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 alpha-keto acid dehydrogenase ... branched-chain oxo-acid dehydrogenase phosphatase, branched-chain 2-keto acid dehydrogenase phosphatase, branched-chain alpha- ... keto acid dehydrogenase phosphatase, BCKDH, [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)]-phosphatase, [3-methyl-2- ...
... 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 ...
Catalyzes the phosphorylation and inactivation of the branched-chain alpha-ketoacid dehydrogenase complex, the key regulatory ... Branched-chain ketoacid dehydrogenase kinase deficiency (BCKDKD)2 Publications. Manual assertion based on experiment ini ... negative regulation of pyruvate dehydrogenase activity Source: GO_CentralInferred from biological aspect of ancestori*. " ... "Two novel mutations in the BCKDK (branched-chain keto-acid dehydrogenase kinase) gene are responsible for a neurobehavioral ...
... lipoamide]] kinase, mitochondrial. A. 418. Rattus norvegicus. Mutation(s): 0 Gene Names: Bckdk. EC: 2.7.11.4. ... Crystal structure of branched-chain alpha-ketoacid dehydrogenase kinase/S-alpha-chloroisocaproate complex. *DOI: 10.2210/ ... BCAA homeostasis is controlled by the mitochondrial branched-chain α-ketoacid dehydrogenase complex (BCKDC), which is ... BCAA homeostasis is controlled by the mitochondrial branched-chain α-ketoacid dehydrogenase complex (BCKDC), which is ...
Recently, six of the autoantigens have been identified as components of the 2-oxo acid dehydrogenase multienzyme complexes ... Immunoblotting studies have shown that two of these components, namely E2 and protein X of pyruvate dehydrogenase complex, are ... Lipoamide) * Autoantibodies / analysis* * Enzyme-Linked Immunosorbent Assay ... Recently, six of the autoantigens have been identified as components of the 2-oxo acid dehydrogenase multienzyme complexes ...
Catalyzes the phosphorylation and inactivation of the branched-chain alpha-ketoacid dehydrogenase complex, the key regulatory ... lipoamide]] kinase, mitochondrial antibody. *[3-methyl-2-oxobutanoate dehydrogenase [lipoamide]] kinase antibody ...
EC 3.1.3.43 [pyruvate dehydrogenase (acetyl-transferring)]-phosphatase. EC 3.1.3.44 [acetyl-CoA carboxylase]-phosphatase. EC ... lipoamide)]-phosphatase. EC 3.1.3.53 [myosin-light-chain] phosphatase. EC 3.1.3.54 fructose-2,6-bisphosphate 6-phosphatase. EC ... EC 3.1.3. Phosphoric Monoester Hydrolases. Contents. EC 3.1.3.1 alkaline phosphatase. EC 3.1.3.2 acid phosphatase. EC 3.1.3.3 ... EC 3.1.3.103 3-deoxy-D-glycero-D-galacto-nononate 9-phosphatase. EC 3.1.3.104 5-amino-6-(5-phospho-D-ribitylamino)uracil ...
... lipoamide]] kinase, mitochondrial Aliases:. Not Available. RefSeq:. Not Available. ...
... lipoamide]] kinase, mitochondrial Show on y-axis - ... The lollipop plot above illustrates recurrent (observed in 3 ...
... and linkers in 2-oxo acid dehydrogenase multienzyme complexes: a paradigm in the design of a multifunctional protein ... Lipoamide) Grant support * Wellcome Trust/United Kingdom ... Domains, motifs, and linkers in 2-oxo acid dehydrogenase ...
Branched-chain ketoacid dehydrogenase kinase deficiency (BCKDKD) [MIM:614923]: A metabolic disorder characterized by autism, ... lipoamide]] kinase, mitochondrial. Gene: BCKDK Chromosomal location: 16p12.3-p13.13 ... Two novel mutations in the BCKDK (branched-chain keto-acid dehydrogenase kinase) gene are responsible for a neurobehavioral ... 3. The score within a Blosum matrix for the corresponding wild-type to variant amino acid change. The log-odds score measures ...
Fingerprint Dive into the research topics where Jeffrey M Chinsky is active. These topic labels come from the works of this person. Together they form a unique fingerprint. ...
