enzyme Name alanine dehydrogenase EC number 1.4.1.1 CAS number 9029 06 5 IUBMB EC number 1 4 1 1 GO code 0000286 image width caption Alanine dehydrogenase EC number 1.4.1.1 is an enzyme that catalysis catalyzes the chemical reaction L alanine H sub 2 sub O NAD sup sup math rightleftharpoons math pyruvate NH sub 3 sub NADH H sup sup The 3 substrate biochemistry substrates of this enzyme are L alanine , water , and nicotinamide adenine dinucleotide , whereas its 4 product chemistry products are pyruvate , ammonia , nicotinamide adenine dinucleotide NADH , and hydrogen ion . This enzyme belongs to the family of oxidoreductase s, specifically those acting on the CH NH2 group of donors with NAD or NADP as acceptor. The systematic name of this enzyme class is L alanine NAD oxidoreductase deaminating . Other names in common use include AlaDH , L alanine dehydrogenase , NAD linked alanine dehydrogenase , alpha alanine dehydrogenase , NAD dependent alanine dehydrogenase , alanine oxidoreductase , and NADH dependent alanine dehydrogenase . This enzyme participates in taurine and hypotaurine metabolism and reductive carboxylate cycle CO2 fixation . Structural studies As of late 2007, 6 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1OMO , PDB link 1PJB , PDB link 1PJC , PDB link 1SAY , PDB link 1VLL , and PDB link 2EEZ . References reflist 1 cite journal author O Connor RJ and Halvorson H date 1961 title The substrate specificity of L alanine dehydrogenase journal Biochim. Biophys. Acta volume 48 issue 1 pages 47&ndash 55 doi 10.1016 0006 3002 61 90513 3 pmid 13730044 cite journal author Pierard A and Wiame JM date 1960 title Proprietes de la L alanine deshydrogenase journal Biochim. Biophys. Acta volume 37 issue 3 pages 490&ndash 502 doi 10.1016 0006 3002 60 90506 0 cite journal author Yoshida A and Freese E date 1965 title Enzymic properties of alanine dehydrogenase of Bacillus subtilis journal Biochim ... more details
15 hydroxyprostaglandin dehydrogenase may refer to 15 hydroxyprostaglandin D dehydrogenase NADP 15 hydroxyprostaglandin I dehydrogenase NADP 15 hydroxyprostaglandin dehydrogenase NAD 15 hydroxyprostaglandin dehydrogenase NADP disambig ... more details
, also named dihydrolipoamide dehydrogenase, is also a component of the pyruvatedehydrogenase complex, the alpha ketoglutarate dehydrogenase complex, and the branched chain alpha keto acide dehydrogenase ... with E3 deficient maple syrup urine disease and Dihydrolipoyl transacetylase Pyruvatedehydrogenase deficiency lipoamide dehydrogenase deficiency . ref name entrez Interactive pathway map TCACycle WP78 highlight Dihydrolipoamide dehydrogenase Enzyme Regulation This protein may use the morpheein ... YS, et al. title How dihydrolipoamide dehydrogenase binding protein binds dihydrolipoamide dehydrogenase in the human pyruvatedehydrogenase complex. journal J. Biol. Chem. volume 281 issue 1 pages ... E3 and E3 binding protein of human pyruvatedehydrogenase complex. journal Structure volume ... oxidation at the level of the pyruvatedehydrogenase complex by PDKs. journal Am. J. Physiol. Endocrinol ... of the cores of the mammalian pyruvatedehydrogenase complex formed by E2 and E2 plus the E3 binding ...PBB geneid 1738 enzyme Name dihydrolipoyl dehydrogenase EC number 1.8.1.4 CAS number 9001 18 7 IUBMB EC number 1 8 1 4 GO code 0004148 image width caption Dihydrolipoamide dehydrogenase DLD , also known as dihydrolipoyl dehydrogenase, mitochondrial , is an enzyme that in humans is encoded by the DLD gene . ref name entrez cite web title Entrez Gene dihydrolipoamide dehydrogenase url http www.ncbi.nlm.nih.gov ... clones for porcine and human lipoamide dehydrogenase. Homology to other disulfide oxidoreductases ... dehydrogenase component human alpha ketoacid dehydrogenase complexes journal Proc. Natl ... G, Robinson BH, Tsui LC title Localization of the human dihydrolipoamide dehydrogenase gene DLD to 7q31 ... Brautigam CA, Chuang JL, Tomchick DR, et al. title Crystal structure of human dihydrolipoamide dehydrogenase ... A, et al. title A novel mutation in the dihydrolipoamide dehydrogenase E3 subunit gene DLD resulting in an atypical form of alpha ketoglutarate dehydrogenase deficiency. journal Hum. Mutat. volume 25 ... more details
enzyme Name alanopine dehydrogenase EC number 1.5.1.17 CAS number 71343 07 2 IUBMB EC number 1 5 1 17 GO code 0047636 image width caption Alanopine dehydrogenase EC number 1.5.1.17 is an enzyme that catalysis catalyzes the chemical reaction 2,2 iminodipropanoate NAD sup sup H sub 2 sub O math rightleftharpoons math L alanine pyruvate NADH H sup sup The 3 substrate biochemistry substrates of this enzyme are 2,2 iminodipropanoate , nicotinamide adenine dinucleotide , and water , whereas its 4 product chemistry products are L alanine , pyruvate , nicotinamide adenine dinucleotide , and hydrogen ion . This enzyme belongs to the family of oxidoreductase s, specifically those acting on the CH NH group of donors with NAD or NADP as acceptor. The systematic name of this enzyme class