3 methyl 2 oxobutanoate dehydrogenase lipoamide. Medical search

A ketone oxidoreductase that catalyzes the overall conversion of alpha-keto acids to ACYL-CoA and CO2. The enzyme requires THIAMINE DIPHOSPHATE as a cofactor. Defects in genes that code for subunits of the enzyme are a cause of MAPLE SYRUP URINE DISEASE. The enzyme was formerly classified as EC 1.2.4.3.

A flavoprotein containing oxidoreductase that catalyzes the reduction of lipoamide by NADH to yield dihydrolipoamide and NAD+. The enzyme is a component of several MULTIENZYME COMPLEXES.

Salts and derivatives of acetoacetic acid.

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

Benzene derivatives which are substituted with two nitro groups in the ortho, meta or para positions.

Compounds of the general formula R:N.NR2, as resulting from the action of hydrazines with aldehydes or ketones. (Grant & Hackh's Chemical Dictionary, 5th ed)

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 tetrameric enzyme that, along with the coenzyme NAD+, catalyzes the interconversion of LACTATE and PYRUVATE. In vertebrates, genes for three different subunits (LDH-A, LDH-B and LDH-C) exist.

An octanoic acid bridged with two sulfurs so that it is sometimes also called a pentanoic acid in some naming schemes. It is biosynthesized by cleavage of LINOLEIC ACID and is a coenzyme of oxoglutarate dehydrogenase (KETOGLUTARATE DEHYDROGENASE COMPLEX). It is used in DIETARY SUPPLEMENTS.

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.

A PYRIDOXAL PHOSPHATE dependent enzyme that catalyzes the decarboxylation of GLYCINE with the transfer of an aminomethyl group to the LIPOIC ACID moiety of the GLYCINE DECARBOXYLASE COMPLEX H-PROTEIN. Defects in P-protein are the cause of non-ketotic hyperglycinemia. It is one of four subunits of the glycine decarboxylase complex.

The E1 component of the multienzyme PYRUVATE DEHYDROGENASE COMPLEX. It is composed of 2 alpha subunits (pyruvate dehydrogenase E1 alpha subunit) and 2 beta subunits (pyruvate dehydrogenase E1 beta subunit).

Enzymes that catalyze the dehydrogenation of GLYCERALDEHYDE 3-PHOSPHATE. Several types of glyceraldehyde-3-phosphate-dehydrogenase exist including phosphorylating and non-phosphorylating varieties and ones that transfer hydrogen to NADP and ones that transfer hydrogen to NAD.

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)

A enzyme complex that catalyzes the oxidative DECARBOXYLATION and DEAMINATION of GLYCINE into CARBON DIOXIDE; AMMONIA; NADH; and N5N10-methylenetetrahydrofolate. It is composed of four different component protein components referred to as H, P, L, and T.

An enzyme that oxidizes an aldehyde in the presence of NAD+ and water to an acid and NADH. This enzyme was formerly classified as EC 1.1.1.70.

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.

An enzyme that catalyzes the conversion of (S)-malate and NAD+ to oxaloacetate and NADH. EC 1.1.1.37.

An enzyme of the oxidoreductase class that catalyzes the conversion of isocitrate and NAD+ to yield 2-ketoglutarate, carbon dioxide, and NADH. It occurs in cell mitochondria. The enzyme requires Mg2+, Mn2+; it is activated by ADP, citrate, and Ca2+, and inhibited by NADH, NADPH, and ATP. The reaction is the key rate-limiting step of the citric acid (tricarboxylic) cycle. (From Dorland, 27th ed) (The NADP+ enzyme is EC 1.1.1.42.) EC 1.1.1.41.

Oxidoreductases that are specific for KETONES.

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).

Reversibly catalyze the oxidation of a hydroxyl group of carbohydrates to form a keto sugar, aldehyde or lactone. Any acceptor except molecular oxygen is permitted. Includes EC 1.1.1.; EC 1.1.2.; and 1.1.99.

A flavoprotein containing oxidoreductase that catalyzes the dehydrogenation of SUCCINATE to fumarate. In most eukaryotic organisms this enzyme is a component of mitochondrial electron transport complex II.

An alcohol oxidoreductase which catalyzes the oxidation of L-iditol to L-sorbose in the presence of NAD. It also acts on D-glucitol to form D-fructose. It also acts on other closely related sugar alcohols to form the corresponding sugar. EC 1.1.1.14

A multienzyme complex responsible for the formation of ACETYL COENZYME A from pyruvate. The enzyme components are PYRUVATE DEHYDROGENASE (LIPOAMIDE); dihydrolipoamide acetyltransferase; and LIPOAMIDE DEHYDROGENASE. Pyruvate dehydrogenase complex is subject to three types of control: inhibited by acetyl-CoA and NADH; influenced by the energy state of the cell; and inhibited when a specific serine residue in the pyruvate decarboxylase is phosphorylated by ATP. PYRUVATE DEHYDROGENASE (LIPOAMIDE)-PHOSPHATASE catalyzes reactivation of the complex. (From Concise Encyclopedia Biochemistry and Molecular Biology, 3rd ed)

A LIPOIC ACID-containing protein that plays the pivotal role in the transfer of methylamine groups and reducing equivalents between the three enzymatic components of the glycine decarboxylase complex.

The rate dynamics in chemical or physical systems.

Enzymes of the oxidoreductase class that catalyze the dehydrogenation of hydroxysteroids. (From Enzyme Nomenclature, 1992) EC 1.1.-.

A glucose dehydrogenase that catalyzes the oxidation of beta-D-glucose to form D-glucono-1,5-lactone, using NAD as well as NADP as a coenzyme.

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)

Catalyzes the oxidation of GLUTATHIONE to GLUTATHIONE DISULFIDE in the presence of NADP+. Deficiency in the enzyme is associated with HEMOLYTIC ANEMIA. Formerly listed as EC 1.6.4.2.

Oxidoreductases that are specific for ALDEHYDES.

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).

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.

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)

D-Glucose:1-oxidoreductases. Catalyzes the oxidation of D-glucose to D-glucono-gamma-lactone and reduced acceptor. Any acceptor except molecular oxygen is permitted. Includes EC 1.1.1.47; EC 1.1.1.118; EC 1.1.1.119 and EC 1.1.99.10.

Catalyze the oxidation of 3-hydroxysteroids to 3-ketosteroids.

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)

An enzyme of the oxidoreductase class that catalyzes the reaction 6-phospho-D-gluconate and NADP+ to yield D-ribulose 5-phosphate, carbon dioxide, and NADPH. The reaction is a step in the pentose phosphate pathway of glucose metabolism. (From Dorland, 27th ed) EC 1.1.1.43.

Reversibly catalyzes the oxidation of a hydroxyl group of sugar alcohols to form a keto sugar, aldehyde or lactone. Any acceptor except molecular oxygen is permitted. Includes EC 1.1.1.; EC 1.1.2. and EC 1.1.99.

Enzymes that catalyze the first step in the beta-oxidation of FATTY ACIDS.

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.

A genus of gram-negative, aerobic bacteria found in soil and water. Its organisms occur singly, in pairs or irregular clumps, and sometimes in chains of varying lengths.