Other name(s): pyruvate decarboxylase (ambiguous); pyruvate dehydrogenase (ambiguous); pyruvate dehydrogenase (lipoamide); ... Evidence for the common identity of α-ketoisocaproic acid and α-keto-β-methyl-valeric acid dehydrogenases. J. Biol. Chem. 243 ( ... α-ketoglutarate dehydrogenase; alphaketoglutaric acid dehydrogenase; α-ketoglutaric dehydrogenase; α-oxoglutarate dehydrogenase ... Other name(s): pyruvate dehydrogenase (ambiguous); pyruvic dehydrogenase (ambiguous); pyruvic (cytochrome b1) dehydrogenase ( ...
Stimulation of reactive oxygen species generation by disease-causing mutations of lipoamide dehydrogenase. Ambrus, A., Törőcsik ... Refolding of the human dihydrolipoamide dehydrogenase. Ambrus, A., Törőcsik, B. & Ádám-Vizi, V., júl. 15 2009, In : Biochemical ... Periplasmic cold expression and one-step purification of human dihydrolipoamide dehydrogenase. Ambrus, A., Törőcsik, B. & Ádám- ... Human dihydrolipoamide dehydrogenase (E3) deficiency: Novel insights into the structural basis and molecular pathomechanism. ...
Riboflavin responsive mitochondrial myopathy is a new phenotype of dihydrolipoamide dehydrogenase deficiency: The chaperon-like ... EHOD consortium, Mar 2019, In : Journal of Inherited Metabolic Disease. 42, 2, p. 333-352 20 p.. Research output: Contribution ... EHOD consortium, Sep 3 2018, In : Journal of Inherited Metabolic Disease.. Research output: Contribution to journal › Article ... 2 others, Taylor, R. W. & Diodato, D., Apr 2018, In : Human Mutation. 39, 4, p. 563-578 16 p.. Research output: Contribution to ...
... like that of pyruvate dehydrogenase, is regulated, at least in part, by interconversion between the active dephosphorylated ... The activity of the intramitochondrial branched-chain 2-oxo acid dehydrogenase (BCDH), ... Pyruvate Dehydrogenase (Lipoamide); Pyruvate Dehydrogenase Complex; Rats ... Lipoamide); Adenosine Triphosphate; Adipose Tissue; Animals; Enzyme Activation; Insulin; Ketone Oxidoreductases; Leucine; Male ...
Riboflavin responsive mitochondrial myopathy is a new phenotype of dihydrolipoamide dehydrogenase deficiency: The chaperon-like ... 2 others, Bertini, E. S. & Carrozzo, R., 2016, (Accepted/In press) In : Clinical Genetics.. Research output: Contribution to ... 2 others, Bertini, E. & Carrozzo, R., 2016, (Accepted/In press) In : Clinical Genetics.. Research output: Contribution to ... Lipoamide) 2013 Novel TTC19 mutation in a family with severe psychiatric manifestations and complex III deficiency. Nogueira, C ...
MECHANISM OF E. COLI PYRUVATE DEHYDROGENASE COMPLEX-E1. Jordan, F.. National Institutes of Health ... DHTKD1 and OGDH display substrate overlap in cultured cells and form a hybrid 2-oxo acid dehydrogenase complex in vivo. Leandro ... Engineering 2-oxoglutarate dehydrogenase to a 2-oxo aliphatic dehydrogenase complex by optimizing consecutive components. ... Structure-function analyses of the G729R 2-oxoadipate dehydrogenase genetic variant associated with a disorder of l-lysine ...
Activation of the branched-chain α-ketoacid dehydrogenase complex by a broad specificity protein phosphatase. Harris, R. A., ... McAteer, J. A., Evan, A. P. & Douglas, W. H. J., Sep 1982, In : Journal of Tissue Culture Methods. 7, 3, p. 85-88 4 p.. ... Roman, A. & Edenberg, H. J., Dec 1 1981, In : Journal of virology. 40, 3, p. 729-734 6 p.. Research output: Contribution to ... Olson, K. R., Flint, K. B. & Budde, R. B., Sep 1 1981, In : Cell And Tissue Research. 219, 3, p. 535-541 7 p.. Research output ...
... lipoamide)] kinase Current Synonym true false 209561015 Branched-chain alpha-ketoacid dehydrogenase kinase Current Synonym true ... lipoamide) kinase (substance). Code System Preferred Concept Name. 3-methyl-2-oxobutanoate dehydrogenase (lipoamide) kinase ( ...