is 2,2 iminodipropanoate NAD oxidoreductase L alanine forming . Other names in common use include ALPDH , alanopine meso N 1 carboxyethyl alanine dehydrogenase , meso N 1 carboxyethyl alanine NAD oxidoreductase , alanopine NAD oxidoreductase , ADH , and alanopine NAD oxidoreductase . References reflist 1 cite journal author Dando PR date 1981 title Strombine N carboxymethyl D alanine dehydrogenase and alanopine meso N 1 carboxyethyl alanine dehydrogenase from the mussel Mytilus edulis L journal Biochem. Soc. Trans. volume 9 pages 297&ndash 298 cite journal author Fields JH, Eng AK, Ramsden WD, Hochachka PW, Weinstein B date 1980 title Alanopine and strombine are novel imino acids produced by a dehydrogenase found in the adductor muscle of the oyster, Crassostrea gigas journal Arch. Biochem. Biophys. volume 201 pages 110&ndash 4 pmid 6156653 doi 10.1016 0003 9861 80 90493 2 issue 1 cite journal author Fields JH, Hochachka PW date 1981 title Purification and properties of alanopine dehydrogenase from the adductor muscle of the oyster, Crassostrea gigas Mollusca, Bivalvia journal Eur. J. Biochem. volume 114 pages 615&ndash 21 pmid 7238503 doi 10.1111 j.1432 1033.1981.tb05188.x issue 3 Category EC 1.5.1 ... more details
enzyme Name tauropine dehydrogenase EC number 1.5.1.23 CAS number 104645 74 1 IUBMB EC number 1 5 1 23 GO code 0050325 image width caption In enzymology , a tauropine dehydrogenase EC number 1.5.1.23 is an enzyme that catalysis catalyzes the chemical reaction tauropine NAD sup sup H sub 2 sub O math rightleftharpoons math taurine pyruvate NADH H sup sup The 3 product biochemistry products of this enzyme are tauropine , nicotinamide adenine dinucleotide NAD sup sup , and water H sub 2 sub O , whereas its 4 substrate chemistry substrates are taurine , pyruvate , nicotinamide adenine dinucleotide NADH , and hydrogen ion H sup sup . This enzyme belongs to the family of oxidoreductase s, specifically those acting on the CH NH group of donors with NAD or NADP as acceptor. The systematic name of this enzyme class is N2 D 1 carboxyethyl taurine NAD oxidoreductase taurine forming . This enzyme is also called 2 N D 1 carboxyethyl taurine NAD oxidoreductase taurine forming . References reflist 1 cite journal author Gade G date 1986 title Purification and properties of tauropine dehydrogenase from the shell adductor muscle of the ormer, Haliotis lamellosa journal Eur. J. Biochem. volume 160 pages 311&ndash 8 pmid 3769931 doi 10.1111 j.1432 1033.1986.tb09973.x issue 2 1.5 enzyme stub Category EC 1.5.1 Category NADH dependent enzymes Category Enzymes of unknown structure it Tauropina deidrogenasi ja ... more details
17beta dehydrogenase or 17 dehydrogenase may refer to Estradiol 17beta dehydrogenase Testosterone 17beta dehydrogenase 17Beta Hydroxysteroid dehydrogenase dab ... more details
enzyme Name opine dehydrogenase EC number 1.5.1.28 CAS number 108281 02 3 IUBMB EC number 1 5 1 28 GO code 0047129 image width caption In enzymology , an opine dehydrogenase EC number 1.5.1.28 is an enzyme that catalysis catalyzes the chemical reaction 2S 2 1 R carboxyethyl amino pentanoate NAD sup sup H sub 2 sub O math rightleftharpoons math L 2 aminopentanoic acid pyruvate NADH H sup sup The 3 substrate biochemistry substrates of this enzyme are 2S 2 1 R carboxyethyl amino pentanoate , nicotinamide adenine dinucleotide NAD sup sup , and water H sub 2 sub O , whereas its 4 product chemistry products are L 2 aminopentanoic acid , pyruvate , nicotinamide adenine dinucleotide NADH , and hydrogen ion H sup sup . This enzyme belongs to the family of oxidoreductase s, specifically those acting on the CH NH group of donors with NAD or NADP as acceptor. The systematic name of this enzyme class is 2S 2 1 R carboxyethyl amino pentanoate NAD oxidoreductase L aminopentanoate forming . Other names in common use include 2S 2 1 R carboxyethyl amino pentanoate dehydrogenase NAD , , and L aminopentanoate forming . References reflist 1 cite journal author Asano Y, Yamaguchi K, Kondo K date 1989 title A new NAD dependent opine dehydrogenase from Arthrobacter sp strain 1C journal J. Bacteriol. volume 171 pages 4466&ndash 71 pmid 2753861 issue 8 pmc 210226 cite journal author Dairi T, Asano Y date 1995 title Cloning, nucleotide sequencing, and expression of an opine dehydrogenase gene from Arthrobacter sp. strain 1C journal Appl. Environ. Microbiol. volume 61 pages 3169&ndash 71 pmid 7487048 issue 8 pmc 167592 cite journal author Kato Y, Yamada H and Asano Y date 1996 title Stereoselective synthesis of opine type secondary amine carboxylic acids by a new enzyme opine dehydrogenase. Use of recombinant enzymes journal J. Mol. Catal., B Enzym. volume 1 pages 151&ndash 160 doi 10.1016 1381 1177 95 00011 9 issue 3 6 1.5 enzyme stub Category EC 1.5.1 Category NADH dependent enzymes Category ... more details
