (vitamin B5). (nih.gov)

Enzymes which transfer coenzyme A moieties from acyl- or acetyl-CoA to various carboxylic acceptors forming a thiol ester. (nih.gov)
Coenzyme A (CoA) functions as a carrier of acetyl and acyl groups in cells and thus plays an important role in numerous synthetic and degradative metabolic pathways in all organisms. (nih.gov)

Role of acyl-coenzyme A: cholesterol transferase 1 (ACAT1) in retinal neovascularization. (bvsalud.org)
We have investigated the efficacy of a new strategy to limit pathological retinal neovascularization (RNV) during ischemic retinopathy by targeting the cholesterol metabolizing enzyme acyl- coenzyme A cholesterol transferase 1 (ACAT1). (bvsalud.org)

in two siblings with the infantile form of CoQ10 deficiency, we identified a homozygous missense mutation in the COQ2 gene which encodes para-hydroxybenzoate-polyprenyl transferase, the enzyme responsible for the condensation of the isoprenoid side chains to the benzoquinone ring. (nih.gov)

It catalyzes 2 types of reactions, which involve either rearrangements (conversion of l methylmalonyl coenzyme A [CoA] to succinyl CoA) or methylation (synthesis of methionine). (medscape.com)

An acyl-CoA that results from the formal condensation of the thiol group of coenzyme A with the carboxy group of propionic acid. (mcw.edu)
The former is required for conversion of L- methylmalonic acid to succinyl coenzyme A (CoA), and the latter acts as a methyltransferase for conversion of homocysteine to methionine. (medscape.com)

The cobalt atom is reduced in a nicotinamide adenine dinucleotide (NADH)-dependent reaction to yield the active coenzyme. (medscape.com)

Aim 4: In collaboration with Professor Placido Navas, University of Sevilla, Spain, we will characterize CoQ10 biosynthetic genes and mutations in yeast.Narrative Coenzyme Q10 (CoQ10) is a vital molecule required for cells to generate energy and to prevent damage from toxic oxygen radicals. (nih.gov)

However, the COQ2 gene variations associated with an increased risk of this disorder are thought to affect coenzyme Q10 levels less severely than the COQ2 gene mutations that cause primary coenzyme Q10 deficiency (described below). (nih.gov)
At least nine mutations in the COQ2 gene have been found to cause a disorder known as primary coenzyme Q10 deficiency. (nih.gov)
These changes can cause cells throughout the body to malfunction, which may help explain the variety of organs and tissues that can be affected by primary coenzyme Q10 deficiency. (nih.gov)

Enzymes which transfer coenzyme A moieties from acyl- or acetyl-CoA to various carboxylic acceptors forming a thiol ester. (nih.gov)

In two siblings of consanguineous parents with the infantile form of CoQ(10) deficiency, we identified a homozygous missense mutation in the COQ2 gene, which encodes para-hydroxybenzoate-polyprenyl transferase. (nih.gov)
in two siblings with the infantile form of CoQ10 deficiency, we identified a homozygous missense mutation in the COQ2 gene which encodes para-hydroxybenzoate-polyprenyl transferase, the enzyme responsible for the condensation of the isoprenoid side chains to the benzoquinone ring. (nih.gov)
Studies suggest that a shortage (deficiency) of coenzyme Q10 impairs oxidative phosphorylation and increases the vulnerability of cells to damage from free radicals. (nih.gov)
A deficiency of coenzyme Q10 may also disrupt the production of pyrimidines. (nih.gov)
Desbats MA, Lunardi G, Doimo M, Trevisson E, Salviati L. Genetic bases and clinical manifestations of coenzyme Q10 (CoQ 10) deficiency. (nih.gov)

Abstract: Coenzyme Q10 (CoQ10) is a small lipophillic molecule composed of a benzoquinone ring and a hydrophobic isoprenoid tail and is present in virtually all cell membranes. (nih.gov)
Aim 4: In collaboration with Professor Placido Navas, University of Sevilla, Spain, we will characterize CoQ10 biosynthetic genes and mutations in yeast.Narrative Coenzyme Q10 (CoQ10) is a vital molecule required for cells to generate energy and to prevent damage from toxic oxygen radicals. (nih.gov)
The COQ2 gene provides instructions for making an enzyme that carries out one step in the production of a molecule called coenzyme Q10, which has several critical functions in cells throughout the body. (nih.gov)