... 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)- ...
... and branched-chain α-ketoacid dehydrogenases by an atypical kinase/phosphatase cascade is well established. More recently, the ... Lipoamide) Medicine & Life Sciences * Phosphotransferases Medicine & Life Sciences ... and branched-chain α-ketoacid dehydrogenases by an atypical kinase/phosphatase cascade is well established. More recently, the ... and branched-chain α-ketoacid dehydrogenases by an atypical kinase/phosphatase cascade is well established. More recently, the ...
Antimitochondrial antibodies (AMA) recognizing the acetyltransferase (E2) of the pyruvate dehydrogenase (PDH) complex have been ... Lipoamide) Medicine & Life Sciences * Biliary Liver Cirrhosis Medicine & Life Sciences ... N2 - Antimitochondrial antibodies (AMA) recognizing the acetyltransferase (E2) of the pyruvate dehydrogenase (PDH) complex have ... AB - Antimitochondrial antibodies (AMA) recognizing the acetyltransferase (E2) of the pyruvate dehydrogenase (PDH) complex have ...
STRUCTURE OF ALCOHOL AND ALDEHYDE DEHYDROGENASES. Hurley, T.. National Institutes of Health ...
Lipoamide) Acid Dehydrogenase, Alpha-Keto Alpha Keto Acid Dehydrogenase Alpha-Keto Acid Dehydrogenase BCKA Decarboxylase ... Lipoamide). Acid Dehydrogenase, Alpha-Keto. Alpha Keto Acid Dehydrogenase. Alpha-Keto Acid Dehydrogenase. BCKA Decarboxylase. ... Dehydrogenase, Alpha-Keto Acid Dehydrogenase, Branched-Chain Oxo-Acid Oxo-Acid Dehydrogenase, Branched-Chain ... Dehydrogenase, Alpha-Keto Acid. Dehydrogenase, Branched-Chain Oxo-Acid. Oxo-Acid Dehydrogenase, Branched-Chain. ...
Lin, Y. H. & Zhu, H., Feb 8 2021, In: Cancer Cell. 39, 2, p. 142-144 3 p.. Research output: Contribution to journal › Article ... Comazzetto, S., Murphy, M. M., Berto, S., Jeffery, E., Zhao, Z. & Morrison, S. J., Mar 7 2019, In: Cell Stem Cell. 24, 3, p. ... 3 others, McNutt, M. C., Pascual, J. M. & DeBerardinis, R. J., Apr 30 2019, In: Cell Reports. 27, 5, p. 1376-1386.e6. Research ... 3-dimensional visualization of implant-tissue interface with the polyethylene glycol associated solvent system tissue clearing ...
Cheon, S., Kaur, K., Nijem, N., Tuncay, I. O., Kumar, P., Dean, M., Juusola, J., Guillen-Sacoto, M. J., Bedoukian, E., Ierardi-Curto, L., Kaplan, P., Bradley Schaefer, G., Mishra, P. & Chahrour, M. H., Feb 26 2019, In : Proceedings of the National Academy of Sciences of the United States of America. 116, 9, p. 3662-3667 6 p.. Research output: Contribution to journal › Article ...
Kinetic characterization of branched chain ketoacid dehydrogenase. Boyer, B. & Odessey, R., Feb 15 1991, In: Archives of ... Boyer, B. & Odessey, R., 1990, In: Biochemical Journal. 271, 2, p. 523-528 6 p.. Research output: Contribution to journal › ... Bennett, P. R., Elder, M. G. & Myatt, L., Jan 1 1990, In: American journal of obstetrics and gynecology. 163, 1, p. 241-242 2 p ... Shepherd, R. W., Patton, P. E., Novy, M. J. & Burry, K. A., Mar 1990, In: Obstetrics and gynecology. 75, 3, p. 417-420 4 p.. ...
Murakami, T. & Tsuchida, K., 01-02-2008, In : Mini-Reviews in Medicinal Chemistry. 8, 2, p. 175-183 9 p.. Research output: ... Manabe, K. & Yokoyama, S., 01-02-2008, In : Applied Radiation and Isotopes. 66, 2, p. 122-125 4 p.. Research output: ... The Japanese journal of clinical pathology. 56, 3, p. 214-220 7 p.. Research output: Contribution to journal › Article ... Nagahama, K., Ogawa, A., Shirane, K., Shimomura, Y., Sugimoto, K. & Mizoguchi, A., 02-2008, In : Gastroenterology. 134, 2, p. ...