enzyme Name glycerate dehydrogenase EC number 1.1.1.29 CAS number 9028 37 9 IUBMB EC number 1 1 1 29 GO code 0008465 image width caption In enzymology , a glycerate dehydrogenase EC number 1.1.1.29 is an enzyme that catalysis catalyzes the chemical reaction R glycerate NAD sup sup math rightleftharpoons math hydroxypyruvate NADH H sup sup Thus, the two substrate biochemistry substrates of this enzyme are R glycerate and nicotinamide adenine dinucleotide NAD sup sup , whereas its 3 product chemistry products are hydroxypyruvate , nicotinamide adenine dinucleotide NADH , and hydrogen ion H sup sup . This enzyme belongs to the family of oxidoreductase s, specifically those acting on the CH OH group of donor with NAD or NADP as acceptor. The systematic name of this enzyme class is R glycerate NAD oxidoreductase . Other names in common use include D glycerate dehydrogenase , and hydroxypyruvate reductase . This enzyme participates in glycine, serine and threonine metabolism and glyoxylate and dicarboxylate metabolism . Structural studies As of late 2007, only one tertiary structure structure has been solved for this class of enzymes, with the Protein Data Bank PDB accession code PDB link 1GDH . References reflist 1 cite journal author HOLZER H, HOLLDORF A date 1957 title Isolation of D glycerate dehydrogenase, some properties of the enzyme and its application to the enzymic optic determination of hydroxypyruvate in presence of pyruvate. journal Biochem. Z. volume 329 pages 292 312 pmid 13522707 issue 4 cite journal author STAFFORD HA, MAGALDI A, VENNESLAND B date 1954 title The enzymatic reduction of hydroxypyruvic acid to D glyceric acid in higher plants journal J. Biol. Chem. volume 207 pages 621 9 pmid 13163046 issue 2 1.1.1 enzyme stub Category EC 1.1.1 Category NADH dependent enzymes Category Enzymes of known structure it Glicerato deidrogenasi ja ... more details
enzyme Name lactaldehyde dehydrogenase EC number 1.2.1.22 CAS number 37250 90 1 IUBMB EC number 1 2 1 22 GO code 0008911 image width caption In enzymology , a lactaldehyde dehydrogenase EC number 1.2.1.22 is an enzyme that catalysis catalyzes the chemical reaction S lactaldehyde NAD sup sup H sub 2 sub O math rightleftharpoons math S lactate NADH 2 H sup sup The 3 substrate biochemistry substrates of this enzyme are S lactaldehyde , nicotinamide adenine dinucleotide NAD sup sup , and water H sub 2 sub O , whereas its 3 product chemistry products are S lactate , nicotinamide adenine dinucleotide NADH , and hydrogen ion H sup sup . This enzyme belongs to the family of oxidoreductase s, specifically those acting on the aldehyde or oxo group of donor with NAD or NADP as acceptor. The systematic name of this enzyme class is S lactaldehyde NAD oxidoreductase . Other names in common use include L lactaldehyde NAD oxidoreductase , and nicotinamide adenine dinucleotide NAD linked dehydrogenase . This enzyme participates in pyruvate metabolism . Structural studies As of late 2007, 4 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 2HG2 , PDB link 2ILU , PDB link 2IMP , and PDB link 2OPX . References reflist 1 cite journal author Rembold H, Simmersbach F date 1969 title Catabolism of pteridine cofactors. II. A specific pterin deaminase in rat liver journal Biochim. Biophys. Acta. volume 184 pages 589&ndash 96 pmid 5821022 issue 3 cite journal author Sridhara S, Wu TT date 1969 title Purification and properties of lactaldehyde dehydrogenase from Escherichia coli journal J. Biol. Chem. volume 244 pages 5233&ndash 8 pmid 4310089 issue 19 1.2 enzyme stub Category EC 1.2.1 Category NADH dependent enzymes Category Enzymes of known structure it Lattaldeide deidrogenasi ja ... more details
enzyme Name Malate dehydrogenase EC number 1.1.1.37 CAS number 9001 64 3 IUBMB EC number 1 1 1 37 GO code image Malate dehydrogenase structure.png width caption Structure of the protein with attached sugars Malate dehydrogenase EC number 1.1.1.37 MDH is an enzyme that reversible reaction reversibly catalyzes ... s, including the citric acid cycle . Other malate dehydrogenase s, which have other EC numbers and catalyze other reactions oxidizing malate, have qualified names like malate dehydrogenase NADP . Malate dehydrogenase is also involved in gluconeogenesis , the synthesis of glucose from smaller molecules. Pyruvate in the mitochondria is acted upon by pyruvate carboxylase to form oxaloacetate, a citric acid cycle intermediate. In order to get the oxaloacetate out of the mitochondria, malate dehydrogenase ..., the malate is oxidized back to oxaloacetate by cytosolic malate dehydrogenase. Finally, phosphoenolpyruvate ... isozymes of malate dehydrogenase exist. There are two main isoforms in eukaryotic cells. ref cite .... ref cite journal author Musrati RA, Koll rov M, Mernik N, Mikul sov D title Malate dehydrogenase ... two malate dehydrogenases table tr td protein Name malate dehydrogenase 1, NAD soluble caption ... malate dehydrogenase 2 , NAD mitochondrial caption image width HGNCid 6971 Symbol Malate dehydrogenase ... organisms, malate dehydrogenase exists as a homodimeric molecule and is closely related to lactate dehydrogenase in structure. It is a large protein molecule with subunits weighing between 30 and 35 ... Malate dehydrogenase chapterurl ref Based on the amino acid sequences, it seems that MDH has diverged ... Malate dehydrogenase a model for structure, evolution, and catalysis journal Protein Sci. volume 3 issue ... ref Because the sequence identity of malate dehydrogenase in the mitochondria is more closely related ... linkage between lactate dehydrogenase and malate dehydrogenase. ref cite journal author Cendrin ... coli of the gene coding for malate dehydrogenase of the extremely halophilic archaebacterium ... more details