The COQ2 gene mutations associated with this disorder greatly reduce or eliminate the production of the COQ2 enzyme, which prevents the normal production of coenzyme Q10. (nih.gov)

Researchers speculate that changes in the COQ2 gene could impair the activity of the COQ2 enzyme, which would affect the production of coenzyme Q10. (nih.gov)

Anatomy9

Organisms15

Diseases1

Chemicals and Drugs156

Analytical, Diagnostic and Therapeutic Techniques and Equipment25

Phenomena and Processes46

Disciplines and Occupations1

Information Science5

Health Care1

A functional 4-hydroxysalicylate/hydroxyquinol degradative pathway gene cluster is linked to the initial dibenzo-p-dioxin pathway genes in Sphingomonas sp. strain RW1. (1/146)

Oxygen exchange between acetate and the catalytic glutamate residue in glutaconate CoA-transferase from Acidaminococcus fermentans. Implications for the mechanism of CoA-ester hydrolysis. (2/146)

Regulation and adaptation of glucose metabolism of the parasitic protist Leishmania donovani at the enzyme and mRNA levels. (3/146)

Protection of mice against brucellosis by vaccination with Brucella melitensis WR201(16MDeltapurEK). (4/146)

Isolation and characterization of a haploid germ cell-specific novel complementary deoxyribonucleic acid; testis-specific homologue of succinyl CoA:3-Oxo acid CoA transferase. (5/146)

Nitration of succinyl-CoA:3-oxoacid CoA-transferase in rats after endotoxin administration. (6/146)

Succinyl-CoA:(R)-benzylsuccinate CoA-transferase: an enzyme of the anaerobic toluene catabolic pathway in denitrifying bacteria. (7/146)

Diabetes-associated nitration of tyrosine and inactivation of succinyl-CoA:3-oxoacid CoA-transferase. (8/146)

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Coenzyme A

Coenzymes

Transferases

Glutathione Transferase

Alkyl and Aryl Transferases

Coenzyme A-Transferases

Ubiquinone

Acetyl Coenzyme A

Coenzyme A Ligases

Transferases (Other Substituted Phosphate Groups)

DNA Nucleotidylexotransferase

Cobamides

Hydroxymethylglutaryl CoA Reductases

Molecular Sequence Data

Kinetics

Mesna

Acyltransferases

Substrate Specificity

NAD

Peptidyl Transferases

Amino Acid Sequence

N-Acetylglucosaminyltransferases

Pantothenic Acid

ADP Ribose Transferases

Farnesyltranstransferase

Escherichia coli

Mevalonic Acid

Liver

Pantetheine

Base Sequence

Euryarchaeota

Catalysis

Nucleotidyltransferases

Propanediol Dehydratase

Binding Sites

Protein Prenylation

Cloning, Molecular

Dinitrochlorobenzene

NADP

Hydroxymethylglutaryl-CoA Reductase Inhibitors

Methanosarcina barkeri

Galactosyltransferases

N-Acetylgalactosaminyltransferases

Palmitoyl Coenzyme A

Alcohol Oxidoreductases

Lovastatin

Acetate-CoA Ligase

Riboflavin

Methyltransferases

Isoenzymes

Malonyl Coenzyme A

Sequence Homology, Amino Acid

Oxidoreductases

gamma-Glutamyltransferase

Mutation

Methanobacterium

Bacterial Proteins

Glycosyltransferases

Polyisoprenyl Phosphates

Oxidation-Reduction

Acetyltransferases

DNA Nucleotidyltransferases

Sulfurtransferases

Recombinant Proteins

Models, Molecular

Hexosyltransferases

Pentosyltransferases

Protein Binding

Hydrogen-Ion Concentration

Acetates

Chromatography, High Pressure Liquid

UTP-Hexose-1-Phosphate Uridylyltransferase

Pyridoxal Phosphate

Molecular Weight

Hydroxymethylglutaryl-CoA-Reductases, NADP-dependent

Methylmalonyl-CoA Mutase

Glutathione

Simvastatin

Genes, Bacterial

Acetylglucosamine