image PDwhole1.jpg width caption Crystallographic structure of pyruvatedehydrogenase PDH . PH is a six ... for flip flop action of thiamin pyrophosphate dependent enzymes revealed by human pyruvatedehydrogenase ... pmid 15264254 doi 10.1002 jcc.20084 url ref Pyruvatedehydrogenase E1 is the first component enzyme of pyruvatedehydrogenase complex PDC . The pyruvatedehydrogenase complex contributes to transforming ... in the citric acid cycle to carry out cellular respiration , so pyruvatedehydrogenase contributes ... adenine dinucleotide NADH . EC number 1.2.4.1 . Function Pyruvatedehydrogenase E1 performs the first two reactions within the pyruvatedehydrogenase complex PDC a decarboxylation of substrate .... The reaction catalyzed by pyruvatedehydrogenase E1 is considered to be the rate limiting step for the pyruvatedehydrogenase complex PDHc . Regulation Phosphorylation of E1 by pyruvatedehydrogenase kinase PDK inactivates E1 and subsequently the entire complex. This is reversed by pyruvatedehydrogenase phosphatase . Pyruvatedehydrogenase phosphatase is stimulated by insulin , Phosphoenolpyruvate ... Dehydrogenase Mechanism File PyruvateDehydrgenaseMech1.gif PyruvateDehydrogenase Mechanism The ylide ... for flip flop action of thiamin pyrophosphate dependent enzymes revealed by human pyruvatedehydrogenase ... bichaw 2002 41 i16 abs bi0118557.html doi 10.1021 bi0118557 ref File Pyruvatedehydrogenase E1 subunit of E. coli 2000 pixels .png thumb Pyruvatedehydrogenase E1 subunit of E. coli. Colors ... The active site for pyruvatedehydrogenase image created from PDB 1NI4 holds TPP through metal ligation ... revealed by human pyruvatedehydrogenase journal J. Biol. Chem. volume 278 issue 23 pages 21240 ... Pyruvatedehydrogenase is an autoantigen recognized in primary biliary cirrhosis . These antibodies ... complex , which are antigens recognized by anti mitochondrial antibodies . Pyruvatedehydrogenase ... J. Benke. PyruvateDehydrogenase Complex Deficiency. EMedicine. 11 Dec. 2007. WebMD. 14 Dec ... more details
enzyme Name pyruvatedehydrogenase cytochrome EC number 1.2.2.2 CAS number 9079 84 9 IUBMB EC number 1 2 2 2 GO code 0008985 image width caption In enzymology , a pyruvatedehydrogenase cytochrome EC number 1.2.2.2 is an enzyme that catalysis catalyzes the chemical reaction pyruvate ferricytochrome b sub 1 sub H sub 2 sub O math rightleftharpoons math acetate CO sub 2 sub ferrocytochrome b sub 1 sub The 3 substrate biochemistry substrates of this enzyme are pyruvate , ferricytochrome b1 , and water H sub 2 sub O , whereas its 3 product chemistry products are acetate , carbon dioxide CO sub 2 sub , and ferrocytochrome b1 . This enzyme belongs to the family of oxidoreductase s, specifically those acting on the aldehyde or oxo group of donor with a cytochrome as acceptor. The systematic name of this enzyme class is pyruvate ferricytochrome b1 oxidoreductase . Other names in common use include pyruvatedehydrogenase , pyruvic dehydrogenase , pyruvic cytochrome b1 dehydrogenase , pyruvate ubiquinone 8 oxidoreductase , and pyruvate oxidase ambiguous . This enzyme participates in pyruvate metabolism . It has 2 cofactor biochemistry cofactors FAD , and Thiamin diphosphate . References reflist 1 cite journal author Williams FR and Hager LP date 1961 title A crystalline flavin pyruvate oxidase journal J. Biol. Chem. volume 236 pages PC36&ndash PC37 cite journal author Koland JG, Gennis RB date 1982 title Identification of an active site cysteine residue in Escherichia coli pyruvate oxidase journal J. Biol. Chem. volume 257 pages 6023&ndash 7 pmid 7042705 issue 11 1.2 enzyme stub Category EC 1.2.2 Category Flavin enzymes Category Thiamin diphosphate enzymes Category Enzymes of unknown structure it Piruvato deidrogenasi citocromo ... more details
enzyme Name pyruvatedehydrogenase acetyl transferring EC number 1.2.4.1 CAS number 9014 20 4 IUBMB EC number 1 2 4 1 GO code 0004739 image width caption In enzymology , a pyruvatedehydrogenase acetyl transferring EC number 1.2.4.1 is an enzyme that catalysis catalyzes the chemical reaction pyruvate dihydrolipoyllysine residue acetyltransferase lipoyllysine math rightleftharpoons math dihydrolipoyllysine residue acetyltransferase S acetyldihydrolipoyllysine CO sub 2 sub Thus, the two substrate biochemistry substrates of this enzyme are pyruvate and dihydrolipoyllysine residue acetyltransferase lipoyllysine, whereas its 3 product chemistry products are dihydrolipoyllysine residue acetyltransferase , S acetyldihydrolipoyllysine , and carbon dioxide CO sub 2 sub . This enzyme belongs to the family of oxidoreductase s, specifically those acting on the aldehyde or oxo group of donor with a disulfide as acceptor. The systematic name of this enzyme class is pyruvate dihydrolipoyllysine residue acetyltransferase lipoyllysine 2 oxidoreductase decarboxylating, acceptor acetylating . Other names in common use include MtPDC mitochondrial pyruvate dehydogenase complex , pyruvate decarboxylase , pyruvatedehydrogenase , pyruvatedehydrogenase lipoamide , pyruvatedehydrogenase complex , pyruvate lipoamide 2 oxidoreductase decarboxylating and , acceptor acetylating , pyruvic acid dehydrogenase , and pyruvic dehydrogenase . This enzyme participates in 5 metabolism metabolic pathways glycolysis gluconeogenesis , alanine and aspartate metabolism , valine, leucine and isoleucine biosynthesis , pyruvate metabolism , and butanoate metabolism . It employs one cofactor biochemistry cofactor , thiamin diphosphate . Structural studies As of late 2007, 12 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1L8A , PDB link 1NI4 , PDB link 1RP7 , PDB link 1W85 , PDB link 1W88 , PDB link 2G25 , PDB link 2G28 , PDB link 2G67 ... more details