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 ...
Alpha-ketoacid/pyruvate dehydrogenase kinase, N-terminal domain. 3tz5A01. 3.30.565.10. Alpha Beta. 2-Layer Sandwich. Heat Shock ... lipoamide]] kinase, total genus 109 structure length 312 ... structure of branched-chain alpha-ketoacid dehydrogenase kinase ...
mitochondrial pyruvate dehydrogenase (lipoamide) phosphatase complex. GO:0020023. kinetoplast. GO:0030062. mitochondrial ...
  • Two novel mutations in the BCKDK (branched-chain keto-acid dehydrogenase kinase) gene are responsible for a neurobehavioral deficit in two pediatric unrelated patients. (expasy.org)
  • Phosphorylation of mitochondrial proteins has been recognized for decades, and the regulation of pyruvate- and branched-chain α-ketoacid dehydrogenases by an atypical kinase/phosphatase cascade is well established. (elsevier.com)
  • 3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)] kinase. (edu.pl)
  • Branched-chain α-keto acid dehydrogenase (BCKDH) kinase (BDK) is responsible for the regulation of BCKDH complex, which is the rate-limiting enzyme in the catabolism of branched-chain amino acids (BCAAs). (fujita-hu.ac.jp)
  • Branched-chain ketoacid dehydrogenase kinase deficiency (BCKDKD) [MIM:614923]: A metabolic disorder characterized by autism, epilepsy, intellectual disability, and reduced branched-chain amino acids. (antibodyplus.com)
  • We propose that particular residues are involved in: (a) binding the 2-oxo acid substrate, (b) decarboxylation of the 2-oxo acid and reductive acetylation of the tethered lipoyl domain in the PDH complex, (c) an 'open-close' mechanism of the active site, and (d) phosphorylation by the E1-specific kinase (in eukaryotic PDH and branched chain 2-oxo acid dehydrogenase complexes). (elsevier.com)
  • The human mitochondrial branched-chain alpha-ketoacid dehydrogenase complex (BCKDC) is a 4 MDa macromolecular machine comprising three catalytic components (E1b, E2b, and E3), a kinase, and a phosphatase. (proteopedia.org)
  • Immunoblotting studies have shown that two of these components, namely E2 and protein X of pyruvate dehydrogenase complex, are the major antigenic polypeptides recognized by autoantibodies. (nih.gov)
  • pyruvate dehydrogenase (cytochrome). (qmul.ac.uk)
  • The activity of the intramitochondrial branched-chain 2-oxo acid dehydrogenase (BCDH), like that of pyruvate dehydrogenase, is regulated, at least in part, by interconversion between the active dephosphorylated enzyme and its inactive phosphorylated form. (umassmed.edu)
  • Antimitochondrial antibodies (AMA) recognizing the acetyltransferase (E2) of the pyruvate dehydrogenase (PDH) complex have been previously well-documented and the immunodominant epitope mapped. (elsevier.com)
  • They play a key role in the primary energy metabolism: in glycolysis (pyruvate dehydrogenase complex), the citric acid cycle (2-oxoglutarate dehydrogenase complex) and in amino acid catabolism (branched-chain 2-oxo acid dehydrogenase complex). (wur.nl)
  • Deficiency of the pyruvate dehydrogenase complex predominantly leads to lactic acidosis combined with impairment of neurological function and/or delayed growth and development. (wur.nl)
  • Three-dimensional structures of three components of the complex are presently available: of the pyruvate dehydrogenase component (E1), of the dihydrolipoyl acyltransferase component (E2) and of the lipoamide dehydrogenase component (E3). (wur.nl)
  • Limited proteolysis of the pyruvate decarboxylase (E1, α 2 β 2 ) component of the pyruvate dehydrogenase (PDH) multi-enzyme complex of Bacillus stearothermophilus has indicated the importance for catalysis of a site (Tyr281-Arg282) in the E1α subunit (Chauhan, H.J., Domingo, G.J., Jung, H.-I. & Perham, R.N. (2000) Eur. (elsevier.com)
  • Pyruvate dehydrogenase complex (PDC) is a complex of three enzymes that converts pyruvate into acetyl-CoA by a process called pyruvate decarboxylation. (hyperleap.com)
  • Pyruvate dehydrogenase is inhibited when one or more of the three following ratios are increased: ATP/ADP, NADH/NAD + and acetyl-CoA/CoA. (hyperleap.com)