A flavoprotein and iron sulfur-containing oxidoreductase that catalyzes the oxidation of NADH to NAD. In eukaryotes the enzyme can be found as a component of mitochondrial electron transport complex I. Under experimental conditions the enzyme can use CYTOCHROME C GROUP as the reducing cofactor. The enzyme was formerly listed as EC 1.6.2.1.

An enzyme that catalyzes the dehydrogenation of inosine 5'-phosphate to xanthosine 5'-phosphate in the presence of NAD. EC 1.1.1.205.

Alcohol oxidoreductases with substrate specificity for LACTIC ACID.

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.

Flavoproteins that catalyze reversibly the reduction of carbon dioxide to formate. Many compounds can act as acceptors, but the only physiologically active acceptor is NAD. The enzymes are active in the fermentation of sugars and other compounds to carbon dioxide and are the key enzymes in obtaining energy when bacteria are grown on formate as the main carbon source. They have been purified from bovine blood. EC 1.2.1.2.

A class of enzymes that catalyzes the oxidation of 17-hydroxysteroids to 17-ketosteroids. EC 1.1.-.

A flavoprotein oxidoreductase that has specificity for medium-chain fatty acids. It forms a complex with ELECTRON TRANSFERRING FLAVOPROTEINS and conveys reducing equivalents to UBIQUINONE.

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.

A class of enzymes that catalyze oxidation-reduction reactions of amino acids.

An enzyme that catalyzes the acetyltransferase reaction using ACETYL CoA as an acetyl donor and dihydrolipoamide as acceptor to produce COENZYME A (CoA) and S-acetyldihydrolipoamide. It forms the (E2) subunit of the PYRUVATE DEHYDROGENASE COMPLEX.

An enzyme that catalyzes the oxidation of XANTHINE in the presence of NAD+ to form URIC ACID and NADH. It acts also on a variety of other purines and aldehydes.

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 one-carbon group transferase that transfers lipoamide-linked methylamine groups to tetrahydrofolate (TETRAHYDROFOLATES) to form methylenetetrahydrofolate and AMMONIA. It is one of four components of the glycine decarboxylase complex.

A species of gram-negative, aerobic bacteria first isolated from soil in Vineland, New Jersey. Ammonium and nitrate are used as nitrogen sources by this bacterium. It is distinguished from other members of its genus by the ability to use rhamnose as a carbon source. (From Bergey's Manual of Determinative Bacteriology, 9th ed)

Enzymes that reversibly catalyze the oxidation of a 3-hydroxyacyl CoA to 3-ketoacyl CoA in the presence of NAD. They are key enzymes in the oxidation of fatty acids and in mitochondrial fatty acid synthesis.

Hydroxysteroid dehydrogenases that catalyzes the reversible conversion of CORTISOL to the inactive metabolite CORTISONE. Enzymes in this class can utilize either NAD or NADP as cofactors.

Any of various animals that constitute the family Suidae and comprise stout-bodied, short-legged omnivorous mammals with thick skin, usually covered with coarse bristles, a rather long mobile snout, and small tail. Included are the genera Babyrousa, Phacochoerus (wart hogs), and Sus, the latter containing the domestic pig (see SUS SCROFA).

(Pyruvate dehydrogenase (lipoamide))-phosphate phosphohydrolase. A mitochondrial enzyme that catalyzes the hydrolytic removal of a phosphate on a specific seryl hydroxyl group of pyruvate dehydrogenase, reactivating the enzyme complex. EC 3.1.3.43.

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

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

An oxidoreductase involved in pyrimidine base degradation. It catalyzes the catabolism of THYMINE; URACIL and the chemotherapeutic drug, 5-FLUOROURACIL.

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)

An enzyme that catalyzes the oxidation of UDPglucose to UDPglucuronate in the presence of NAD+. EC 1.1.1.22.

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

A disease-producing enzyme deficiency subject to many variants, some of which cause a deficiency of GLUCOSE-6-PHOSPHATE DEHYDROGENASE activity in erythrocytes, leading to hemolytic anemia.

A low-affinity 11 beta-hydroxysteroid dehydrogenase found in a variety of tissues, most notably in LIVER; LUNG; ADIPOSE TISSUE; vascular tissue; OVARY; and the CENTRAL NERVOUS SYSTEM. The enzyme acts reversibly and can use either NAD or NADP as cofactors.

An NAD-dependent enzyme that catalyzes the reversible DEAMINATION of L-ALANINE to PYRUVATE and AMMONIA. The enzyme is needed for growth when ALANINE is the sole CARBON or NITROGEN source. It may also play a role in CELL WALL synthesis because L-ALANINE is an important constituent of the PEPTIDOGLYCAN layer.

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 3-hydroxysteroid dehydrogenase which catalyzes the reversible reduction of the active androgen, DIHYDROTESTOSTERONE to 5 ALPHA-ANDROSTANE-3 ALPHA,17 BETA-DIOL. It also has activity towards other 3-alpha-hydroxysteroids and on 9-, 11- and 15- hydroxyprostaglandins. The enzyme is B-specific in reference to the orientation of reduced NAD or NADPH.

Sugar alcohol dehydrogenases that have specificity for MANNITOL. Enzymes in this category are generally classified according to their preference for a specific reducing cofactor.

A genus of gram-negative, aerobic, rod-shaped bacteria widely distributed in nature. Some species are pathogenic for humans, animals, and plants.

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)

Catalyzes reversibly the oxidation of hydroxyl groups of prostaglandins.

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

A flavoprotein oxidoreductase that has specificity for short-chain fatty acids. It forms a complex with ELECTRON-TRANSFERRING FLAVOPROTEINS and conveys reducing equivalents to UBIQUINONE.

A metalloflavoprotein enzyme involved the metabolism of VITAMIN A, this enzyme catalyzes the oxidation of RETINAL to RETINOIC ACID, using both NAD+ and FAD coenzymes. It also acts on both the 11-trans- and 13-cis-forms of RETINAL.

Dithionite. The dithionous acid ion and its salts.

A genus of gram-positive, rod-shaped bacteria found in cavities of man and animals, animal and plant products, infections of soft tissue, and soil. Some species may be pathogenic. No endospores are produced. The genus Eubacterium should not be confused with EUBACTERIA, one of the three domains of life.

A group of enzymes that catalyze the reversible reduction-oxidation reaction of 20-hydroxysteroids, such as from a 20-ketosteroid to a 20-alpha-hydroxysteroid (EC 1.1.1.149) or to a 20-beta-hydroxysteroid (EC 1.1.1.53).

The coenzyme form of Vitamin B1 present in many animal tissues. It is a required intermediate in the PYRUVATE DEHYDROGENASE COMPLEX and the KETOGLUTARATE DEHYDROGENASE COMPLEX.

An high-affinity, NAD-dependent 11-beta-hydroxysteroid dehydrogenase that acts unidirectionally to catalyze the dehydrogenation of CORTISOL to CORTISONE. It is found predominantly in mineralocorticoid target tissues such as the KIDNEY; COLON; SWEAT GLANDS; and the PLACENTA. Absence of the enzyme leads to a fatal form of childhood hypertension termed, APPARENT MINERALOCORTICOID EXCESS SYNDROME.