Pyruvatedehydrogenase kinase also pyruvatedehydrogenase complex kinase , PDC kinase , or PDK EC number 2.7.11.2 is a kinase enzyme which acts to inactivate the enzyme pyruvatedehydrogenase by phosphorylate ... of the pyruvatedehydrogenase complex of which pyruvatedehydrogenase is the first component. Both PDK and the pyruvatedehydrogenase complex are located in the mitochondrial matrix of eukaryote s. The complex ... the dephosphorylation and activation of pyruvatedehydrogenase, is catalyzed by a phosphoprotein phosphatase called pyruvatedehydrogenase phosphatase . Pyruvatedehydrogenase kinase should not be confused ... Sites File Pyruvatedehydrogenase phosphorylation sites.png thumb The areas around the three ..., and site 3 in the bottom right. PDK can phosphorylate a serine residue on pyruvatedehydrogenase ... on pyruvatedehydrogenase from bovine kidney and heart. Biochemistry Vol. 17. Issue 12 1978 2364 ... that is responsible for pyruvatedehydrogenase deactivation. Isozymes There are four known isozymes ..., Zhao Y, Gudi R and Harris RA. Molecular Cloning of the p45 subunit of pyruvatedehydrogenase kinase ... change the reaction rates. ref Korotchkina L and Patel M. Site specificity of four pyruvatedehydrogenase kinase isoenzymes toward the three phosphorylation sites of human pyruvatedehydrogenase. J. Biol ... html ref ref Kolobova E, Tuganova A, Boulatnikov I, and Popov K. Regulation of pyruvatedehydrogenase ... of tissue specific regulation of the mammalian pyruvatedehydrogenase complex. Biochem. J. Vol ... dehydrogenase is deactivated when phosphorylated by PDK. Normally, the active site of pyruvatedehydrogenase .... ref Korotchkina LG and Patel MS. Probing the mechanism of inactivation of human pyruvatedehydrogenase ..., and Chuang DT. Structural basis for inactivation of human pyruvatedehydrogenase complex by phosphorylation ... requirement for ADP inhibition of pyruvatedehydrogenase kinase. Biochemical and Biophysical Research Communications. Vol. 59, Issue 4 1341 1348, Aug. 1974. ref Pyruvatedehydrogenase kinase is stimulated ... more details
Pyruvatedehydrogenase complex PDC is a complex of three enzyme s that transform pyruvate into acetyl CoA by a process called pyruvate decarboxylation . Acetyl CoA may then be used in the citric acid cycle ... acid cycle . Pyruvate decarboxylation is also known as the pyruvatedehydrogenase reaction ... by pyruvatedehydrogenase complex is Enzymatic Reaction foward enzyme pyruvatedehydrogenase complex ... product image acetyl co A wpmp.png Structure & function in eukaryotes Pyruvatedehydrogenase complex ..., W.G. 1992 Atomic structure of the cubic core of the pyruvatedehydrogenase multienzyme complex. Science 255, 1544 1550. ref Pyruvatedehydrogenase complex is located in the mitochondrial matrix of eukaryotes ... pyruvatedehydrogenase complex. J. Biol. Chem. 281, 19772 19780. ref class wikitable Enzyme Abbrev. cofactor biochemistry Cofactor s subunits prokaryotes subunits eukaryotes pyruvatedehydrogenase ... thumb 500px PDC Mechanism with pyruvate R H Pyruvatedehydrogenase E1 Initially, pyruvate and thiamine thiamine pyrophosphate TPP or thiamine vitamin B sub 1 sub are bound by pyruvatedehydrogenase ... process is the rate limiting step of the whole pyruvatedehydrogenase complex. Dihydrolipoyl ... FADH sub 2 sub back to its FAD resting state, producing NADH. Regulation Pyruvatedehydrogenase ... regulated by its own specific pyruvatedehydrogenase kinase PDK and pyruvatedehydrogenase ... transacetylase E2 . Up to 24 copies of Pyruvatedehydrogenase E1 and 12 molecules of dihydrolipoyl ... cerevisiae pyruvatedehydrogenase complex. J. Biol. Chem. 272, 5757 5764. ref However, it has ... in vivo and often reflects the metabolic requirements of the tissue in question. See also Pyruvatedehydrogenase ... of Leeds MeshName PyruvateDehydrogenase Complex 3D structures Cite pmid 11752427 , cow bovine kidney pyruvatedehydrogenase complex Cite doi 10.1016 j.str.2007.10.024 , human full length and truncated ... acid cycle enzymes Glycolysis DEFAULTSORT PyruvateDehydrogenase Complex Category EC 1.2.1 Category ... more details
PBB geneid 5162 Pyruvatedehydrogenase lipoamide beta , also known as pyruvatedehydrogenase E1 component ... . ref name entrez cite web title Entrez Gene pyruvatedehydrogenase lipoamide beta url http www.ncbi.nlm.nih.gov ... pyruvatedehydrogenase beta subunit gene journal Proc. Natl. Acad. Sci. U.S.A. volume 87 issue ... Function The pyruvatedehydrogenase PDH complex is a nuclear encoded mitochondrial multienzyme complex that catalyzes the overall conversion of pyruvate to acetyl CoA and CO sub 2 sub , and provides the primary ... is composed of multiple copies of three enzymatic components pyruvatedehydrogenase E1 , dihydrolipoyl transacetylase dihydrolipoamide acetyltransferase E2 and lipoamide dehydrogenase E3 . The E1 .... ref name entrez Clinical significance Mutations in this gene are associated with pyruvatedehydrogenase E1 beta deficiency. ref name entrez Interactive pathway map TCACycle WP78 highlight Pyruvatedehydrogenase lipoamide beta References reflist Further reading refbegin 2 cite journal author Ciszak ... dependent enzymes revealed by human pyruvatedehydrogenase journal J. Biol. Chem. volume ... families with pyruvatedehydrogenase deficiency journal Mol. Genet. Metab. volume 93 issue 4 pages 371 ... of pyruvatedehydrogenase deficiency journal Hum. Genet. volume 115 issue 2 pages 123 7 year 2004 pmid ... in mechanisms regulating glucose oxidation at the level of the pyruvatedehydrogenase complex ... 97 00411 3 cite journal author Korotchkina LG, Patel MS title Binding of pyruvatedehydrogenase to the core of the human pyruvatedehydrogenase complex journal FEBS Lett. volume 582 issue 3 pages 468 ... pyruvatedehydrogenase journal FEBS Lett. volume 437 issue 3 pages 273 7 year 1998 pmid 9824306 doi ... Pyruvatedehydrogenase complex deficiency caused by ubiquitination and proteasome mediated degradation ... of pyruvatedehydrogenase complex activity in muscle and liver cells journal J. Biol. Chem. volume 276 ... T, Aso Y, Roche TE title Organization of the cores of the mammalian pyruvatedehydrogenase complex ... more details