DHAP to glycerol 3 phosphate G3P by G3P dehydrogenase, followed by dephosphorylation to glycerol by G3Pase. E The lower part of glycolysis converts GAP to pyruvate while generating 1 NADH and 2 ATP via a series of 5 enzymes. F Alcoholic fermentation decarboxylation of pyruvate by pyruvate decarboxylase, followed by reduction of acetaldehyde to ethanol. G mitochondrial pyruvatedehydrogenase converts ...enzyme Name Glycerol 3 phosphate dehydrogenase NAD sup sup EC number 1.1.1.8 CAS number 9075 65 4 IUBMB EC number 1 1 1 8 GO code 0004367 image Glycerol 3 phosphate dehydrogenase 1.png width caption Crystallographic structure of human glycerol 3 phosphate dehydrogenase 1. ref name pmid16460752 PDB 1X0V ... structures of human glycerol 3 phosphate dehydrogenase 1 GPD1 journal J. Mol. Biol. volume 357 issue ... Name Glycerol 3 phosphate dehydrogenase quinone EC number 1.1.5.3 CAS number 9001 49 4 IUBMB EC ... glycerol 3 phosphate dehydrogenase N terminus image PDB 1bg6 EBI.jpg width caption crystal structure of the n 1 d carboxylethyl l norvaline dehydrogenase from arthrobacter sp. strain 1c Pfam PF01210 ... dehydrogenase C terminus image PDB 1txg EBI.jpg width caption structure of glycerol 3 phosphate dehydrogenase from archaeoglobus fulgidus Pfam PF07479 Pfam clan CL0106 InterPro IPR006109 SMART PROSITE PDOC00740 MEROPS SCOP 1m66 TCDB OPM family OPM protein CAZy CDD Glycerol 3 phosphate dehydrogenase ..., Rao Zihe title Crystal Structures of Human Glycerol 3 phosphate Dehydrogenase 1 GPD1 journal Journal ... May 2011 doi 10.1016 j.jmb.2005.12.074 pmid 16460752 ref Glycerol 3 phosphate dehydrogenase serves as a major ... dehydrogenase include alpha glycerol 3 phosphate dehydrogenase alphaGPDH and glycerolphosphate dehydrogenase GPDH . However, glycerol 3 phosphate dehydrogenase is not the same as glyceraldehyde 3 phosphate dehydrogenase GAPDH whose substrate is an aldehyde not an alcohol . Metabolic Function GPDH ..., Eric A. Copeland, Eric S. White III, Harold B. title Role of Glycerol 3 Phosphate Dehydrogenase ... more details
Lahfa N, Forterre P, Labedan B title Evolution of glutamate dehydrogenase genes evidence ... phosphate dependent glutamate dehydrogenase journal J. Biol. Chem. volume 260 issue 14 pages 8502 ... of cDNA clones encoding human liver glutamate dehydrogenase evidence for a small gene ... 3368458 pmc 280238 doi 10.1073 pnas.85.10.3494 url ref Leucine dehydrogenase EC number 1.4.1.9 LeuDH ... of leucine dehydrogenase from Bacillus stearothermophilus and structural comparison with other ... of the catalytic cycle . Phenylalanine dehydrogenase EC number 1.4.1.20 PheDH is an NAD dependent enzyme that catalyses the reversible deamidation of L phenylalanine into phenyl pyruvate. ref name pmid1880121 ... phenylalanine dehydrogenase of Thermoactinomyces intermedius cloning, expression, and sequencing of its ... ref Valine dehydrogenase EC number 1.4.1.8 ValDH is an NADP dependent enzyme that catalyses the reversible ... chain amino acid dehydrogenase gene of Streptomyces coelicolor journal J. Bacteriol. volume ... more details
enzyme Name pyruvate kinase phosphatase EC number 3.1.3.49 CAS number 79986 25 7 IUBMB EC number 3 1 3 49 GO code 0050408 image width caption In enzymology , a pyruvate kinase phosphatase EC number 3.1.3.49 is an enzyme that catalysis catalyzes the chemical reaction pyruvate kinase phosphate H sub 2 sub O math rightleftharpoons math pyruvate kinase phosphate Thus, the two substrate biochemistry substrates of this enzyme are pyruvate kinase phosphate and water H sub 2 sub O , whereas its two product chemistry products are pyruvate kinase and phosphate . This enzyme belongs to the family of hydrolase s, specifically those acting on phosphoric ester monoester bonds. The systematic name of this enzyme class is ATP pyruvate 2 O phosphotransferase phosphate phosphohydrolase . This enzyme is also called pyruvate kinase phosphatase . References reflist 1 cite journal author Jett MF, Hue L, Hers HG date 1981 title Pyruvate kinase phosphatase journal FEBS. Lett. volume 132 pages 183&ndash 6 pmid 6271587 doi 10.1016 0014 5793 81 81156 8 issue 2 DEFAULTSORT Pyruvate Kinase Phosphatase Category EC 3.1.3 Category Enzymes of unknown structure hydrolase stub ... more details