A series of oxidative reactions in the breakdown of acetyl units derived from GLUCOSE; FATTY ACIDS; or AMINO ACIDS by means of tricarboxylic acid intermediates. The end products are CARBON DIOXIDE, water, and energy in the form of phosphate bonds.

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)

A non-selective inhibitor of nitric oxide synthase. It has been used experimentally to induce hypertension.

A flavoprotein oxidoreductase that has specificity for long-chain fatty acids. It forms a complex with ELECTRON-TRANSFERRING FLAVOPROTEINS and conveys reducing equivalents to UBIQUINONE.

The muscle tissue of the HEART. It is composed of striated, involuntary muscle cells (MYOCYTES, CARDIAC) connected to form the contractile pump to generate blood flow.

An enzyme that catalyzes the reduction of aspartic beta-semialdehyde to homoserine, which is the branch point in biosynthesis of methionine, lysine, threonine and leucine from aspartic acid. EC 1.1.1.3.

A mitochondrial flavoprotein, this enzyme catalyzes the oxidation of 3-methylbutanoyl-CoA to 3-methylbut-2-enoyl-CoA using FAD as a cofactor. Defects in the enzyme, is associated with isovaleric acidemia (IVA).

An NAD+ dependent enzyme that catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate to 3-carboxy-4-methyl-2-oxopentanoate. It is involved in the biosynthesis of VALINE; LEUCINE; and ISOLEUCINE.

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

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

An octameric enzyme belonging to the superfamily of amino acid dehydrogenases. Leucine dehydrogenase catalyzes the reversible oxidative deamination of L-LEUCINE, to 4-methyl-2-oxopentanoate (2-ketoisocaproate) and AMMONIA, with the corresponding reduction of the cofactor NAD+.

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).

A FLAVOPROTEIN enzyme that catalyzes the oxidation of THIOREDOXINS to thioredoxin disulfide in the presence of NADP+. It was formerly listed as EC 1.6.4.5

Enzymes that catalyze the oxidation of estradiol at the 17-hydroxyl group in the presence of NAD+ or NADP+ to yield estrone and NADH or NADPH. The 17-hydroxyl group can be in the alpha- or beta-configuration. EC 1.1.1.62

The functional hereditary units of BACTERIA.

An enzyme that catalyzes the oxidation of 3-phosphoglycerate to 3-phosphohydroxypyruvate. It takes part in the L-SERINE biosynthesis pathway.

The methyl homolog of parathion. An effective, but highly toxic, organothiophosphate insecticide and cholinesterase inhibitor.

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

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

Inorganic or organic compounds derived from phosphine (PH3) by the replacement of H atoms. (From Grant & Hackh's Chemical Dictionary, 5th ed)

An enzyme that plays a role in the GLUTAMATE and butanoate metabolism pathways by catalyzing the oxidation of succinate semialdehyde to SUCCINATE using NAD+ as a coenzyme. Deficiency of this enzyme, causes 4-hydroxybutyricaciduria, a rare inborn error in the metabolism of the neurotransmitter 4-aminobutyric acid (GABA).

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

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.

An NAD-dependent glyceraldehyde-3-phosphate dehydrogenase found in the cytosol of eucaryotes. It catalyses the dehydrogenation and phosphorylation of GLYCERALDEHYDE 3-PHOSPHATE to 3-phospho-D-glyceroyl phosphate, which is an important step in the GLYCOLYSIS pathway.

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

A subclass of enzymes which includes all dehydrogenases acting on carbon-carbon bonds. This enzyme group includes all the enzymes that introduce double bonds into substrates by direct dehydrogenation of carbon-carbon single bonds.

Measurement of the intensity and quality of fluorescence.

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.

An enzyme that catalyzes the conversion of prephenate to p-hydroxyphenylpyruvate in the presence of NAD. In the enteric bacteria, this enzyme also possesses chorismate mutase activity, thereby catalyzing the first two steps in the biosynthesis of tyrosine. EC 1.3.1.12.

A type of ion exchange chromatography using diethylaminoethyl cellulose (DEAE-CELLULOSE) as a positively charged resin. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)

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.

An enzyme that catalyzes the oxidation of 1-pyrroline-5-carboxylate to L-GLUTAMATE in the presence of NAD. Defects in the enzyme are the cause of hyperprolinemia II.

Proteins prepared by recombinant DNA technology.

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

An alkylating agent in cancer therapy that may also act as a mutagen by interfering with and causing damage to DNA.

Enzymes catalyzing the dehydrogenation of secondary amines, introducing a C=N double bond as the primary reaction. In some cases this is later hydrolyzed.

A flavoprotein enzyme that is responsible for the catabolism of LYSINE; HYDROXYLYSINE; and TRYPTOPHAN. It catalyzes the oxidation of GLUTARYL-CoA to crotonoyl-CoA using FAD as a cofactor. Glutaric aciduria type I is an inborn error of metabolism due to the deficiency of glutaryl-CoA dehydrogenase.

A family of compounds containing an oxo group with the general structure of 1,5-pentanedioic acid. (From Lehninger, Principles of Biochemistry, 1982, p442)

Compounds containing the -SH radical.

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

An enzymes that catalyzes the reversible reduction-oxidation reaction of 20-alpha-hydroxysteroids, such as from PROGESTERONE to 20-ALPHA-DIHYDROPROGESTERONE.

A variable annual leguminous vine (Pisum sativum) that is cultivated for its rounded smooth or wrinkled edible protein-rich seeds, the seed of the pea, and the immature pods with their included seeds. (From Webster's New Collegiate Dictionary, 1973)

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.

Use of restriction endonucleases to analyze and generate a physical map of genomes, genes, or other segments of DNA.

A colorless, flammable liquid used in the manufacture of acetic acid, perfumes, and flavors. It is also an intermediate in the metabolism of alcohol. It has a general narcotic action and also causes irritation of mucous membranes. Large doses may cause death from respiratory paralysis.

A species of nonpathogenic fluorescent bacteria found in feces, sewage, soil, and water, and which liquefy gelatin.

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

Amine oxidoreductases that use either NAD+ (EC 1.5.1.7) or NADP+ (EC 1.5.1.8) as an acceptor to form L-LYSINE or NAD+ (EC 1.5.1.9) or NADP+ (EC 1.5.1.10) as an acceptor to form L-GLUTAMATE. Deficiency of this enzyme causes HYPERLYSINEMIAS.

D-Galactose:NAD(P)+ 1-oxidoreductases. Catalyzes the oxidation of D-galactose in the presence of NAD+ or NADP+ to D-galactono-gamma-lactone and NADH or NADPH. Includes EC 1.1.1.48 and EC 1.1.1.120.

A species of gram-negative, aerobic bacteria isolated from soil and water as well as clinical specimens. Occasionally it is an opportunistic pathogen.

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

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

A FLAVOPROTEIN enzyme that catalyzes the oxidative demethylation of dimethylglycine to SARCOSINE and FORMALDEHYDE.

An enzyme that catalyzes the conversion of L-aspartate 4-semialdehyde, orthophosphate, and NADP+ to yield L-4-aspartyl phosphate and NADPH. EC 1.2.1.11.