enzyme Name Pyruvatedehydrogenase NADP EC number 1.2.1.51 CAS number 93389 35 6 IUBMB EC number 1 2 1 51 GO code 0050243 image width caption Pyruvatedehydrogenase NADP sup sup EC number 1.2.1.51 is an enzyme that should not be confused with PyruvatedehydrogenasePyruvatedehydrogenase acetyltransferase EC number 1.2.4.1 . Sfn Inui 1984 pp 931 934 Sfn Inui 1987 pp 9130 9135 It catalyzes the following Chemical reaction reaction Pyruvic acid Pyruvate Coenzyme A Nicotinamide adenine dinucleotide phosphate NADP sup sup acetyl CoA NADPH Hydron chemistry H sup sup Carbon dioxide CO sub 2 sub References Reflist Bibliography Refbegin Cite journal ref SfnRef Ctrnacta 2006 authors Ctrnacta, V. Ault, J. G. Stejskal, F. Keithly, J. S. year 2006 title Localization of pyruvate NADP oxidoreductase in sporozoites of Cryptosporidium parvum journal J. Eukaryot. Microbiol. issue Issue 53 pages 225 231 Cite journal ref SfnRef Inui 1984 authors Inui, H. Miyatake, K. Nakano, Y. Kitaoka, S. year 1984 title Occurrence of oxygen sensitive, NADP dependent pyruvatedehydrogenase in mitochondria of Euglena gracilis ... sensitive pyruvatedehydrogenase in mitochondrial fatty acid synthesis in Euglena gracilis journal ... php result flat.php4?ecno 1.2.1.51 EC 1.2.1.51 pyruvatedehydrogenase NADP at Brenda enzymes.org http ..., H. Miyatake, K. Nakano, Y. Kitaoka, S. year 1989 title Pyruvate NADP oxidoreductase from Euglena ... 1990 title Pyruvate NADP oxidoreductase from Euglena gracilis mechanism of O2 inactivation of the enzyme ... 1987 title Purification and characterization of pyruvate NADP oxidoreductase in Euglena gracilis journal ... authors Inui, H. Yamaji, R. Saidoh, H. Miyatake, K. Nakano, Y. Kitaoka, S. year 1991 title Pyruvate ..., C. Fuchs, G. year 1990 title NADP specific 2 oxoglutarate dehydrogenase in denitrifying Pseudomonas ..., K. year 2000 title The origin of pyruvate NADP oxidoreductase in mitochondria of Euglena gracilis ..., M. Takenaka, S. Ueda, M. Inui, H. Nakano, Y. Miyatake, K. year 2003 title Pyruvate NADP oxidoreductase ... more details
Infobox disease Name PyruvateDehydrogenase Complex Deficiency Image Caption DiseasesDB 30060 ICD10 ICD10 E 74 4 e 70 ICD9 ICD9 271.8 ICDO OMIM 312170 MedlinePlus eMedicineSubj ped eMedicineTopic 1969 MeshID D015325 PyruvateDehydrogenase Deficiency PDH is one of the most common neurodegenerative disorders associated with abnormal mitochondrial metabolism. PDH deficiency is an X linked disease that shows heterogeneous characteristics in both clinical presentation and biochemical abnormality. The PDH Complex is a multi enzyme complex that plays a vital role as a key regulatory step in the central pathways of energy metabolism in the mitochondria. Inheritance and pathophysiology The most commonly seen form of PyruvateDehydrogenase Complex Deficiency is caused by mutations in the X linked E1 alpha gene and is approximately equally prevalent in both males and females. However, a greater severity of symptoms tends to affect males more often than heterozygous females. This can be explained by x inactivation , as females carry one normal and one mutant gene. Cells with a normal allele active can metabolize the lactic acid that is released by the PDH deficient cells. They cannot, however, supply ATP to these cells and, therefore, phenotype depends largely on the nature severity of the mutation. ref name PMC1016663 cite journal author G K Brown, L J Otero, M LeGris, and R M Brown title Pyruvatedehydrogenase deficiency journal J Med Genet. volume 31 issue 11 pages 875 879 year 1994 month November pmc 1016663 url http www.ncbi.nlm.nih.gov pmc articles PMC1016663 pdf jmedgene00001 0059.pdf ref ref name PMC1801181 cite journal author H H Dahl title Pyruvatedehydrogenase E1 alpha deficiency ... 0006.pdf ref Clinical Presentation PyruvateDehydrogenase Complex Deficiency is generally present ... out. ref name PMC1016663 Treatment Direct treatment that stimulates the pyruvatedehydrogenase complex ... the inhibitory phosphorylation of pyruvatedehydrogenase complex and thereby activates any residual ... more details
of the catalytic subunit of bovine pyruvatedehydrogenase phosphatase and sequence similarity ... the effects of pyruvatedehydrogenase kinase upon pyruvatedehydrogenase . Function Pyruvatedehydrogenase E1 is one of the three components E1, E2, and E3 of the large pyruvatedehydrogenase complex. Pyruvatedehydrogenase kinases catalyze phosphorylation of serine residues of E1 to inactivate the E1 component and inhibit the complex. Pyruvatedehydrogenase phosphatases catalyze the dephosphorylation and activation of the E1 component to reverse the effects of pyruvatedehydrogenase kinases. Pyruvatedehydrogenase phosphatase is a heterodimer consisting of catalytic and regulatory subunits ..., and belongs to the protein phosphatase 2C PP2C superfamily. Along with the pyruvatedehydrogenase complex and pyruvatedehydrogenase kinases, this enzyme is located in the mitochondrial matrix. ref name entrez Clinical significance Mutation in this gene causes pyruvatedehydrogenase phosphatase deficiency. ref name entrez Interactive pathway map TCACycle WP78 highlight Pyruvatedehydrogenase ... Down regulation of pyruvatedehydrogenase phosphatase in obese subjects is a defect that signals ... title Pyruvatedehydrogenase phosphatase 1 PDP1 null mutation produces a lethal infantile phenotype ... A. last9 Schulze first9 A. cite journal author Maj MC title Pyruvatedehydrogenase phosphatase deficiency ... regulating glucose oxidation at the level of the pyruvatedehydrogenase complex by PDKs journal ... crystallographic studies of the catalytic subunits of human pyruvatedehydrogenase phosphatase isoforms ... pyruvatedehydrogenase. Site specific regulation journal J. Biol. Chem. volume 270 issue 24 pages 14297 ... first7 LM cite journal author Ito M title Decrease of pyruvatedehydrogenase phosphatase activity ... of pyruvatedehydrogenase complex activity in muscle and liver cells journal J. Biol. Chem ... author Huang B title Isoenzymes of pyruvatedehydrogenase phosphatase. DNA derived amino acid sequences ... more details