  • It is catalyzed by the pyruvate dehydrogenase complex. (hyperleap.com)
  • One of the most studied roles of RLA is as a cofactor of the pyruvate dehydrogenase complex (PDC or PDHC), though it is a cofactor in other enzymatic systems as well (described below). (hyperleap.com)
  • Pyruvate decarboxylation or pyruvate oxidation, also known as link reaction, is the conversion of pyruvate into acetyl-CoA by the enzyme complex pyruvate dehydrogenase complex. (hyperleap.com)
  • Pyruvate is oxidized to acetyl-CoA and CO 2 by the pyruvate dehydrogenase complex (PDC). (hyperleap.com)
  • Initially, pyruvate and thiamine pyrophosphate (TPP or vitamin B 1 ) are bound by pyruvate dehydrogenase subunits. (hyperleap.com)
  • Pyruvate decarboxylation by the pyruvate dehydrogenase complex produces acetyl-CoA. (hyperleap.com)
  • PDK thus participates in the regulation of the pyruvate dehydrogenase complex of which pyruvate dehydrogenase is the first component. (hyperleap.com)
  • The E3 binding protein is a component of the pyruvate dehydrogenase complex found only in eukaryotes.Defects in this gene are a cause of pyruvate dehydrogenase deficiency which results in neurological dysfunction and lactic acidosis in infancy and early childhood. (hyperleap.com)
  • Flgurr 9,45 Upoamide is a covalently bound prosthetic group of pyruvate dehydrogenase and four other enzymes and 226. (doctorabel.us)
  • Another component of ihe complex, dihydrolipoamide dehydrogenase (1:3: ECI.8.I.4) transfers the hydrogens \ia FAD to NAD Ihe same gene encodes the dihydrolipoamide dehydrogenase of pyruvate dehydrogenase and the other two alpha-ketoacid dehydrogenases. (doctorabel.us)
  • In the pyruvate dehydrogenase complex, it binds to the core of EC 2.3.1.12, dihydrolipoyllysine-residue acetyltransferase, and catalyses oxidation of its dihydrolipoyl groups. (creative-enzymes.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. (uniprot.org)
  • 2. Knox, W.E. The quinine-oxidizing enzyme and liver aldehyde oxidase. (qmul.ac.uk)
  • In this study, we demonstrate that sera from patients with primary biliary cirrhosis (PBC) react with another lipoic acid containing acyltransferase enzyme, namely the E2 of the branched α-ketoacid dehydrogenase (BCKD) complex. (elsevier.com)
  • An NAD+ dependent enzyme that catalyzes the oxidation 3-methyl-2-oxobutanoate to 2-methylpropanoyl-CoA. (bireme.br)
  • A mitochondrial enzyme associated with the 3-methyl-2-oxobutanoate dehydrogenase complex. (creative-enzymes.com)
  • This enzyme catalyses the following chemical reaction [3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring)] phosphate + H2O ⇌ {\displaystyle \rightleftharpoons } [3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring)] + phosphate This mitochondrial enzyme is associated with the 3-methyl-2-oxobutanoate dehydrogenase complex. (wikipedia.org)
  • This multi-enzyme complex is related structurally and functionally to the oxoglutarate dehydrogenase and branched-chain oxo-acid dehydrogenase multi-enzyme complexes. (hyperleap.com)
  • The branched-chain alpha-keto acid dehydrogenase complex (BCKD) is an inner-mitochondrial enzyme complex involved in the breakdown of the branched-chain amino acids isoleucine, leucine, and valine. (nih.gov)
  • In addition, 2-ketobutyric acid and coenzyme A can be converted into propionyl-CoA through its interaction with the enzyme branched-chain alpha-keto dehydrogenase complex. (hmdb.ca)
  • It is the second to last step in the synthesis of isobutyryl-CoA and is converted from 3-methyl-2-oxobutanoate via the enzyme 2-oxoisovalerate dehydrogenase [EC:1.2.4.4]. (hmdb.ca)
  • Recently, six of the autoantigens have been identified as components of the 2-oxo acid dehydrogenase multienzyme complexes located within mammalian mitochondria. (nih.gov)
  • 2-oxo acid dehydrogenase complexes are a ubiquitous family of multienzyme systems that catalyse the oxidative decarboxylation of various 2-oxo acid substrates. (wur.nl)