An NAD+ dependent enzyme that catalyzes the oxidation of betain aldehyde to BETAINE.

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

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.

Hydrocarbon rings which contain two ketone moieties in any position. They can be substituted in any position except at the ketone groups.

Chemical groups containing the covalent disulfide bonds -S-S-. The sulfur atoms can be bound to inorganic or organic moieties.

A hydrocarbon used as an industrial solvent. It has been used as an aerosal propellent, as a refrigerant and as a local anesthetic. (From Martindale, The Extra Pharmacopoeia, 31st ed, p1403)

The rate at which oxygen is used by a tissue; microliters of oxygen STPD used per milligram of tissue per hour; the rate at which oxygen enters the blood from alveolar gas, equal in the steady state to the consumption of oxygen by tissue metabolism throughout the body. (Stedman, 25th ed, p346)

A category of nucleic acid sequences that function as units of heredity and which code for the basic instructions for the development, reproduction, and maintenance of organisms.

A colorless, flammable liquid used in the manufacture of FORMALDEHYDE and ACETIC ACID, in chemical synthesis, antifreeze, and as a solvent. Ingestion of methanol is toxic and may cause blindness.

Mitochondria in hepatocytes. As in all mitochondria, there are an outer membrane and an inner membrane, together creating two separate mitochondrial compartments: the internal matrix space and a much narrower intermembrane space. In the liver mitochondrion, an estimated 67% of the total mitochondrial proteins is located in the matrix. (From Alberts et al., Molecular Biology of the Cell, 2d ed, p343-4)

Organic compounds containing a carbonyl group in the form -CHO.

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

An inherited metabolic disorder caused by deficient enzyme activity in the PYRUVATE DEHYDROGENASE COMPLEX, resulting in deficiency of acetyl CoA and reduced synthesis of acetylcholine. Two clinical forms are recognized: neonatal and juvenile. The neonatal form is a relatively common cause of lactic acidosis in the first weeks of life and may also feature an erythematous rash. The juvenile form presents with lactic acidosis, alopecia, intermittent ATAXIA; SEIZURES; and an erythematous rash. (From J Inherit Metab Dis 1996;19(4):452-62) Autosomal recessive and X-linked forms are caused by mutations in the genes for the three different enzyme components of this multisubunit pyruvate dehydrogenase complex. One of the mutations at Xp22.2-p22.1 in the gene for the E1 alpha component of the complex leads to LEIGH DISEASE.

Deoxyribonucleic acid that makes up the genetic material of bacteria.

Derivatives of formic acids. Included under this heading are a broad variety of acid forms, salts, esters, and amides that are formed with a single carbon carboxy group.

A pyrrolo-quinoline having two adjacent keto-groups at the 4 and 5 positions and three acidic carboxyl groups. It is a coenzyme of some DEHYDROGENASES.

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.

An enzyme that catalyzes the interconversion of a ketone and hydroxy group at C-20 of cortisone and other 17,20,21-trihydroxy steroids. EC 1.1.1.53.

The first enzyme of the proline degradative pathway. It catalyzes the oxidation of proline to pyrroline-5-carboxylic acid in the presence of oxygen and water. The action is not reversible. The specific activity of proline oxidase increases with age. EC 1.5.3.-.

A primary source of energy for living organisms. It is naturally occurring and is found in fruits and other parts of plants in its free state. It is used therapeutically in fluid and nutrient replacement.

A family of iminourea derivatives. The parent compound has been isolated from mushrooms, corn germ, rice hulls, mussels, earthworms, and turnip juice. Derivatives may have antiviral and antifungal properties.

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

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.

An enzyme that plays a role in the VALINE; LEUCINE; and ISOLEUCINE catabolic pathways by catalyzing the oxidation of 2-methyl-3-oxopropanate to propanoyl-CoA using NAD+ as a coenzyme. Methylmalonate semialdehyde dehydrogenase deficiency is characterized by elevated BETA-ALANINE and 3-hydropropionic acid.

Plants whose roots, leaves, seeds, bark, or other constituent parts possess therapeutic, tonic, purgative, curative or other pharmacologic attributes, when administered to man or animals.

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 branched-chain essential amino acid that has stimulant activity. It promotes muscle growth and tissue repair. It is a precursor in the penicillin biosynthetic pathway.

Proteins found in any species of bacterium.

A bifunctional protein consisting of aspartokinase, and homoserine dehydrogenase activities. It is found primarily in BACTERIA and in PLANTS.

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

An intermediate compound in the metabolism of carbohydrates, proteins, and fats. In thiamine deficiency, its oxidation is retarded and it accumulates in the tissues, especially in nervous structures. (From Stedman, 26th ed)

The composition, conformation, and properties of atoms and molecules, and their reaction and interaction processes.

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

Enzyme that catalyzes the first step of the tricarboxylic acid cycle (CITRIC ACID CYCLE). It catalyzes the reaction of oxaloacetate and acetyl CoA to form citrate and coenzyme A. This enzyme was formerly listed as EC 4.1.3.7.

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.

A clear, colorless liquid rapidly absorbed from the gastrointestinal tract and distributed throughout the body. It has bactericidal activity and is used often as a topical disinfectant. It is widely used as a solvent and preservative in pharmaceutical preparations as well as serving as the primary ingredient in ALCOHOLIC BEVERAGES.

Alkyl compounds containing a hydroxyl group. They are classified according to relation of the carbon atom: primary alcohols, R-CH2OH; secondary alcohols, R2-CHOH; tertiary alcohols, R3-COH. (From Grant & Hackh's Chemical Dictionary, 5th ed)

A flavoprotein that reversibly oxidizes NADPH to NADP and a reduced acceptor. EC 1.6.99.1.

An enzyme that catalyzes the conversion of acetoin to diacetyl in the presence of NAD.

A LIVER mitochondrial matrix flavoenzyme that catalyzes the oxidation of SARCOSINE to GLYCINE and FORMALDEHYDE. Mutation in the enzyme causes sarcosinemia, a rare autosomal metabolic defect characterized by elevated levels of SARCOSINE in BLOOD and URINE.

A metabolic process that converts GLUCOSE into two molecules of PYRUVIC ACID through a series of enzymatic reactions. Energy generated by this process is conserved in two molecules of ATP. Glycolysis is the universal catabolic pathway for glucose, free glucose, or glucose derived from complex CARBOHYDRATES, such as GLYCOGEN and STARCH.

A carbamate derivative used as an alcohol deterrent. It is a relatively nontoxic substance when administered alone, but markedly alters the intermediary metabolism of alcohol. When alcohol is ingested after administration of disulfiram, blood acetaldehyde concentrations are increased, followed by flushing, systemic vasodilation, respiratory difficulties, nausea, hypotension, and other symptoms (acetaldehyde syndrome). It acts by inhibiting aldehyde dehydrogenase.

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 sequence of successive nucleotide triplets that are read as CODONS specifying AMINO ACIDS and begin with an INITIATOR CODON and end with a stop codon (CODON, TERMINATOR).

Amino-substituted glyoxylic acid derivative.