enzyme Name pyruvatedehydrogenase lipoamide phosphatase EC number 3.1.3.43 CAS number 9073 70 5 IUBMB EC number 3 1 3 43 GO code 0004741 image width caption In enzymology , a pyruvatedehydrogenase acetyl transferring phosphatase EC number 3.1.3.43 is an enzyme that catalysis catalyzes the chemical reaction pyruvatedehydrogenase acetyl transferring phosphate H sub 2 sub O math rightleftharpoons math pyruvatedehydrogenase acetyl transferring phosphate Thus, the two substrate biochemistry substrates of this enzyme are pyruvatedehydrogenase acetyl transferring phosphate and water H sub 2 sub O , whereas its two product chemistry products are pyruvatedehydrogenase acetyl transferring 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 pyruvatedehydrogenase acetyl transferring phosphate phosphohydrolase . Other names in common use include pyruvatedehydrogenase phosphatase , phosphopyruvate dehydrogenase phosphatase , pyruvatedehydrogenase lipoamide phosphatase , and pyruvatedehydrogenase lipoamide phosphate phosphohydrolase . 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 2PNQ . References reflist 1 cite journal author Linn TC, Pelley JW, Pettit FH, Hucho F, Randall DD, Reed LJ date 1972 title Keto acid dehydrogenase complexes. XV. Purification and properties of the component enzymes of the pyruvatedehydrogenase complexes from bovine kidney and heart journal Arch. Biochem. Biophys. volume 148 pages 327&ndash 42 pmid 4401694 doi 10.1016 0003 9861 72 90151 8 issue 2 cite journal author Reed LJ, Damuni Z, Merryfield ML date 1985 title Regulation of mammalian pyruvate and branched chain alpha keto acid dehydrogenase complexes by phosphorylation dephosphorylation journal Curr. Top. Cell. Regul. volume 27 pages 41&ndash 9 pmid ... more details
PBB geneid 5160 Pyruvatedehydrogenase E1 component subunit alpha, somatic form, mitochondrial is an enzyme ... text The pyruvatedehydrogenase complex is a nuclear encoded mitochondrial matrix multienzyme complex ... Gene PDHA1 pyruvatedehydrogenase lipoamide alpha 1 url http www.ncbi.nlm.nih.gov sites entrez?Db ... Pyruvatedehydrogenase lipoamide alpha 1 References reflist Further reading refbegin 2 PBB Further ... in the pyruvatedehydrogenase E1 alpha gene. journal Hum. Mutat. volume 1 issue 2 pages ... M, Brown RM title Pyruvatedehydrogenase deficiency. journal J. Med. Genet. volume 31 issue 11 ... LL, Brown RM, et al. title X linked pyruvatedehydrogenase E1 alpha subunit deficiency in heterozygous ... AH, Naito E, et al. title Mutation of E1 alpha gene in a female patient with pyruvatedehydrogenase ... W, Vamos E, Liebaers I title Pyruvatedehydrogenase PDH deficiency caused by a 21 base pair insertion ... Characterization of the mutations in three patients with pyruvatedehydrogenase E1 alpha deficiency ... sequence of the gene encoding the human pyruvatedehydrogenase alpha subunit. journal Gene volume ... chromosome localization of the functional gene for the E1 alpha subunit of the human pyruvatedehydrogenase ... organization of the gene for the E1 alpha subunit of the human pyruvatedehydrogenase complex. journal ... Ho L, Wexler ID, Liu TC, et al. title Characterization of cDNAs encoding human pyruvatedehydrogenase ... encoding alpha and beta subunits of human pyruvatedehydrogenase. journal Proc. Natl. Acad. Sci ... author Hansen LL, Horn N, Dahl HH, Kruse TA title Pyruvatedehydrogenase deficiency caused by a 33 base ... N, et al. title An amino acid substitution in the pyruvatedehydrogenase E1 alpha gene, affecting .... title Pyruvatedehydrogenase complex deficiency due to a point mutation P188L within the thiamine pyrophosphate ... the irreversible conversion of pyruvate into acetyl CoA. The PDH complex is composed of multiple ... dehydrogenase DLD MIM 238331 E3 EC 1.8.1.4 . The E1 enzyme is a heterotetramer of 2 alpha ... more details
PBB geneid 5161 Pyruvatedehydrogenase lipoamide alpha 2 , also known as pyruvatedehydrogenase E1 component subunit alpha, testis specific form, mitochondrial or PDHE1 A type II , is an enzyme that in humans is encoded by the PDHA2 gene . ref name entrez cite web title Entrez Gene pyruvatedehydrogenase lipoamide alpha 2 url http www.ncbi.nlm.nih.gov sites entrez?Db gene&Cmd ShowDetailView&TermToSearch 5161 accessdate ref ref name pmid2249846 cite journal author Dahl HH, Brown RM, Hutchison WM, Maragos C, Brown GK title A testis specific form of the human pyruvatedehydrogenase E1 alpha subunit is coded for by an intronless gene on chromosome 4 journal Genomics volume 8 issue 2 pages 225 32 year 1990 month October pmid 2249846 doi 10.1016 0888 7543 90 90275 Y url ref Interactive pathway map TCACycle WP78 highlight Pyruvatedehydrogenase lipoamide alpha 2 References reflist Further reading refbegin 2 cite journal author Jacobia SJ, Korotchkina LG, Patel MS title Differential effects of two mutations at arginine 234 in the alpha subunit of human pyruvatedehydrogenase. journal Arch. Biochem. Biophys. volume 395 issue 1 pages 121 8 year 2001 pmid 