enzyme Name L glutamate oxidase EC number 1.4.3.11 CAS number 39346 34 4 IUBMB EC number 1 4 3 11 GO code 0050025 image width caption In enzymology , a L glutamate oxidase EC number 1.4.3.11 is an enzyme that catalysis catalyzes the chemical reaction L glutamate O sub 2 sub H sub 2 sub O math rightleftharpoons math 2 oxoglutarate NH sub 3 sub H sub 2 sub O sub 2 sub The 3 substrate biochemistry substrates of this enzyme are L glutamate , oxygen O sub 2 sub , and water H sub 2 sub O , whereas its 3 product chemistry products are 2 oxoglutarate , ammonia NH sub 3 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 CH NH2 group of donors with oxygen as acceptor. The systematic name of this enzyme class is L glutamate oxygen oxidoreductase deaminating . Other names in common use include glutamate acceptor dehydrogenase , glutamate oxidase , glutamic acid oxidase , glutamic dehydrogenase acceptor , and L glutamic acid oxidase . It employs one cofactor biochemistry cofactor , FAD . References reflist 1 cite journal author Yoshino H date 1983 title Purification and properties of a new enzyme, L glutamate oxidase, from Streptomyces sp X 119 6 grown on wheat bran journal Agric. Biol. Chem. volume 47 pages 1323&ndash 1328 1.4 enzyme stub Category EC 1.4.3 Category Flavin enzymes Category Enzymes of unknown structure it L glutammato ossidasi ja L ... more details
Drugbox verifiedrevid 428758397 Combo data type combo component1 Arginine class1 amino acid component2 Glutamic acid class2 amino acid Clinical data tradename Drugs.com drugs.com international arginine glutamate pregnancy AU A B1 B2 B3 C D X pregnancy US A B C D X pregnancy category legal AU S2, S3, S4, S5, S6, S7, S8, S9 or Unscheduled legal CA Schedule I, II, III, IV, V, VI, VII, VIII legal UK GSL, P, POM, CD, or Class A, B, C legal US OTC Rx only Schedule I, II, III, IV, V legal status routes of administration Identifiers CAS number 4320 30 3 ATC prefix A05 ATC suffix BA01 PubChem 165268 DrugBank Ref drugbankcite correct drugbank DrugBank Chemical data Arginine glutamate is a mixture of two amino acid s, arginine and glutamic acid , used in liver therapy. Bile and liver therapy Category Amino acids Category Combination drugs gastrointestinal drug stub ... more details
enzyme Name 1 pyrroline 5 carboxylate dehydrogenase EC number 1.5.1.12 CAS number 9054 82 4 IUBMB EC number 1 5 1 12 GO code 0003842 image width caption In enzymology , a 1 pyrroline 5 carboxylate dehydrogenase EC number 1.5.1.12 is an enzyme that catalysis catalyzes the chemical reaction 1 pyrroline 5 carboxylic acid S 1 pyrroline 5 carboxylate NAD sup sup 2 H sub 2 sub O math rightleftharpoons math glutamic acid small L small glutamate NADH H sup sup The three substrate biochemistry substrates of this enzyme are S 1 pyrroline 5 carboxylate, nicotinamide adenine dinucleotide NAD sup sup , and water H sub 2 sub O , whereas its three product chemistry products are glutamate, 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 S 1 pyrroline 5 carboxylate NAD sup sup oxidoreductase . Other names in common use include delta 1 pyrroline 5 carboxylate dehydrogenase , 1 pyrroline dehydrogenase , pyrroline 5 carboxylate dehydrogenase , pyrroline 5 carboxylic acid dehydrogenase , small L small pyrroline 5 carboxylate NAD sup sup oxidoreductase , and 1 pyrroline 5 carboxylate NAD sup sup oxidoreductase . This enzyme participates in glutamate metabolism and arginine and proline metabolism . Structural studies As of late 2007, 14 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 2BHP , PDB link 2BHQ , PDB link 2BJA ... 1 cite journal author Adams E and Goldstone A date 1960 title Hydroxyproline metabolism. IV. Enzymatic ... title The interconversion of glutamic acid and proline. III Delta1 Pyrroline 5 carboxylic acid dehydrogenase ... EC 1.5.1 Category NADH dependent enzymes Category Enzymes of known structure it 1 pirrolina 5 carbossilato deidrogenasi ja 1 5 ... more details