... lipoamide)]-phosphate phosphohydrolase) is an enzyme with systematic name (3-methyl-2-oxobutanoate dehydrogenase (2- ... Reed LJ, Damuni Z, Merryfield ML (1985). "Regulation of mammalian pyruvate and branched-chain α-keto acid dehydrogenase ... branched-chain oxo-acid dehydrogenase phosphatase, branched-chain 2-keto acid dehydrogenase phosphatase, branched-chain α-keto ... "Dephosphorylation and reactivation of phosphorylated purified ox-kidney branched-chain dehydrogenase complex by co-purified ...

https://en.wikipedia.org/wiki/(3-methyl-2-oxobutanoate_dehydrogenase_(2-methylpropanoyl-transferring))-phosphatase

... pyruvate dehydrogenase (lipoamide)-phosphatase MeSH D08.811.277.352.650.700 - 6-phytase MeSH D08.811.277.352.650.850 - pten ... malate dehydrogenase MeSH D08.811.682.047.748 - malate dehydrogenase (nadp+) MeSH D08.811.682.047.892 - xanthine dehydrogenase ... acetoin dehydrogenase MeSH D08.811.682.047.070 - alcohol dehydrogenase MeSH D08.811.682.047.150 - carbohydrate dehydrogenases ... pyruvate dehydrogenase (lipoamide) MeSH D08.811.682.657.350.937 - pyruvate oxidase MeSH D08.811.682.657.350.968 - pyruvate ...

https://en.wikipedia.org/wiki/List_of_MeSH_codes_(D08)

Pyruvate dehydrogenase (lipoamide) [D08.811.682.657.350.875] Pyruvate dehydrogenase (lipoamide) * Pyruvate oxidase [D08.811. ... 3-Methyl-2-oxobutanoate dehydrogenase (lipoamide) - Concept préféré Concept UI. M0077442. Terme préféré. 3-Methyl-2- ... oxobutanoate dehydrogenase (lipoamide) Synonymes. 2-Oxoisovalérate déshydrogénase (lipoamide) 3-Méthyl-2-oxobutanoate ... 3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide) Descripteur en espagnol: 3-Metil-2-Oxobutanoato Deshidrogenasa (Lipoamida) ...

https://decs.bvsalud.org/fr/ths/resource/?id=38207

... lipoamide)] kinase Active Synonym false false 209561015 Branched-chain alpha-ketoacid dehydrogenase kinase Active Synonym false ... lipoamide) kinase (substance). Code System Preferred Concept Name. 3-methyl-2-oxobutanoate dehydrogenase (lipoamide) kinase ( ...

https://phinvads.cdc.gov/vads/ViewCodeSystemConcept.action?oid=2.16.840.1.113883.6.96&code=130417002

mitochondrial pyruvate dehydrogenase (lipoamide) phosphatase complex GO:0019910 * Atg12-Atg5-Atg16 complex ...

https://bio2vec.cbrc.kaust.edu.sa/bio2vec/details/1?iri=GO:0042719

Decanoyl CoA Dehydrogenase use Acyl-CoA Dehydrogenase, Long-Chain Decanoyl CoA-Dehydrogenase use Acyl-CoA Dehydrogenase, Long- ... Dalf use Methyl Parathion Dalfampridine use 4-Aminopyridine Dall Porpoise use Porpoises ... Lipoamide) Decarboxylase, Dopa use Dopa Decarboxylase ... D Amino Acid Dehydrogenase use D-Amino-Acid Oxidase D Amino ... D-beta-Hydroxybutyrate Dehydrogenase use Hydroxybutyrate Dehydrogenase D-D Carboxypeptidase use Serine-Type D-Ala-D-Ala ...

https://decs.bvs.br/I/DeCS2018_Alfab-D.htm

https://decs2020.bvsalud.org/I/DeCS2020_Alfab-D.htm

https://decs2019.bvsalud.org/I/DeCS2019_Alfab-D.htm

Decanoyl CoA Dehydrogenase use Acyl-CoA Dehydrogenase, Long-Chain Decanoyl CoA-Dehydrogenase use Acyl-CoA Dehydrogenase, Long- ... Dalf use Methyl Parathion Dall Porpoise use Porpoises Dall Sheep use Sheep ... Lipoamide) Decarboxylase, Dopa use Dopa Decarboxylase ... D Amino Acid Dehydrogenase use D-Amino-Acid Oxidase D Amino ... D-beta-Hydroxybutyrate Dehydrogenase use Hydroxybutyrate Dehydrogenase D-D Carboxypeptidase use Serine-Type D-Ala-D-Ala ...

https://decs2017.bvsalud.org/I/DeCS2017_Alfab-D.htm

https://decs2018.bvsalud.org/I/DeCS2018_Alfab-D.htm

Acyl-CoA Dehydrogenase. Acil-CoA Deshidrogenasa. Acil-CoA Desidrogenase de Cadeia Longa. Acyl-CoA Dehydrogenase, Long-Chain. ... Lipoamide). 3-Metil-2-Oxobutanoato Deshidrogenasa (Lipoamida). ... Acyl-CoA Dehydrogenases. Acil-CoA Deshidrogenasas. Acil-CoA ... Dihydrouracil Dehydrogenase (NADP). Dihidrouracilo Deshidrogenasa (NADP). Endo-1,3(4)-beta-Glucanase. Endo-1,3(4)-beta- ... Glucose 1-Dehydrogenase. Glucosa 1-Deshidrogenasa. Glutamato Carboxipeptidase II. Glutamate Carboxypeptidase II. Glutamato ...

https://decs2011.bvsalud.org/P/new_2004.htm

Acyl-CoA Dehydrogenase. Acil-CoA Desidrogenase. Acil-CoA Deshidrogenasa de Cadena Larga. Acyl-CoA Dehydrogenase, Long-Chain. ... Lipoamide). 3-Metil-2-Oxobutanoato Desidrogenase (Lipoamida). ... Acyl-CoA Dehydrogenases. Acil-CoA Desidrogenases. Acil-CoA ... Dihydrouracil Dehydrogenase (NADP). Diidrouracila Desidrogenase (NADP). Endo-1,3(4)-beta-Glucanasa. Endo-1,3(4)-beta-Glucanase ... Glucose 1-Dehydrogenase. Glucose 1-Desidrogenase. Glutamato Carboxipeptidasa II. Glutamate Carboxypeptidase II. Glutamato ...

https://decs2008.bvsalud.org/E/new_2004.htm

https://decs2012.bvsalud.org/E/new_2004.htm

https://decs2010.bvsalud.org/E/new_2004.htm

https://decs2016.bvsalud.org/P/new_2004.htm

https://decs2009.bvsalud.org/P/new_2004.htm

Acyl-CoA Dehydrogenase. Acil-CoA Desidrogenase. Acil-CoA Deshidrogenasa. Acyl-CoA Dehydrogenase, Long-Chain. Acil-CoA ... Lipoamide). 3-Metil-2-Oxobutanoato Desidrogenase (Lipoamida). 3-Metil-2-Oxobutanoato Deshidrogenasa (Lipoamida). ... Acyl-CoA Dehydrogenases. Acil-CoA Desidrogenases. Acil-CoA Deshidrogenasas. Acyl-CoA Oxidase. Acil-CoA Oxidase. Acil-CoA ... Butyryl-CoA Dehydrogenase. Butiril-CoA Desidrogenase. Butiril-CoA Deshidrogenasa. CDC2-CDC28 Kinases. CDC2-CDC28 Quinases. ...