11673873 doi 10.1006 abbi.2001.2576 cite journal author Olsen JV, Blagoev B, Gnad F, et al. title Global, in vivo, and site specific phosphorylation dynamics in signaling networks. journal Cell volume 127 issue 3 pages 635 48 year 2006 pmid 17081983 doi 10.1016 j.cell.2006.09.026 cite journal author Caruso M, Maitan MA, Bifulco G, et al ... stimulation of pyruvatedehydrogenase complex activity in muscle and liver cells. journal J. Biol ... testis specific form of the pyruvatedehydrogenase alpha subunit PDHA 2 gene. journal Biochim ... Fitzgerald J, Hutchison WM, Dahl HH title Isolation and characterisation of the mouse pyruvatedehydrogenase ... pyruvatedehydrogenase complex journal Arch. Biochem. Biophys. volume 316 issue 2 pages 926 40 ... Pyruvatedehydrogenase E1 alpha subunit genes in the mouse mapping and comparison with human homologs ... more details
A dehydrogenase also called DHO in the literature is an enzyme that oxidise s a substrate biochemistry substrate by a reduction reaction that transfers one or more hydride s H sup sup to an electron acceptor, usually Nicotinamide adenine dinucleotide NAD sup sup NADP NADP sup sup or a Flavin group flavin coenzyme such as FAD or FMN . Examples aldehyde dehydrogenase acetaldehyde dehydrogenase alcohol dehydrogenase glutamate dehydrogenase an enzyme that can convert glutamate to Ketoglutarate and vice versa . lactate dehydrogenasepyruvatedehydrogenase a common enzyme that feeds the Citric acid cycle TCA Cycle in converting Pyruvate to Acetyl CoA glucose 6 phosphate dehydrogenase involved in the pentose phosphate pathway glyceraldehyde 3 phosphate dehydrogenase involved in glycolysis sorbitol dehydrogenase TCA cycle examples isocitrate dehydrogenase alpha ketoglutarate dehydrogenase succinate dehydrogenase malate dehydrogenase External links eMedicineDictionary Dehydrogenase Enzymes Category Oxidoreductases enzyme stub it Deidrogenasi de Dehydrogenasen es Deshidrogenasa fr D shydrog nase he ja pl Dehydrogenazy pt Desidrogenase ru sl Dehidrogenaza sv Dehydrogenas zh ... more details
cellspacing 15 width 25 style border 1px solid a79c83 Enzymatic Reaction foward enzyme pyruvatedehydrogenase complex PDHC reverse enzyme substrate pyruvate Pyr product acetyl CoA Ac CoA reaction direction ...Pyruvate decarboxylation also known as the Swanson Conversion ref http www.rpi.edu dept bcbp molbiochem MBWeb mb1 part2 krebs.htm ref , or oxidative decarboxylation reaction is the Autocatalytic reaction Far from equilibrium far from equilibrium biochemical reaction that uses pyruvate to form acetyl CoA , releasing NADH , a reducing equivalent, and carbon dioxide via decarboxylation . It is known as the link reaction because it forms an important link between the metabolic pathway s of glycolysis and the citric acid cycle . This reaction is usually catalyzed by the pyruvatedehydrogenase complex as part of aerobic respiration . ref Alberts et al. Molecular Biology of the Cell. Garland Science, 2001. ISBN 0 8153 4072 9 ref In eukaryotes , pyruvate decarboxylation takes place exclusively inside the mitochondrial matrix in prokaryotes similar reactions take place in the cytoplasm and at the plasma ... of glycolysis which are cytosol ic. The conversion of pyruvate to acetyl CoA by the pyruvatedehydrogenase complex is a key step in the liver in particular, as it removes any chance of conversion of pyruvate to glucose, or as a transamination substrate. It commits pyruvate to entering the citric .... The oxidative decarboxylation of pyruvate in anaerobic organisms differs from the aerobic ... Crystal Structure of the Free Radical Intermediate of Pyruvate Ferredoxin Oxidoreductase Science 2001 ... sub via hydrogenase. p To summarise p 1. Pyruvate is decarboxylated p 2. It is added to Coenzyme A CoA to form Acetyl CoA p p Acetyl CoA is then ready for use in the Krebs Cycle . File Pyruvate decarboxylation steps.png thumb none 600px Pyruvate decarboxylation steps References references External links http www.rahulgladwin.com blog 2007 01 notes on pyruvate metabolism.html Notes on Pyruvate decarboxylation ... more details
pathway, which produces pyruvate molecules, the final product of aerobic glycolysis. However, in anaerobic glycolysis, lactate dehydrogenase will utilize the NADH produced by glyceraldehyde phosphate dehydrogenase to reduce pyruvate to lactate. In humans, there are two pyruvate kinase isozymes type ...Image pkb.jpg thumb right 250px Typical Pyruvate Kinase Structure, small X ray Crystallography Derived small Pyruvate kinase List of EC numbers EC 2 EC 2.7.1 Phosphotransferases with an Alcohol Group as Acceptor ... of pyruvate and one molecule of adenosine triphosphate ATP . Reaction The pyruvate kinase reaction Image Pyruvate kinase.png left thumb This process also requires a magnesium ion. The enzyme is a transferase ... activity of the pathway, and are, in general, irreversible under wild type conditions . Pyruvate ... Citation&list uids 22182754 doi 10.1016 j.abb.2011.11.020 ref Liver pyruvate kinase is also regulated ... liver pyruvate kinase to deactivate it. Muscle pyruvate kinase is not inhibited by epinephrine ... of pyruvate kinase. These controls prevent pyruvate kinase from being active at the same time as the enzymes that catalyze the reverse reaction pyruvate carboxylase and phosphoenolpyruvate ... of this enzyme cause the disease known as pyruvate kinase deficiency . In this condition, a lack of pyruvate kinase slows down the process of glycolysis. This effect is especially devastating in cells ... cells , which in a state of pyruvate kinase deficiency rapidly become deficient in ATP and can undergo hemolysis . Therefore, pyruvate kinase deficiency can cause hemolytic anemia . Role in gluconeogenesis Pyruvate kinase also serves as a regulatory enzyme for gluconeogenesis , a biochemical pathway in which the liver generates glucose from pyruvate and other substrates. When pyruvate kinase ... is prevented from being converted to pyruvate. Instead, it is converted to glucose in a series of gluconeogenesis .... Alternatives A reversible enzyme with a similar function, Pyruvate phosphate dikinase PPDK , is found ... more details