enzyme Name Lactate dehydrogenase EC number 1.1.1.27 CAS number 9001 60 9 IUBMB EC number 1 1 1 27 GO code 0004459 image width caption protein Name LDHA lactate dehydrogenase A br subunit M caption Human lactate dehydrogenase M sub 4 sub the isoenzyme found in skeletal muscle . From PDB 1I10 . image Lactate dehydrogenase M4 muscle 1I10.png width HGNCid 6535 Symbol LDHA AltSymbols LDHM EntrezGene 3939 ... protein Name lactate dehydrogenase B br subunit H caption image width HGNCid 6541 ... 1.1.1.27 Chromosome 12 Arm p Band 12.2 12.1 LocusSupplementaryData protein Name lactate dehydrogenase ... Infobox protein family Symbol Lact deh memb Name D lactate dehydrogenase, membrane binding image PDB 1f0x EBI.jpg width caption crystal structure of d lactate dehydrogenase, a peripheral membrane ... TCDB OPM family OPM protein CAZy CDD Lactate dehydrogenase LDH or LD is an enzyme EC number 1.1.1.27 ... D lactate D lactate dehydrogenase cytochrome EC 1.1.2.4 or L lactate L lactate dehydrogenase cytochrome ... or L lactate EC 1.1.1.27 . This article is about the NAD P dependent L lactate dehydrogenase. Reactions File LDH reaction.png center thumb 355px Catalytic function of LDH Lactate dehydrogenase catalyzes the interconversion of pyruvate and lactic acid lactate with concomitant interconversion of NADH and Nicotinamide adenine dinucleotide NAD sup sup . It converts pyruvate, the final product of glycolysis ... inhibition, and the rate of conversion of pyruvate to lactate is decreased. It also catalyzes ... ref Ethanol Induced Hypoglycemia Ethanol is dehydrogenated to acetaldehyde by alcohol dehydrogenase, and further into acetic acid by acetaldehyde dehydrogenase. During this reaction 2 NADH are produced ... of NAD sup sup . Thus, the conversion of pyruvate to lactate is increased due to the associated ... acidosis may ensue in ethanol poisoning. Enzyme isoforms Functional lactate dehydrogenase are homo ... of lactate dehydrogenase in cerebrospinal fluid are often associated with bacterium bacteria l meningitis ... more details
dehydrogenase plays an important part in fermentation pyruvate resulting from glycolysis is converted ..., acetaldehyde dehydrogenase acetylating EC number 1.2.1.10 and pyruvate formate lyase deactivase. Bacteria ...enzyme Name alcohol dehydrogenase EC number 1.1.1.1 IUBMB EC number 1 1 1 1 CAS number 9031 72 5 GO code ... PC, Robinson H, Bosron WF, Hurley TD title Human glutathione dependent formaldehyde dehydrogenase ... dehydrogenases ADH EC number 1.1.1.1 are a group of dehydrogenase enzyme s that occur in many organisms ... dehydrogenase , identical to a ADH5 class III alcohol dehydrogenase ADH 3 ADH5 , probably is the ancestral ... H title Enzymogenesis classical liver alcohol dehydrogenase origin from the glutathione dependent formaldehyde dehydrogenase line journal Proc. Natl. Acad. Sci. U.S.A. volume 89 issue 19 pages ... cite journal author Persson B, Hedlund J, J rnvall H title Medium and short chain dehydrogenase ..., H g JO title Medium and short chain dehydrogenase reductase gene and protein families Dual functions of alcohol dehydrogenase 3 implications with focus on formaldehyde dehydrogenase and S nitrosoglutathione ... Liver Alcohol Dehydrogenase The first ever isolated alcohol dehydrogenase ADH was purified in 1937 ... author Theorell H, McKee JS title Mechanism of action of liver alcohol dehydrogenase journal Nature ... Horse liver alcohol dehydrogenase. On the primary structure of the ethanol active isoenzyme journal ... dehydrogenase at 2.9 angstrom resolution journal Proc. Natl. Acad. Sci. U.S.A. volume 70 issue 8 pages ... ref name isbn978 91 7409 567 8 cite book author Hellgren M title Enzymatic studies of alcohol dehydrogenase ... of alcohol dehydrogenase gene expression in Drosophila journal Annual Review of Genetics volume ... the coenzyme nicotinamide adenine dinucleotide NAD sup sup and cofactor PQQ . Alcohol dehydrogenase ... dehydrogenase The active site consists of a zinc atom, His 67, Cys 174, Cys 46, Ser 48, His 51 ... binding motif in alcohol dehydrogenase from a MD simulation Mammalian alcohol dehydrogenases also have ... more details
enzyme Name pyruvate, phosphate dikinase EC number 2.7.9.1 CAS number 9027 40 1 IUBMB EC number 2 7 9 1 GO code 0050242 image width caption File PPDK reaction.svg thumb 350px Reaction of the pyruvate, phosphate dikinase the phosphorylation of pyruvate to phosphoenolpyruvate. In enzymology , a pyruvate, phosphate dikinase EC number 2.7.9.1 is an enzyme that catalysis catalyzes the chemical reaction ATP pyruvate phosphate math rightleftharpoons math AMP phosphoenolpyruvate diphosphate The 3 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , pyruvate , and phosphate , whereas its 3 product chemistry products are adenosine monophosphate AMP , phosphoenolpyruvate PEP , and diphosphate . With that enzyme, bacteria can also form ATP if the reaction is running backwards ... Mariano D title Analysis of sequence homologies in plant and bacterial pyruvate phosphate dikinase ... performed by pyruvate kinase in Embden Meyerhof Parnas glycolysis. It should not be confused with pyruvate ... name of this enzyme class is ATP pyruvate, phosphate phosphotransferase . Other names in common use include pyruvate, orthophosphate