https://decs2015.bvsalud.org/I/new_2004.htm

https://decs2013.bvsalud.org/E/new_2004.htm

https://decs2014.bvsalud.org/E/new_2004.htm

https://decs2007.bvsalud.org/I/new_2004.htm

https://metacrop.ipk-gatersleben.de/apex/f?p=269:9:::NO::P9_SUBSTANCE_ID:1020

Pyruvate dehydrogenase (lipoamide). 2-oxoisovalerate dehydrogenase subunit alpha; Branched-chain alpha-keto acid dehydrogenase ... 1 candidates for bkdA: branched-chain alpha-ketoacid dehydrogenase, E1 component alpha subunit. Score. Gene. Description. ... TPP-dependent acetoin dehydrogenase complex, E1 component, alpha subunit; EC 1.1.1.-. 41%. 262.3. ... branched-chain α-keto acid dehydrogenase E1 component α subunit (EC 1.2.4.4) ...

https://papers.genomics.lbl.gov/cgi-bin/gapView.cgi?orgs=orgsFit&set=carbon&orgId=FitnessBrowser__SynE&path=leucine&step=bkdA

... "alpha-ketoglutarate dehydrogenase, tricarboxylic acid cycle*, oxoglutarate dehydrogenase (lipoamide), mitochondrial matrix" ... "carboxy methyl transferase; homolog of PPM1, protein modification," YGL032C 2.404126 INESSENTIAL AGA2 "adhesion subunit of a- ... "alpha subunit of pyruvate dehydrogenase (E1 alpha),pyruvate dehydrogenase (lipoamide), " YOR265W 0.71321 INESSENTIAL RBL2 "beta ... "dihydrolipoamide dehydrogenase precursor (mature protein is the E3 component of alpha-ketoacid dehydrogenase complexes), serine ...

https://genomics.lbl.gov/YeastFitnessData/websitefiles/ratioresults/thrRatio_07.txt

... lipoamide]] kinase, mitochondrial. BRSK1. Serine/threonine-protein kinase BRSK1. ... Voltage-dependent calcium channel subunit alpha-2/delta-2. CACNA2D3. Voltage-dependent calcium channel subunit alpha-2/delta-3 ... Phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing subunit beta. PIK3C2G. Phosphatidylinositol 4-phosphate 3-kinase ... Dual specificity tyrosine-phosphorylation-regulated kinase 2. DYRK3. Dual specificity tyrosine-phosphorylation-regulated kinase ...

https://commonfund.nih.gov/idg/understudiedproteins

This gene encodes the E2 subunit of the branched-chain α-keto acid dehydrogenase (BCKDH) complex, a core component of branched- ... Lipoamide)/metabolism*; Amino Acids, Branched-Chain/metabolism*; Animals; Arsenic/toxicity*; Biological Variation, Population ...

https://tools.niehs.nih.gov/portfolio/index.cfm?do=portfolio.publicationDetail&id=3619736

... recessive inherited metabolic disorder caused by the deficient activity of the branched-chain α-keto acid dehydrogenase (BCKD) ... Lipoamide) / genetics Actions. * Search in PubMed * Search in MeSH ... Diana Ruffato Resende Campanholi 1 , Ana Vitoria Barban Margutti 1 , Wilson A Silva Jr 2 3 4 , Daniel F Garcia 2 3 , Greice A ... Diana Ruffato Resende Campanholi 1 , Ana Vitoria Barban Margutti 1 , Wilson A Silva Jr 2 3 4 , Daniel F Garcia 2 3 , Greice A ...

https://pubmed.ncbi.nlm.nih.gov/33955723/

Lipoamide) Alpha-Keto Acid Dehydrogenase BCKA Decarboxylase Branched Chain Alpha-Keto Acid Decarboxylase Branched Chain ... Branched-Chain Keto Acid Dehydrogenase Branched-Chain Oxo-Acid Dehydrogenase Registry Number. EC 1.2.4.4. Related Numbers. 9082 ... Branched Chain Ketoacid Dehydrogenase Term UI T107440. LexicalTag NON. ThesaurusID NLM (2004). ... Alpha-Keto Acid Dehydrogenase Term UI T107437. LexicalTag NON. ThesaurusID NLM (2004). ...

https://meshb.nlm.nih.gov/record/ui?ui=D042942

https://meshb-prev.nlm.nih.gov/record/ui?ui=D042942

... lipoamide)]-phosphatase Current Synonym true false 209707015 Branched-chain oxo-acid dehydrogenase phosphatase Current Synonym ... lipoamide)-phosphatase (substance). Code System Preferred Concept Name. 3-methyl-2-oxobutanoate dehydrogenase (lipoamide)- ...

https://phinvads.cdc.gov/vads/ViewCodeSystemConcept.action?oid=2.16.840.1.113883.6.96&code=130506001

We tested if expression of the mitochondrial BCAA oxidation checkpoint, branched-chain α-ketoacid dehydrogenase (BCKD) complex ... Lipoamide) Medicine & Life Sciences 36% * Insulin Resistance Medicine & Life Sciences 18% ... We tested if expression of the mitochondrial BCAA oxidation checkpoint, branched-chain α-ketoacid dehydrogenase (BCKD) complex ... We tested if expression of the mitochondrial BCAA oxidation checkpoint, branched-chain α-ketoacid dehydrogenase (BCKD) complex ...

https://ucdavis.pure.elsevier.com/en/publications/regulation-of-adipose-branched-chain-amino-acid-catabolism-enzyme

The branched-chain alpha-ketoacid dehydrogenase complex (BCKD) is an important regulator of the valine, leucine, and isoleucine ... Catalyzes the phosphorylation and inactivation of the branched-chain alpha-ketoacid dehydrogenase complex, the key regulatory ... Lipoamide]] Kinase, Mitochondrial. DTO Classes. Protein. / Kinase. / Protein Kinase. / Atypical Group. / Pdhk Family. / [3- ... methyl-2-oxobutanoate Dehydrogenase [Lipoamide]] Kinase, Mitochondrial. IDG Development Level Summary. help help. ...

https://pharos.ncats.nih.gov/targets/BCKDK

https://pharos.nih.gov/targets/BCKDK

Lipoamide);Enzyme Activation;Interleukin-1;Cytokines;Muscle, Skeletal;Tumor Necrosis Factor-alpha;Rats, Wistar;Models, Animal; ... or interleukin 1 to rats activates skeletal muscle branched-chain a-keto acid dehydrogenase ... Lipoamide);Enzyme Activation;Interleukin-1;Cytokines;Muscle, Skeletal;Tumor Necrosis Factor-alpha;Rats, Wistar;Models, Animal; ... or interleukin 1 to rats activates skeletal muscle branched-chain a-keto acid dehydrogenase ...