About the enzyme that forms acetaldehyde the enzyme that feeds the citric acid cycle pyruvatedehydrogenase enzyme Name Pyruvate decarboxylase EC number 4.1.1.1 CAS number 9001 04 1 IUBMB EC number 4 1 1 1 GO code 0004737 image Pyruvate decarb 1.jpg width caption Reaction catalyzed by pyruvate decarboxylase br pyruvate thiamine pyrophasphate TPP hydroxyethyl TPP CO sub 2 sub Pyruvate decarboxylase .... Pyruvate decarboxylase starts this process by converting pyruvate into acetaldehyde and carbon ... ref Pyruvate decarboxylase depends on Cofactor biochemistry cofactors thiamine pyrophosphate TPP and magnesium. This enzyme should not be mistaken for the unrelated enzyme pyruvatedehydrogenase , an oxidoreductase EC number 1.2.4.1 , that catalyzes the oxidative decarboxylation of pyruvate to acetyl CoA . Yeast In yeast, pyruvate decarboxylase acts independently during wikt anaerobic anaerobic fermentation and releases the 2 carbon fragment as acetaldehyde plus carbon dioxide. Pyruvate decarboxylase ... F title Catalytic centers in the thiamin diphosphate dependent enzyme pyruvate decarboxylase at 2.4 ... keto acid pyruvate to meet. ref name pmid8512926 Structure Pyruvate decarboxylase occurs as a dimer ... B, Jordan F title Catalytic centers in the thiamin diphosphate dependent enzyme pyruvate decarboxylase ... 8512926 doi 10.1021 bi00075a008 url issn ref Gallery title Crystallographic structures of pyruvate decarboxylase width 275 lines 3 Image 1pvd with TPP.jpg Cartoon diagram of pyruvate decarboxylase monomer with TPP attached. Image 1pvd image.jpg Cartoon diagram of pyruvate decarboxylase tetramer. Image PDC chimera cropped r3 c4.jpg Active site of pyruvate decarboxylase with selected amino acids ... in conformation changes when interacting with pyruvate substrate. Active site residues Image ... a cavity in the core of the enzyme where hydrogen bonding can occur and where the pyruvate reacts ... DHG title Pyruvate Decarboxylase A Molecular Modeling Study of Pyruvate Decarboxylation and Acyloin ... more details
dehydrogenase and pyruvate carboxylase in pancreatic islets of Zucker diabetic fatty rats journal Diabetes ... by insulin of low mitochondrial glycerol phosphate dehydrogenase and pyruvate carboxylase in pancreatic ...enzyme Name Pyruvate carboxylase EC number 6.4.1.1 CAS number 9014 19 1 IUBMB EC number 6 4 1 1 GO code 0004736 image Pyruvate Carboxylase fromPDB 2QF7.png width caption X ray crystallography Biological macromolecular crystallography Crystallographic structure of pyruvate carboxylase from Rhizobium Rhizobium ... of pyruvate carboxylase journal Biochem. J. volume 413 issue 3 pages 369 87 year 2008 month August pmid 18613815 pmc 2859305 doi 10.1042 BJ20080709 url issn ref Pfam box Symbol PYR CT Name Pyruvate ... PDB2 1rqe PDB2 1s3h PDB2 1sr9 PDB2 1u5j Protein Name Pyruvate carboxylase image caption Symbol PC ... 608786 EntrezGene 5091 RefSeq NM 000920 UniProt P11498 PDB Pyruvate carboxylase PC is an enzyme of the ligase class that catalyzes the depending on the species irreversible carboxylation of pyruvate ... oxaloacetate from pyruvate. The enzyme is a mitochondrial protein containing a biotin prosthetic ... . ref name pmid18613815 Pyruvate carboxylase was first discovered in 1959 at Western Reserve University ... Formation of oxaloacetate from pyruvate and carbon dioxide journal J. Biol. Chem. volume 235 issue ... appearance of pyruvate carboxylase from chicken liver journal J. Biol. Chem. volume 254 issue 5 pages ... Puig A, Wallace JC title Anaplerotic roles of pyruvate carboxylase in mammalian tissues journal Cell ... Y, Wallace JC title Molecular cloning and domain structure of chicken pyruvate carboxylase journal Biochem ... spliced pyruvate carboxylase mRNAs with divergent 5 untranslated regions which are expressed in a tissue ... subunit of pyruvate carboxylase from Aquifex aeolicus at 2.2 A resolution journal Acta Crystallogr ... G, Gil D, Valle M, Tong L title A symmetrical tetramer for S. aureus pyruvate carboxylase in complex ..., Rayment I title Domain architecture of pyruvate carboxylase, a biotin dependent multifunctional enzyme ... more details
A pyruvate cycling pathway involving cytosolic NADP dependent isocitrate dehydrogenase regulates ...Pyruvate cycling commonly refers to an intracellular loop of spatial movements and chemical transformations involving pyruvate . Spatial movements occur between Mitochondrion mitochondria and cytosol and chemical transformations create various Krebs cycle intermediates. In all variants, pyruvate is imported into the mitochnodrion for processing through part of the Krebb s cycle. In addition to pyruvate ... to the cytosol for additional transformations and then re imported. Three specific pyruvate cycles ... may exist, such as dissipative or futile pyruvate cycles ref cite journal author Gregory RB, Berry ... of pyruvate cycling to loss of 6 3Hglucose during conversion of glucose to glycogen in hepatocytes effects ... citrate lyase, malic enzyme, and pyruvate citrate cycling in glucose induced insulin secretion journal ... PJ title Role for malic enzyme, pyruvate carboxylation, and mitochondrial malate import in glucose ... url pmc 2692397 ref .It has been observed in various cell types including islet cells. The pyruvate ... Scaduto RC, Davis EJ title The involvement of pyruvate