  • In this review we have combined this knowledge to gain more insight into the structural basis of the dysfunctioning of the 2-oxo acid dehydrogenase complexes. (wur.nl)
  • A component of the multienzyme 2-oxo-acid dehydrogenase complexes. (creative-enzymes.com)
  • It plays a similar role in the oxoglutarate and 3-methyl-2-oxobutanoate dehydrogenase complexes. (creative-enzymes.com)
  • This mechanism provides a paradigm for regulation of mitochondrial alpha-ketoacid dehydrogenase complexes by phosphorylation. (proteopedia.org)
  • Maple urine disease is an inborn metabolic error caused by dysfunction of the branched-chain 2-oxo acid dehydrogenase complex. (wur.nl)
  • BCAA catabolism in skeletal muscle is regulated by the branched-chain alpha-keto acid dehydrogenase (BCKDH) complex, located at the second step in the BCAA catabolic pathway. (semanticscholar.org)
  • The dihydrolipoate, still bound to a lysine residue of the complex, then migrates to the dihydrolipoyl dehydrogenase (E3) active site where it undergoes a flavin-mediated oxidation, identical in chemistry to disulfide isomerase. (hyperleap.com)
  • Maple syrup urine disease (MSUD) is an inherited metabolic disorder caused by mutations in the branched chain alpha-keto acid dehydrogenase complex. (cdc.gov)
  • Maple syrup urine disease (MSUD) is predominantly caused by mutations in the BCKDHA, BCKDHB and DBT genes, which encode for the E1α, E1β and E2 subunits of the branched-chain α-keto acid dehydrogenase complex, respectively. (bvsalud.org)
  • The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). (nih.gov)
  • The BCKD complex is thought to be composed of a core of 24 transacylase (E2) subunits, and associated decarboxylase (E1), dehydrogenase (E3), and regulatory subunits. (nih.gov)
  • 2-Oxoglutarate dehydrogenase (EC2.3 1 61): The TC A-cycle intermediate 2-oxoglu-tarate is metabolized to suceinyl-CoA by a large TCP-dependent multienzyme complex containing 24 copies of the lipoamide-contaming subunit K2 (dihydrolipoamide suc-cinyltransferase) with octahedral symmetry: these subunits contain a single lipoamide attached to lysine 110. (doctorabel.us)
  • Molecular mechanism for regulation of the human mitochondrial branched-chain alpha-ketoacid dehydrogenase complex by phosphorylation. (proteopedia.org)
  • Structure of the gene encoding the entire mature E1 alpha subunit of human branched-chain alpha-keto acid dehydrogenase complex. (proteopedia.org)
  • Molecular basis of maple syrup urine disease: novel mutations at the E1 alpha locus that impair E1(alpha 2 beta 2) assembly or decrease steady-state E1 alpha mRNA levels of branched-chain alpha-keto acid dehydrogenase complex. (proteopedia.org)
  • Matsuda I, Nobukuni Y, Mitsubuchi H, Indo Y, Endo F, Asaka J, Harada A. A T-to-A substitution in the E1 alpha subunit gene of the branched-chain alpha-ketoacid dehydrogenase complex in two cell lines derived from Menonite maple syrup urine disease patients. (proteopedia.org)
  • Occurrence of a Tyr393----Asn (Y393N) mutation in the E1 alpha gene of the branched-chain alpha-keto acid dehydrogenase complex in maple syrup urine disease patients from a Mennonite population. (proteopedia.org)
  • Simultaneously dephosphorylates and activates EC 1.2.4.4 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring), that has been inactivated by phosphorylation. (creative-enzymes.com)
  • 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring))-phosphatase (EC 3.1.3.52, branched-chain oxo-acid dehydrogenase phosphatase, branched-chain 2-keto acid dehydrogenase phosphatase, branched-chain alpha-keto acid dehydrogenase phosphatase, BCKDH, [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)]-phosphatase, [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)]-phosphate phosphohydrolase) is an enzyme with systematic name (3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring))-phosphate phosphohydrolase. (wikipedia.org)
  • Effects of insulin on the regulation of branched-chain alpha-keto acid dehydrogenase E1 alpha subunit gene expression. (naver.com)