http://digital.library.musc.edu/cdm/search/searchterm/mg%252Fkg

... lipoamide]] kinase, publication title Structures of branched-chain alpha-ketoacid dehydrogenase kinase-inhibitor complexes rcsb ... Alpha-ketoacid/pyruvate dehydrogenase kinase, N-terminal domain. 4dzyA01. 3.30.565.10. Alpha Beta. 2-Layer Sandwich. Heat Shock ... Crystal structure of branched-chain alpha-ketoacid dehydrogenase kinase/(s)-2-chloro-3-phenylpropanoic acid complex with adp ...

https://genus.fuw.edu.pl/view/4DZY/A/

mitochondrial pyruvate dehydrogenase (lipoamide) phosphatase complex GO:0019910 * no_name DOID:8434 ... synaptotagmin-synaptobrevin 2-SNAP-25-syntaxin-1a-syntaxin-1b-Rab3a-complexin II complex ...

https://bio2vec.cbrc.kaust.edu.sa/bio2vec/details/1?iri=GO:0030390

http://digital.library.musc.edu/cdm/search/searchterm/interleukin-1

Lipoamide) N0000167644 Pyruvate Dehydrogenase (Lipoamide)-Phosphatase N0000167744 Pyruvate Dehydrogenase Complex N0000168216 ... Methyl Ethers N0000166537 Methyl Green N0000166483 Methyl Methanesulfonate N0000166799 Methyl n-Butyl Ketone N0000166451 Methyl ... H Dehydrogenase (Quinone) N0000168358 NAD+ Nucleosidase N0000169644 NADH Dehydrogenase N0000167808 NADH Tetrazolium Reductase ... N0000167885 Methylenetetrahydrofolate Dehydrogenase (NAD+) N0000167878 Methylenetetrahydrofolate Dehydrogenase (NADP) ...

https://evs.nci.nih.gov/ftp1/FDA/ndfrt/Archive/StructuralClass%202012-06-04.txt

Lipoamide) Medicine & Life Sciences 100% * Thiamine Pyrophosphate Medicine & Life Sciences 95% ... Danner, D. J., Lemmon, S. K., & Elsas, L. J. (1980). Stabilization of mammalian liver branched-chain α-ketoacid dehydrogenase ... Danner, DJ, Lemmon, SK & Elsas, LJ 1980, Stabilization of mammalian liver branched-chain α-ketoacid dehydrogenase by thiamin ... Stabilization of mammalian liver branched-chain α-ketoacid dehydrogenase by thiamin pyrophosphate. / Danner, Dean J.; Lemmon, ...

https://miami.pure.elsevier.com/en/publications/stabilization-of-mammalian-liver-branched-chain-%CE%B1-ketoacid-dehydr

D3.383.129.578.770 Pyruvate Dehydrogenase (Lipoamide) D8.811.682.75.725 D5.500.562.625.875 D8.811.682.657.350.875 Pyruvate ... 1-Methyl-4-phenyl-1,2,3,6-tetrahydropyridine D24.185.926.640.550 1-Sarcosine-8-Isoleucine Angiotensin II D17.350.50.50.50.725 ... E2.831.580.499.100 Acyl-CoA Dehydrogenase D8.811.682.675.150.100 D8.811.682.660.150.100 Acyl-CoA Dehydrogenase, Long-Chain ... D2.886.740.703.350 Glutamate Dehydrogenase D8.811.682.135.398 D8.811.682.664.500.398 Glutamate Dehydrogenase (NADP+) D8.811. ...

https://nlmpubs.nlm.nih.gov/projects/mesh/1999-2010/newterms/mnchg2006.txt

Other name(s): branched-chain oxo-acid dehydrogenase phosphatase; branched-chain 2-keto acid dehydrogenase phosphatase; ... lipoamide)]-phosphatase. Systematic name: [3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring)]-phosphate ... Regulation of mammalian pyruvate and branched-chain α-keto acid dehydrogenase complexes by phosphorylation-dephosphorylation. ... Dephosphorylation and reactivation of phosphorylated purified ox-kidney branched-chain dehydrogenase complex by co-purified ...

https://iubmb.qmul.ac.uk/enzyme/EC3/1/3/52.html

https://decs.bvsalud.org/I/DeCS2016_Alfab-D.htm

... "lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial" Dbt 482 Rattus ... similar to Succinate semialdehyde dehydrogenase (NAD(+)-dependent succinic semialdehyde dehydrogenase) Aldh5a1 523 Rattus ... Branched-chain alpha-keto acid dehydrogenase E1 component alpha chain) (BCKDH E1-alpha)" Bckdha 480 Rattus norvegicus ... "acyl-CoA dehydrogenase family member 9, mitochondrial" Acad9 625 Rattus norvegicus ...

https://esbl.nhlbi.nih.gov/helixweb/Database/IMCD_Proteome_Dev/images/IMCD_Proteome.txt

https://decs2019.bvsalud.org/P/new_2004.htm

https://decs2012.bvsalud.org/P/new_2004.htm

https://decs2013.bvsalud.org/P/new_2004.htm

... lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity). Required for the production of the monomethyl ... The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2 ... and lipoamide dehydrogenase (E3) (By similarity).. Required for the production of the monomethyl branched-chain fatty acids ( ... mitochondrial alpha-ketoglutarate dehydrogenase complex Source: GO_CentralInferred from biological aspect of ancestori*. " ...

https://www.uniprot.org/uniprot/O45924

Human Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial(DBT) ELISA kit ... Human Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial(DBT) ELISA kit ... Mouse Dbt/ Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial ELISA Kit ... Human DBT/ Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial ELISA Kit ...

https://orbitalbiosciences.com/rat-bckdkbranched-chain-alpha-ketoacid-dehydrogenase-kinase-elisa-kit/

Lipoamide dehydrogenase is a component of the alpha- ketoacid dehydrogenase complexes. This includes the pyruvate dehydrogenase ... Catalyzes the transfer of a methyl group from 5- methyltetrahydrofolate to homocysteine resulting in methionine formation. Gene ... oxobutanoate + H(2)O = tetrahydrofolate + 2-dehydropantoate. Gene Name:. ECM31. Uniprot ID:. P38122 Molecular weight:. ... 4. Dihydrolipoyl dehydrogenase, mitochondrial. General function:. Involved in oxidoreductase activity. Specific function:. ...

http://www.ymdb.ca/compounds/YMDB00483

... pyruvate dehydrogenase (lipoamide) e1 component aceF 419944 - 421215 + , dihydrolipoamide S-acetyltransferase ydeD 421222 - ... NADH dehydrogenase subunit G nuoH 856052 - 857050 + , NADH dehydrogenase I chain H nuoI 857053 - 857538 + , NADH dehydrogenase ... NADH dehydrogenase I chain E nuoF 852685 - 854016 + , NADH dehydrogenase I subunit F TERM 765 855437 - 855419 - g 75 -6 - ... NADH dehydrogenase subunit B nuoC 850317 - 850925 + , NADH dehydrogenase I chain C TERM 762 851897 - 851917 + G 73 -5.5 - ...