dikinase , pyruvate phosphate dikinase phosphorylating , pyruvate, phosphate dikinase , pyruvate inorganic phosphate dikinase , pyruvate phosphate dikinase , pyruvate phosphate ligase , pyruvic phosphate dikinase , pyruvic phosphate ligase , pyruvate, Pi dikinase , and PPDK . This enzyme participates in pyruvate metabolism and carbon fixation . PPDK has been shown to undergo light dark regulation by the pyruvate dikinase regulatory protein PDRP . PDRP reversibly ... CR date 1968 title A new enzyme for the interconversion of pyruvate and phosphopyruvate and its role ... function of pyruvate kinase journal J. Biol. Chem. volume 243 pages 3202&ndash 4 pmid 4297474 issue 11 cite journal author Reeves RE date 1971 title Pyruvate,phosphate dikinase from ... cite journal author Reeves RE, Menzies RA, Hsu DS date 1968 title The pyruvate phosphate dikinase ... more details
enzyme Name R 3 amino 2 methylpropionate pyruvate transaminase EC number 2.6.1.40 CAS number 37279 00 8 IUBMB EC number 2 6 1 40 GO code 0047305 image width caption In enzymology , a R 3 amino 2 methylpropionate pyruvate transaminase EC number 2.6.1.40 is an enzyme that catalysis catalyzes the chemical reaction R 3 amino 2 methylpropanoate pyruvate math rightleftharpoons math 2 methyl 3 oxopropanoate L alanine Thus, the two substrate biochemistry substrates of this enzyme are R 3 amino 2 methylpropanoate and pyruvate , whereas its two product chemistry products are 2 methyl 3 oxopropanoate and L alanine . This enzyme belongs to the family of transferase s, specifically the transaminases , which transfer nitrogenous groups. The systematic name of this enzyme class is R 3 amino 2 methylpropanoate pyruvate aminotransferase . Other names in common use include D 3 aminoisobutyrate pyruvate transaminase , beta aminoisobutyrate pyruvate aminotransferase , D 3 aminoisobutyrate pyruvate aminotransferase , D 3 aminoisobutyrate pyruvate transaminase , R 3 amino 2 methylpropionate transaminase , and D beta aminoisobutyrate pyruvate aminotransferase . References reflist 1 cite journal author Kakimoto Y, Taniguchi K, Sano I year 1969 title D beta aminoisobutyrate pyruvate aminotransferase in mammalian liver and excretion of beta aminoisobutyrate by man journal J. Biol. Chem. volume 244 pages 335&ndash 40 pmid 5773299 issue 2 cite journal author Tamaki N, Sakata SF, Matsuda K year 2000 title Purification, properties, and sequencing of aminoisobutyrate aminotransferases from rat liver journal Methods Enzymol. volume 324 pages 376&ndash 89 pmid 10989446 doi 10.1016 S0076 6879 00 24247 X Category EC 2.6.1 Category Enzymes of unknown structure transferase stub ... more details
enzyme Name Arginine pyruvate transaminase EC number 2.6.1.84 CAS number IUBMB EC number 2 6 1 84 GO code image width caption Orphan date February 2009 In enzymology , an arginine pyruvate transaminase EC number 2.6.1.84 is an enzyme that catalysis catalyzes the chemical reaction L arginine pyruvate math rightleftharpoons math 5 guanidino 2 oxopentanoate L alanine Thus, the two substrate biochemistry substrates of this enzyme are L arginine and pyruvate , whereas its two product chemistry products are 5 guanidino 2 oxopentanoate and L alanine . This enzyme belongs to the family of transferase s, specifically the transaminases , which transfer nitrogenous groups. The systematic name of this enzyme class is L arginine pyruvate aminotransferase . Other names in common use include arginine pyruvate transaminase , and AruH . References reflist 1 cite journal author Yang Z, Lu CD date 2007 title Characterization of an arginine pyruvate transaminase in arginine catabolism of Pseudomonas aeruginosa PAO1 journal J. Bacteriol. volume 189 pages 3954&ndash 9 pmid 17416668 doi 10.1128 JB.00262 07 issue 11 pmc 1913410 cite journal author Yang Z, Lu CD date 2007 title Functional genomics enables identification of genes of the arginine transaminase pathway in Pseudomonas aeruginosa journal J. Bacteriol. volume 189 pages 3945&ndash 53 pmid 17416670 doi 10.1128 JB.00261 07 issue 11 pmc 1913404 transferase stub Category EC 2.6.1 Category Enzymes of unknown structure ... more details
enzyme Name lysine pyruvate 6 transaminase EC number 2.6.1.71 CAS number 114189 79 6 IUBMB EC number 2 6 1 71 GO code 0050065 image width caption In enzymology , a lysine pyruvate 6 transaminase EC number 2.6.1.71 is an enzyme that catalysis catalyzes the chemical reaction L lysine pyruvate math rightleftharpoons math L 2 aminoadipate 6 semialdehyde L alanine Thus, the two substrate biochemistry substrates of this enzyme are L lysine and pyruvate , whereas its two product chemistry products are L 2 aminoadipate 6 semialdehyde and L alanine . This enzyme belongs to the family of transferase s, specifically the transaminases , which transfer nitrogenous groups. The systematic name of this enzyme class is L lysine pyruvate aminotransferase . Other names in common use include lysine pyruvate aminotransferase , and Lys AT . References reflist 1 cite journal author Schmidt H, Bode R and Birnbaum D date 1988 title A novel enzyme, L lysine pyruvate aminotransferase, catalyses the first step of lysine catabolism in Pichia guilliermondii journal FEMS Microbiol. Lett. volume 49 pages 203&ndash 206 transferase stub Category EC 2.6.1 Category Enzymes of unknown structure ... more details