  • However, within Old Order Mennonite communities, the incidence is 1:150 live births and results from a common tyrosine to asparagine substitution (Y438N) in the E1alpha subunit of branched chain alpha-keto acid dehydrogenase. (cdc.gov)
  • It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3). (nih.gov)
  • Branched-chain alpha-keto acid dehydrogenase ('£€1.2.4.4'): The alpha-ketoacids 3-methyl-2-oxobutanoate. (doctorabel.us)
  • In humans, 2-ketobutyric acid is involved in threonine and 2-oxobutanoate degradation. (hmdb.ca)
  • The branched-chain amino acids (BCAAs) leucine, isoleucine, and valine are elevated in maple syrup urine disease, heart failure, obesity, and type 2 diabetes. (rcsb.org)
  • 4-methyl-2-oxopentanoate, and (S)-3-methy 1-2-oxopen l anoat c, generated by deamination of the branched-chain amino acids valine, leucine, and isoieucme. (doctorabel.us)
  • 2-Ketobutyric acid is a substance that is involved in the metabolism of many amino acids (glycine, methionine, valine, leucine, serine, threonine, isoleucine) as well as propanoate metabolism and C-5 branched dibasic acid metabolism. (hmdb.ca)
  • Succinyl-CoA is an important intermediate in the citric acid cycle, where it is synthesized from α-Ketoglutarate by α-ketoglutarate dehydrogenase (EC 1.2.4.2) through decarboxylation, and is converted into succinate through the hydrolytic release of coenzyme A by succinyl-CoA synthetase (EC 6.2.1.5). (hmdb.ca)
  • An association between both Alzheimer disease and Parkinson's disease and the 2-oxoglutarate dehydrogenase gene has been reported. (wur.nl)
  • 2-Methyl-1-hydroxypropyl-ThPP is an intermediate in valine, leucine and isoleucine degradation(KEGG ID C15976). (hmdb.ca)
  • To examine the effect of bafilomycin biosynthesis on valinomycin production, the bafilomycin biosynthetic gene cluster was cloned from the genome of strain M10, as were two branched-chain α-keto acid dehydrogenase (BCDH) gene clusters related to precursor supply for bafilomycin biosynthesis. (elsevier.com)
  • In a fashion, similar to the three lipoatC'-dependent alpha-ketoacid dehydrogenases, the lipoamide arm acts as an acceptor for a methylene group from glycine, transfers it to folate, and is reduced in the process. (doctorabel.us)
  • Another substrate is the dihydrolipoyl group in the H-protein of the glycine-cleavage system (click here for diagram), in which it acts, together with EC 1.4.4.2, glycine dehydrogenase (decarboxylating), and EC 2.1.2.10, aminomethyltransferase, to break down glycine. (creative-enzymes.com)
  • Mutations in this gene result in maple syrup urine disease, type 2. (nih.gov)
  • The standard prep protocol starts with 100 µl of clarified cellular extracts, or approximately 2 mg total cellular extract protein, but the process can be scaled up or down to accommodate different sample volumes and protein concentrations. (biotechsupportgroup.com)
  • The higher valinomycin yield was likely the result of redistribution of the metabolic flux from bafilomycin to valinomycin biosynthesis, because the two antibiotics share a common precursor, 2-ketoisovaleric acid, a deamination product of valine. (elsevier.com)
  • In the present study, we investigated the expression and activity of hepatic BDK in spontaneous type 2 diabetes using hyperinsulinemic Zucker diabetic fatty rats aged 9 weeks and hyperglycemic, but not hyperinsulinemic rats aged 18 weeks. (fujita-hu.ac.jp)
  • These results suggest that insulin regulates BCAA catabolism in type 2 diabetic rats by modulating the hepatic BDK activity. (fujita-hu.ac.jp)
  • 2-Ketobutyric acid, also known as alpha-ketobutyrate or 2-oxobutyrate, belongs to the class of organic compounds known as short-chain keto acids and derivatives. (hmdb.ca)
  • Phosphoric acid, also known as phosphate or [po(OH)3], belongs to the class of inorganic compounds known as non-metal phosphates. (bovinedb.ca)
  • The lipoyl-bearing domain (LBD) of the transacylase (E2) subunit of the branched-chain α-keto acid dehydrogenase complex plays a central role in substrate channeling in this mitochondrial multienzyme complex. (ntnu.edu.tw)