http://transterm.cbcb.umd.edu/tt/Candidatus_Pelagibacter_ubique_HTCC1062.tt

Dihydrothioctic dehydrogenase, Lipoamide dehydrogenase (NADH), Lipoamide oxidoreductase (NADH), Lipoamide reductase, Lipoamide ... m] : 4mopName: 4-Methyl-2-oxopentanoate. Formula: C6H9O3. Charge: -1. click to see details on this item + coaName: Coenzyme A. ... dihydrothioctic dehydrogenase, lipoamide dehydrogenase (NADH), lipoamide oxidoreductase (NADH), lipoamide reductase, lipoamide ... dihydrothioctic dehydrogenase, lipoamide dehydrogenase (NADH), lipoamide oxidoreductase (NADH), lipoamide reductase, lipoamide ...

http://wormflux.umassmed.edu/Enzymes/1.8.1.4.html

Mitochondrial Branched-chain alpha-ketoacid dehydrogenase kinase Phosphatase Pyruvate Kinase BCKDH Enzyme Amino Acids Activates Complex Chain Type Cell

We tested if expression of the mitochondrial BCAA oxidation checkpoint, branched-chain α-ketoacid dehydrogenase (BCKD) complex, is reduced in obese WAT and regulated by metabolic signals. (elsevier.com)
Thiamin pyrophosphate, CoASH, and NAD + have been shown to reversibly bind to the purified bovine liver mitochondrial branched-chain α-ketoacid dehydrogenase complex. (elsevier.com)
A mitochondrial enzyme associated with the 3-methyl-2-oxobutanoate dehydrogenase complex. (qmul.ac.uk)

Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Rat Branched Chain Alpha-Ketoacid Dehydrogenase Kinase (BCKDK) in Tissue homogenates, cell lysates and other biological fluids. (orbitalbiosciences.com)

1. Fatania, H.R., Patston, P.A. and Randle, P.J. Dephosphorylation and reactivation of phosphorylated purified ox-kidney branched-chain dehydrogenase complex by co-purified phosphatase. (qmul.ac.uk)

2. Reed, L.J., Damuni, Z. and Merryfield, M.L. Regulation of mammalian pyruvate and branched-chain α-keto acid dehydrogenase complexes by phosphorylation-dephosphorylation. (qmul.ac.uk)

3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)] kinase. (edu.pl)

This gene encodes the E2 subunit of the branched-chain α-keto acid dehydrogenase (BCKDH) complex, a core component of branched-chain amino acid (BCAA) metabolism. (nih.gov)

Treatment of 3T3-L1 adipocytes or mice with peroxisome proliferatoractivated receptor-γ agonists increased WAT BCAA catabolism enzyme mRNAs, whereas the nonmetabolizable glucose analog 2-deoxy-D-glucose had the opposite effect. (elsevier.com)
Catalyzes the phosphorylation and inactivation of the branched-chain alpha-ketoacid dehydrogenase complex, the key regulatory enzyme of the valine, leucine and isoleucine catabolic pathways. (nih.gov)

Elevated blood branched-chain amino acids (BCAA) are often associated with insulin resistance and type 2 diabetes, which might result from a reduced cellular utilization and/or incomplete BCAA oxidation. (elsevier.com)

Simultaneously dephosphorylates and activates EC 1.2.4.4 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring), that has been inactivated by phosphorylation. (qmul.ac.uk)

The branched-chain alpha-ketoacid dehydrogenase complex (BCKD) is an important regulator of the valine, leucine, and isoleucine catabolic pathways. (nih.gov)
The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO 2 . (uniprot.org)

Danner, DJ , Lemmon, SK & Elsas, LJ 1980, ' Stabilization of mammalian liver branched-chain α-ketoacid dehydrogenase by thiamin pyrophosphate ', Archives of Biochemistry and Biophysics , vol. 202, no. 1, pp. 23-28. (elsevier.com)
It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity). (uniprot.org)

The results support the hypothesis that suboptimal insulin action and/or perturbed metabolic signals in WAT, as would be seen with insulin resistance/type 2 diabetes, could impair WAT BCAA utilization. (elsevier.com)

3 Ribeirão Preto Regional Center of Hematology, National Institute of Science and Technology in Cell Therapy and Cell Therapy Center, Ribeirão Preto, Brazil. (nih.gov)

Anatomy4

Organisms12

Diseases2

Chemicals and Drugs141

Analytical, Diagnostic and Therapeutic Techniques and Equipment12

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3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide)

Dihydrolipoamide Dehydrogenase

Acetoacetates

Keto Acids

Butyrates

Dinitrobenzenes

Hydrazones

Stereoisomerism

L-Lactate Dehydrogenase

Ketoglutarate Dehydrogenase Complex

Thioctic Acid

Alcohol Dehydrogenase

Glycine Dehydrogenase (Decarboxylating)

Pyruvate Dehydrogenase (Lipoamide)

Glyceraldehyde-3-Phosphate Dehydrogenases

NAD

Glycine Decarboxylase Complex

Aldehyde Dehydrogenase

Glutamate Dehydrogenase

Glucosephosphate Dehydrogenase

Malate Dehydrogenase

Isocitrate Dehydrogenase

Ketone Oxidoreductases

Alcohol Oxidoreductases

Carbohydrate Dehydrogenases

Succinate Dehydrogenase

L-Iditol 2-Dehydrogenase

Pyruvate Dehydrogenase Complex

Glycerolphosphate Dehydrogenase

Glycine Decarboxylase Complex H-Protein

Kinetics

Hydroxysteroid Dehydrogenases

Glucose 1-Dehydrogenase

Oxidoreductases

Glutathione Reductase

Aldehyde Oxidoreductases

Oxidation-Reduction

Molecular Sequence Data

NADP

Glucose Dehydrogenases

3-Hydroxysteroid Dehydrogenases

Flavin-Adenine Dinucleotide

Phosphogluconate Dehydrogenase

Sugar Alcohol Dehydrogenases

Acyl-CoA Dehydrogenases

Amino Acid Sequence

Azotobacter

NADH Dehydrogenase

IMP Dehydrogenase

Lactate Dehydrogenases

Apoenzymes

Formate Dehydrogenases

17-Hydroxysteroid Dehydrogenases

Acyl-CoA Dehydrogenase

Multienzyme Complexes

Amino Acid Oxidoreductases

Dihydrolipoyllysine-Residue Acetyltransferase

Xanthine Dehydrogenase

Escherichia coli

Hydroxybutyrate Dehydrogenase

Aminomethyltransferase

Azotobacter vinelandii

3-Hydroxyacyl CoA Dehydrogenases

11-beta-Hydroxysteroid Dehydrogenases

Swine

Pyruvate Dehydrogenase (Lipoamide)-Phosphatase

Spectrophotometry

Substrate Specificity

Dihydrouracil Dehydrogenase (NADP)

Hydrogen-Ion Concentration

Uridine Diphosphate Glucose Dehydrogenase

Base Sequence

Glucosephosphate Dehydrogenase Deficiency

11-beta-Hydroxysteroid Dehydrogenase Type 1

Pyruvates

Alanine Dehydrogenase

Cloning, Molecular

3-alpha-Hydroxysteroid Dehydrogenase (B-Specific)

Mannitol Dehydrogenases

Pseudomonas