enzyme Name pyruvate oxidase CoA acetylating EC number 1.2.3.6 CAS number 62213 57 4 IUBMB EC number 1 2 3 6 GO code 0050244 image width caption In enzymology , a pyruvate oxidase CoA acetylating EC number 1.2.3.6 is an enzyme that catalysis catalyzes the chemical reaction pyruvate CoA O sub 2 sub math rightleftharpoons math acetyl CoA CO sub 2 sub H sub 2 sub O sub 2 sub The 3 substrate biochemistry substrates of this enzyme are pyruvate , coenzyme A CoA , and oxygen O sub 2 sub , whereas its 3 product chemistry products are acetyl CoA , carbon dioxide CO sub 2 sub , and hydrogen peroxide H sub 2 sub O sub 2 sub . This enzyme belongs to the family of oxidoreductase s, specifically those acting on the aldehyde or oxo group of donor with oxygen as acceptor. The systematic name of this enzyme class is pyruvate oxygen 2 oxidoreductase CoA acetylating . This enzyme participates in pyruvate metabolism . It employs one cofactor biochemistry cofactor , FAD . References reflist 1 cite journal author Reeves RE, Warren LG, Susskind B, Lo HS date 1977 title An energy conserving pyruvate to acetate pathway in Entamoeba histolytica. Pyruvate synthase and a new acetate thiokinase journal J. Biol. Chem. volume 252 pages 726&ndash 31 pmid 13076 issue 2 cite journal author Takeuchi T, Weinbach EC, Diamond LS date 1975 title Pyruvate oxidase CoA acetylating in Entamoeba histolytica journal Biochem. Biophys. Res. Commun. volume 65 pages 591&ndash 6 pmid 167776 doi 10.1016 S0006 291X 75 80187 2 issue 2 1.2 enzyme stub Category EC 1.2.3 Category Flavin enzymes Category Enzymes of unknown structure it Piruvato ossidasi CoA acetilante ja CoA ... more details
enzyme Name diaminobutyrate pyruvate transaminase EC number 2.6.1.46 CAS number 37277 95 5 IUBMB EC number 2 6 1 46 GO code 0047307 image width caption In enzymology , a diaminobutyrate pyruvate transaminase EC number 2.6.1.46 is an enzyme that catalysis catalyzes the chemical reaction L 2,4 diaminobutanoate pyruvate math rightleftharpoons math L aspartate 4 semialdehyde L alanine Thus, the two substrate biochemistry substrates of this enzyme are L 2,4 diaminobutanoate and pyruvate , whereas its two product chemistry products are L aspartate 4 semialdehyde and L alanine . This enzyme belongs to the family of transferase s, specifically the transaminases , which transfer nitrogenous groups. The systematic name of this enzyme class is L 2,4 diaminobutanoate pyruvate aminotransferase . Other names in common use include diaminobutyrate pyruvate aminotransferase , and L diaminobutyric acid transaminase . It employs one cofactor biochemistry cofactor , pyridoxal phosphate . References reflist 1 cite journal author Rao DR, Hariharan K, Vijayalakshmi KR date 1969 title A study of the metabolism of L alpha gamma diaminobutyric acid in a Xanthomonas species journal Biochem. J. volume 114 pages 107&ndash 15 pmid 4390206 issue 1 pmc 1184802 transferase stub Category EC 2.6.1 Category Pyridoxal phosphate enzymes Category Enzymes of unknown structure ... more details
enzyme Name pyridoxamine pyruvate transaminase EC number 2.6.1.30 CAS number 9023 38 5 IUBMB EC number 2 6 1 30 GO code 0047300 image width caption In enzymology , a pyridoxamine pyruvate transaminase EC number 2.6.1.30 is an enzyme that catalysis catalyzes the chemical reaction pyridoxamine pyruvate math rightleftharpoons math pyridoxal L alanine Thus, the two substrate biochemistry substrates of this enzyme are pyridoxamine and pyruvate , whereas its two product chemistry products are pyridoxal and L alanine . This enzyme belongs to the family of transferase s, specifically the transaminases , which transfer nitrogenous groups. The systematic name of this enzyme class is pyridoxamine pyruvate aminotransferase . This enzyme is also called pyridoxamine pyruvic transaminase . This enzyme participates in vitamin B6 vitamin B sub 6 sub metabolism . References reflist 1 cite journal author Wada H and Snell EE date 1962 title Enzymatic transamination of pyridoxamine. II. Crystalline pyridoxamine pyruvate transaminase journal J. Biol. Chem. volume 237 pages 133&ndash 137 pmid 14004227 transferase stub Category EC 2.6.1 Category Enzymes of unknown structure ... more details