cycling in the metabolism of aspartate and glycerate ... year 1986 month August pmid 3800911 pmc 1147046 doi url ref . section stubs pyruvate malate pyruvate citrate pyruvate isocitrate References reflist Further reading cite journal author Kley S, Hoenig M ... Islets Results in Elevated U 13CGlucose Metabolism, Glutaminolysis, and Pyruvate Cycling but a Decreased ... U, Rosengren AH, Schuit FC, Renstr m E, Mulder H title Anaplerosis via pyruvate carboxylase is required ... url cite journal author Jensen MV, Joseph JW, Ilkayeva O, et al. title Compensatory responses to pyruvate ... analysis reveals a connection between pyruvate cycling and glucose stimulated insulin secretion ... author Thompson SN title Pyruvate cycling and implications for regulation of gluconeogenesis ... P cite journal author Rognstad R title Pyruvate cycling involving possible oxaloacetate decarboxylase ... more details
enzyme Name pyruvate synthase EC number 1.2.7.1 CAS number 9082 51 3 IUBMB EC number 1 2 7 1 GO code 0019164 image width caption In enzymology , a pyruvate synthase EC number 1.2.7.1 is an enzyme that catalysis catalyzes the chemical reaction pyruvate CoA 2 oxidized ferredoxin math rightleftharpoons math acetyl CoA CO sub 2 sub 2 reduced ferredoxin 2 H sup sup The 3 substrate biochemistry substrates of this enzyme are pyruvate , coenzyme A CoA , and oxidized ferredoxin , whereas its 4 product chemistry products are acetyl CoA , carbon dioxide CO sub 2 sub , reduced ferredoxin, 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 an iron sulfur protein as acceptor. The systematic name of this enzyme class is pyruvate ferredoxin 2 oxidoreductase CoA acetylating . Other names in common use include pyruvate oxidoreductase , pyruvate synthetase , pyruvate ferredoxin oxidoreductase , and pyruvic ferredoxin oxidoreductase . This enzyme participates in 4 metabolism metabolic pathways pyruvate metabolism , propanoate metabolism , butanoate metabolism , and reductive carboxylate cycle CO2 fixation . Structural studies As of late 2007, 10 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1B0P , PDB link 1KEK , PDB link 2C3M , PDB link 2C3O , PDB link 2C3P , PDB link 2C3U , PDB link 2C3Y , PDB link 2C42 , PDB link 2PDA , and PDB link 2RAA . References reflist 1 cite journal author Evans MC, Buchanan BB date 1965 title Photoreduction of ferredoxin and its use in carbon dioxide fixation by a subcellular system from ..., Rabinowitz JC date 1971 title Pyruvate ferredoxin oxidoreductase. 3. Purification and properties of the enzyme ... author Uyeda K, Rabinowitz JC date 1971 title Pyruvate ferredoxin oxidoreductase. IV. Studies on the reaction ... and electron transfer mechanism of pyruvate ferredoxin oxidoreductase journal Curr. Opin. Struct ... more details
enzyme Name pyruvate oxidase EC number 1.2.3.3 CAS number 9001 96 1 IUBMB EC number 1 2 3 3 GO code 0047112 image width caption In enzymology , a pyruvate oxidase EC number 1.2.3.3 is an enzyme that catalysis catalyzes the chemical reaction pyruvate phosphate O sub 2 sub math rightleftharpoons math acetyl phosphate CO sub 2 sub H sub 2 sub O sub 2 sub The 3 substrate biochemistry substrates of this enzyme are pyruvate , phosphate , and oxygen O sub 2 sub , whereas its 3 product chemistry products are acetyl phosphate , 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 phosphorylating . Other names in common use include pyruvic oxidase , and phosphate dependent pyruvate oxidase . This enzyme participates in pyruvate metabolism . It has 2 cofactor biochemistry cofactors FAD , and Thiamin diphosphate . Structural studies As of late 2007, 12 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1POW , PDB link 1POX , PDB link 1V5E , PDB link 1V5F , PDB link 1V5G , PDB link 1Y9D , PDB link 2DJI , PDB link 2EZ4 , PDB link 2EZ8 , PDB link 2EZ9 , PDB link 2EZT , and PDB link 2EZU . References reflist 1 cite journal author Williams FR, Hager LP date 1966 title Crystalline flavin pyruvate oxidase from Escherichia coli. I Isolation and properties of the flavoprotein journal Arch. Biochem. Biophys. volume 116 pages 168&ndash 76 pmid 5336022 doi 10.1016 0003 9861 66 90025 7 issue 1 cite journal author Tittmann K, Wille G, Golbik R, Weidner A, Ghisla S, Hubner G date 2005 title Radical phosphate transfer mechanism for the thiamin diphosphate and FAD dependent pyruvate oxidase from Lactobacillus plantarum Kinetic coupling of intercofactor electron transfer with phosphate ... more details
chembox verifiedrevid 464403469 Name Sodium pyruvate ImageFile Sodium pyruvate.png ImageFileL1 Pyruvate 3D balls.png ImageSizeL1 160px ImageNameL1 Ball and stick model of the pyruvate anion ImageFileR1 Sodium 3D.png ImageSizeR1 80px ImageNameR1 The sodium cation OtherNames ketopropionic acid sodium salt 2 oxopropanoic acid sodium salt Pyruvic acid sodium salt Section1 Chembox Identifiers ChemSpiderID Ref chemspidercite correct chemspider ChemSpiderID 7931 ChEMBL Ref ebicite correct EBI ChEMBL 181886 PubChem 23662274 UNII Ref fdacite correct FDA UNII POD38AIF08 InChI 1 C3H4O3.Na c1 2 4 3 5 6 h1H3, H,5,6 q 1 p 1 InChIKey DAEPDZWVDSPTHF REWHXWOFAL ChEBI Ref ebicite correct EBI ChEBI 50144 SMILES Na . O C O C O C StdInChI Ref stdinchicite correct chemspider StdInChI 1S C3H4O3.Na c1 2 4 3 5 6 h1H3, H,5,6 q 1 p 1 StdInChIKey Ref stdinchicite correct chemspider StdInChIKey DAEPDZWVDSPTHF UHFFFAOYSA M CASNo Ref cascite correct CAS CASNo 113 24 6 Section2 Chembox Properties Formula C sub 3 sub H sub 3 sub NaO sub 3 sub MolarMass 110.044 g mol Density Solvent other solvents SolubleOther 100 mg mL MeltingPt BoilingPt Sodium pyruvate is commonly added to cell culture media as an additional source of energy, but may also have protective effects against hydrogen peroxide . This was reported by Giandomenico et al. . ref cite journal author Giandomenico AR, Cerniglia GE, Biaglow JE, Stevens CW, Koch CJ title The importance of sodium pyruvate in assessing damage produced by hydrogen peroxide. journal Free Radic Biol Med volume 23 issue 3 pages 426 34 year 1997 pmid 9214579 doi 10.1016 S0891 5849 97 00113 5 url ref and has been confirmed by several independent groups. References reflist Category Sodium compounds biochem stub ar fa ... more details