enzyme Name valine pyruvate transaminase EC number 2.6.1.66 CAS number 132421 38 6 IUBMB EC number 2 6 1 66 GO code 0009042 image width caption In enzymology , a valine pyruvate transaminase EC number 2.6.1.66 is an enzyme that catalysis catalyzes the chemical reaction L valine pyruvate math rightleftharpoons math 3 methyl 2 oxobutanoate L alanine Thus, the two substrate biochemistry substrates of this enzyme are L valine and pyruvate , whereas its two product chemistry products are 3 methyl 2 oxobutanoate and L alanine . This enzyme belongs to the family of transferase s, specifically the transaminases , which transfer nitrogenous groups. The systematic name of this enzyme class is L valine pyruvate aminotransferase . Other names in common use include transaminase C , valine pyruvate aminotransferase , and alanine oxoisovalerate aminotransferase . This enzyme participates in valine, leucine and isoleucine biosynthesis . References reflist 1 cite journal author Falkinham JO 3rd date 1979 title Identification of a mutation affecting an alanine alpha ketoisovalerate transaminase activity in Escherichia coli K 12 journal Mol. Gen. Genet. volume 176 pages 147&ndash 9 pmid 396446 doi 10.1007 BF00334306 issue 1 cite journal author RUDMAN D, MEISTER A date 1953 title Transamination in Escherichia coli journal J. Biol. Chem. volume 200 pages 591&ndash 604 pmid 13034817 issue 2 transferase stub Category EC 2.6.1 Category Enzymes of unknown structure ... more details
Infobox Disease Name Pyruvate carboxylase deficiency Image Oxaloacetic acid.png Caption Oxaloacetate is the product of pyruvate carboxylase DiseasesDB 7378 ICD10 ICD10 E 74 4 e 70 ICD9 ICD9 271.8 ICDO OMIM 266150 MedlinePlus eMedicineSubj med eMedicineTopic 1979 eMedicine mult eMedicine2 ped 1967 MeshID D015324 Pyruvate carboxylase deficiency is an inherited disorder that causes lactic acid and other potentially toxic compounds to accumulate in the blood . High levels of these substances can damage the body s organs and tissues, particularly in the nervous system. Pyruvate carboxylase deficiency is a rare condition, with an estimated incidence of 1 in 250,000 births worldwide. This disorder appears ... needed date December 2007 Classification Researchers have identified at least three types of pyruvate .... Children with pyruvate carboxylase deficiency type A typically survive only into early childhood. Type B Pyruvate carboxylase deficiency type B has life threatening signs and symptoms that become apparent ... for less than 3 months after birth. Genetics Image autorecessive.svg thumb right Pyruvate carboxylase ... gene cause pyruvate carboxylase deficiency. The PC gene provides instructions for making an enzyme called pyruvate carboxylase . This enzyme is active in mitochondria , which are the energy producing ... of glucose , a simple sugar that is the body s main energy source. Pyruvate carboxylase also plays ... of pyruvate carboxylase in cells or disrupt the enzyme s activity. The missing or altered enzyme cannot ... in mitochondria. Additionally, a loss of pyruvate carboxylase allows potentially toxic compounds ... of pyruvate carboxylase function in the nervous system, particularly the role of the enzyme in myelin formation and neurotransmitter production, also contributes to the neurologic features of pyruvate ...?book gene&part pdc GeneReview NCBI NIH UW entry on Pyruvate Carboxylase Deficiency See also NLM ... Pyruvate Carboxylase Deficiency Category Autosomal recessive disorders Category Inborn errors of carbohydrate ... more details
enzyme Name 2,2 dialkylglycine decarboxylase pyruvate EC number 4.1.1.64 CAS number 9032 17 1 IUBMB EC number 4 1 1 64 GO code 0047432 image width caption In enzymology , a 2,2 dialkylglycine decarboxylase pyruvate EC number 4.1.1.64 is an enzyme that catalysis catalyzes the chemical reaction 2,2 dialkylglycine pyruvate math rightleftharpoons math dialkyl ketone CO sub 2 sub L alanine Thus, the two substrate biochemistry substrates of this enzyme are 2,2 dialkylglycine and pyruvate , whereas its 3 product chemistry products are dialkyl ketone , carbon dioxide CO sub 2 sub , and L alanine . This enzyme belongs to the family of lyase s, specifically the carboxy lyases, which cleave carbon carbon bonds. The systematic name of this enzyme class is 2,2 dialkylglycine carboxy lyase amino transferring L alanine forming . Other names in common use include dialkyl amino acid pyruvate decarboxylase , alpha dialkyl amino acid transaminase , 2,2 dialkyl 2 amino acid pyruvate aminotransferase , L alanine alpha ketobutyrate aminotransferase , dialkylamino acid decarboxylase pyruvate , and 2,2 dialkylglycine carboxy lyase amino transferring . It employs one cofactor biochemistry cofactor , pyridoxal phosphate . Structural studies As of late 2007, 16 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1D7R , PDB link 1D7S , PDB link 1D7U , PDB link 1D7V , PDB link 1DGD , PDB link 1DGE , PDB link 1DKA , PDB link 1M0N , PDB link 1M0O , PDB link 1M0P , PDB link 1M0Q , PDB link 1Z3Z , PDB link 1ZC9 , PDB link 1ZOB , PDB link 1ZOD , and PDB link 2DKB . References reflist 1 cite journal author Bailey GB and Dempsey WB year 1967 title Purification and properties of an alpha dialkyl amino acid transaminase journal Biochemistry volume 6 pages 1526&ndash 1533 doi 10.1021 bi00857a039 issue 5 DEFAULTSORT 2,2 Dialkylglycine Decarboxylase Pyruvate Category EC 4.1.1 Category Pyridoxal phosphate enzymes Category Enzymes of known ... more details
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