The pyruvate scale measures pungency in onions and garlic with units of Mole unit mol g sub fw sub micromoles per gram fresh weight . ref cite web title Spring 2001 Commercial Vegetable Variety Trials url http www.aaes.auburn.edu comm pubs vegetables spring2001.pdf accessdate 2011 06 21 ref It is named after pyruvic acid , the alpha keto acid co product created in the biochemical pathway that forms the lacrimator, syn Propanethial S oxide . The standard onion has an eight rating, while sweet onions have a two or three rating on the scale. The lower the score or scale the more sweet the onions are rated. Anything less than five is considered a sweet onion. The Vidalia onion variety is considered sweet and must have a score of 5.0 mol g sub fw sub or less. Citation needed date February 2007 The Supasweet onion usually grown in Lincolnshire , England registers 1.5 to 2 on the scale. A standard brown onion is usually in the range of 6 7 out of 10. Soil type, rain, and sunlight affect the pungency in onions and garlic and, therefore, their score on the pyruvate scale. References Reflist External links http www.ams.usda.gov nop indexNet.htm The National Organic Program &mdash by the USDA Failed verification date January 2011 Category Scales Agri stub ... more details
enzyme Name tryptophan dehydrogenase EC number 1.4.1.19 CAS number 94047 13 9 IUBMB EC number 1 4 1 19 GO code 0050363 image width caption In enzymology , a tryptophan dehydrogenase EC number 1.4.1.19 is an enzyme that catalysis catalyzes the chemical reaction L tryptophan NAD P H sub 2 sub O math rightleftharpoons math indol 3 yl pyruvate NH sub 3 sub NAD P H H sup sup The 4 substrate biochemistry substrates of this enzyme are L tryptophan , nicotinamide adenine dinucleotide NAD sup sup , nicotinamide adenine dinucleotide phosphate NADP sup sup , and water H sub 2 sub O , whereas its 5 product chemistry products are indol 3 yl pyruvate , ammonia NH sub 3 sub , nicotinamide adenine dinucleotide NADH , nicotinamide adenine dinucleotide phosphate NADPH , and hydrogen ion H sup sup . 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 tryptophan NAD P oxidoreductase deaminating . Other names in common use include NAD P L tryptophan dehydrogenase , L tryptophan dehydrogenase , L Trp dehydrogenase , and TDH . This enzyme has at least one effector biology effector , calcium . References reflist 1 cite journal author Vackova K, Mehta A and Kutacek M date 1985 title Tryptophan aminotransferase and tryptophan dehydrogenase activities in some cell compartments of spinach leaves the effect of calcium ions on tryptophan dehydrogenase journal Biol. Plant. volume 27 pages 154&ndash 158 doi 10.1007 BF02902153 issue 2 3 1.4 enzyme stub Category EC 1.4.1 Category NADPH dependent enzymes Category NADH dependent enzymes Category Enzymes of unknown structure it Triptofano deidrogenasi ja ... more details
enzyme Name indolelactate dehydrogenase EC number 1.1.1.110 CAS number 37250 41 2 IUBMB EC number 1 1 1 110 GO code 0047722 image width caption In enzymology , an indolelactate dehydrogenase EC number 1.1.1.110 is an enzyme that catalysis catalyzes the chemical reaction indol 3 yl lactate NAD sup sup math rightleftharpoons math indol 3 yl pyruvate NADH H sup sup Thus, the two substrate biochemistry substrates of this enzyme are indol 3 yl lactate and nicotinamide adenine dinucleotide NAD sup sup , whereas its 3 product chemistry products are indol 3 yl 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 OH group of donor with NAD or NADP as acceptor. The systematic name of this enzyme class is indol 3 yl lactate NAD oxidoreductase . This enzyme is also called indolelactate NAD oxidoreductase . This enzyme participates in tryptophan metabolism . References reflist 1 cite journal doi 10.1139 m68 068 author Jean M, DeMoss RD date 1968 title Indolelactate dehydrogenase from Clostridium sporogenes journal Can. J. Microbiol. volume 14 pages 429&ndash 35 pmid 4384683 issue 4 1.1.1 enzyme stub Category EC 1.1.1 Category NADH dependent enzymes Category Enzymes of unknown structure it Indololattato deidrogenasi ja ... more details
enzyme Name strombine dehydrogenase EC number 1.5.1.22 CAS number 79393 84 3 IUBMB EC number 1 5 1 22 GO code 0050305 image width caption In enzymology , a strombine dehydrogenase EC number 1.5.1.22 is an enzyme that catalysis catalyzes the chemical reaction N carboxymethyl D alanine NAD sup sup H sub 2 sub O math rightleftharpoons math glycine pyruvate NADH H sup sup The 3 substrate biochemistry substrates of this enzyme are N carboxymethyl D alanine , nicotinamide adenine dinucleotide NAD sup sup , and water H sub 2 sub O , whereas its 4 product chemistry products are glycine , 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 donor with NAD or NADP as acceptor. The systematic name of this enzyme class is N carboxymethyl D alanine NAD oxidoreductase glycine forming . Other names in common use include strombine N carboxymethyl D alanine dehydrogenase , and N carboxymethyl D alanine 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 1.5 enzyme stub Category EC 1.5.1 Category NADH dependent enzymes Category Enzymes of unknown structure it Strombina deidrogenasi ja ... more details
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