pyruvate dehydrogenase activity include protein Name Pyruvate dehydrogenase lipoamide alpha 1 caption image width HGNCid 8806 Symbol Pyruvate dehydrogenase lipoamide alpha 1 PDHA1 AltSymbols PDHA EntrezGene ... enzyme Name EC number 1.2.4.1 CAS number 9014 20 4 IUBMB EC number 1 2 4 1 GO code 0004739 image PDwhole1.jpg width caption Crystallographic structure of pyruvate dehydrogenase PDH . PH is a six ... for flip flop action of thiamin pyrophosphate dependent enzymes revealed by human pyruvate dehydrogenase ... pmid 15264254 doi 10.1002 jcc.20084 url ref Pyruvate dehydrogenase E1 is the first component enzyme of pyruvate dehydrogenase complex PDC . The pyruvate dehydrogenase complex contributes to transforming ... in the citric acid cycle to carry out cellular respiration , so pyruvate dehydrogenase contributes ... adenine dinucleotide NADH . EC number 1.2.4.1 . Function Pyruvate dehydrogenase E1 performs the first two reactions within the pyruvate dehydrogenase complex PDC a decarboxylation of substrate 1 pyruvate and a reductive acetylation of substrate 2 lipoic acid . Lipoic acid is covalently bound .... The reaction catalyzed by pyruvate dehydrogenase E1 is considered to be the rate limiting step for the pyruvate dehydrogenase complex PDHc . Regulation Phosphorylation of E1 by pyruvate dehydrogenase kinase PDK inactivates E1 and subsequently the entire complex. This is reversed by pyruvate dehydrogenase phosphatase . Pyruvate dehydrogenase phosphatase is stimulated by insulin , Phosphoenolpyruvate ... Dehydrogenase Mechanism File PyruvateDehydrgenaseMech1.gif Pyruvate Dehydrogenase Mechanism The ylide ... the conserved hydrogen bond with glutamate residue Glu59 in human E1 and by imposing a V conformation ... for flip flop action of thiamin pyrophosphate dependent enzymes revealed by human pyruvate dehydrogenase ... dehydrogenase multienzyme complex E1 component from Escherichia coli at 1.85 A resolution journal Biochemistry ... bichaw 2002 41 i16 abs bi0118557.html doi 10.1021 bi0118557 ref File Pyruvate dehydrogenase ... more details
orphan date October 2011 Infobox protein family Symbol ELFV dehydrog Name Glutamate Leucine Phenylalanine Valine dehydrogenase image PDB 1b3b EBI.jpg width caption thermotoga maritima glutamatedehydrogenase mutant n97d, g376k Pfam PF00208 Pfam clan CL0063 InterPro IPR006096 SMART PROSITE PDOC00071 MEROPS ... oxidative deamination reaction. Glutamatedehydrogenase s EC number 1.4.1.2 , EC number 1.4.1.3 ... Lahfa N, Forterre P, Labedan B title Evolution of glutamatedehydrogenase genes evidence ... phosphate dependent glutamatedehydrogenase journal J. Biol. Chem. volume 260 issue 14 pages 8502 ... of cDNA clones encoding human liver glutamatedehydrogenase evidence for a small gene ... Glu Leu Phe Val dehydrogenase, dimerisation domain Pfam PF02812 Pfam clan InterPro SMART PROSITE MEROPS SCOP 1leh TCDB OPM family OPM protein CAZy CDD In molecular biology, the ELFV dehydrogenase family of enzymes include glutamate , leucine , phenylalanine and valine dehydrogenases . These enzymes ... and or Nicotinamide adenine dinucleotide phosphate NADP dependent reversible deamination of L glutamate ..., Stillman TJ title Structural relationship between the hexameric and tetrameric family of glutamate ... doi url ref GluDH isozymes are generally involved with either ammonia assimilation or glutamate ... catalyses the amination of alpha ketoglutarate to L glutamate and the NAD dependent enzyme, which ... 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 ... 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
Distinguish aldehyde oxidase enzyme Name Aldehyde dehydrogenase NAD EC number 1.2.1.3 CAS number 9028 86 8 IUBMB EC number 1 2 1 3 GO code 0004029 image Monomer with an NAD with surface .png width caption Monomer of human aldehyde dehydrogenase 2 ALDH2 with a space filling model of nicotinamide adenine ... dehydrogenase is a Polymorphism biology polymorphic enzyme ref name Crabb2004 responsible for the oxidation ... class 1 low K sub m sub , cytosolic , class 2 low K sub m sub , mitochondrial , and class 3 high ... Site The active site of the aldehyde dehydrogenase enzyme is largely conserved throughout the different ... and an NAD P sup sup that functions as a cofactor. A cysteine and a glutamate will interact with the aldehyde ... surface.png Tetramer of aldehyde dehydrogenase 2 with a space filling model of NAD sup sup in each ... site of a human mitochondrial aldehyde dehydrogenase 2. Cys302 and Glu268 interact with the aldehyde ... aldehyde dehydrogenase 2 with a space filling model of NAD sup sup in the active site. The amino ... functional. ref name Liu et al1997 Image Aldehyde dehydrogenase mechanism.png left 600 px Mechanism of Aldehyde Dehydrogenase A sulfur from a cysteine in the active site makes a nucleophilic attack ... by a glutamate in the active site, and the water makes a nucleophilic attack on the carbonyl carbon ... Role of aldehyde dehydrogenase shown in red box in norepinephrine degradation, creating vanillylmandelic ... . ref name Thomasson1991 There is a mutant form of aldehyde dehydrogenase, termed ALDH2 2, wherein a lysine residue replaces a glutamate in the active site at position 487 of ALDH2. ref name Steinmetz1997 ... al. found that decreased enzyme activity of aldehyde dehydrogenase 2, caused by the mutated ALDH2 ... dehydrogenase oxidation References Reflist refs ref name pmid12795606 PDB 1o02 cite journal author Perez Miller SJ, Hurley TD title Coenzyme isomerization is integral to catalysis in aldehyde dehydrogenase ... M title Overview of the role of alcohol dehydrogenase and aldehyde dehydrogenase and their variants ... more details
dehydrogenase1 ALDH1A1 polymorphisms in harmful alcohol consumption in a Finnish population journal ...enzyme Name Acetaldehyde dehydrogenase br acetylating EC number 1.2.1.10 CAS number 9028 91 5 IUBMB EC number 1 2 1 10 GO code 0008774 image AcetaldehydeDehydrogenase 1NVM.png width caption Crystallographic structure of the acetaldehyde dehydrogenase from Pseudomonas Pseudomonas sp . ref name pmid12764229 ... aldolase dehydrogenase sequestering a reactive and volatile intermediate journal Proc ... 165818 doi 10.1073 pnas.1236794100 url issn ref Acetaldehyde dehydrogenases EC number 1.2.1.10 are dehydrogenase ... are members of the larger class of aldehyde dehydrogenase s. The CAS number for this type of the enzyme ... cite journal author Hempel J, Kaiser R, Jornvall H. title Mitochondrial aldehyde dehydrogenase from human liver journal Eur. J. Biochem. volume 153 issue 1 pages 13 28 year 1985 pmid 4065146 doi 10.1111 ... blue and residue 302 red highlighted. thumb 200px As discovered by site directed mutagenesis , glutamate 268 is a key component of liver acetaldehyde dehydrogenase and is also critical to catalytic activity ... journal author Wang X, Weiner H. title Involvement of glutamate 268 in the active site of human liver mitochondrial class 2 aldehyde dehydrogenase as probed by site directed mutagenesis journal Biochemistry ... pubmed 7819202 doi 10.1021 bi00001a028 ref In bacteria, acylating acetaldehyde dehydrogenase forms ... active site to the acetaldehyde dehydrogenase active site. Such communication between proteins ... K, Yoshida A. title Cloning of cDNAs for human aldehyde dehydrogenases 1 and 2 journal Porc ... In the liver , the enzyme alcohol dehydrogenase oxidize s ethanol into acetaldehyde , which is then further converted into the harmless acetic acid vinegar by acetaldehyde dehydrogenase. Acetaldehyde ... dehydrogenase gene , ref name Xiao Q, Weiner H, Crabb DW 1996 2027 32 cite journal author Xiao Q, Weiner H, Crabb DW title The mutation in the mitochondrial aldehyde dehydrogenase ALDH2 gene responsible ... more details
enzyme Name glutamate synthase NADH EC number 1.4.1.14 CAS number 65589 88 0 IUBMB EC number 1 4 1 14 GO code 0016040 image width caption In enzymology , a glutamate synthase NADH EC number 1.4.1.14 is an enzyme that catalysis catalyzes the chemical reaction 2 L glutamate NAD sup sup math rightleftharpoons math L glutamine 2 oxoglutarate NADH H sup sup Thus, the two substrate biochemistry substrates of this enzyme are L glutamate and nicotinamide adenine dinucleotide NAD sup sup , whereas its 4 product chemistry products are L glutamine , 2 oxoglutarate , 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 sub 2 sub group of donors with NAD sup sup or NADP sup sup as acceptor. This enzyme participates in glutamate metabolism and nitrogen metabolism . It employs one cofactor biochemistry cofactor , FMN . Nomenclature The systematic name of this enzyme class is L glutamate NAD sup sup oxidoreductase transaminating . Other names in common use include glutamate reduced nicotinamide adenine dinucleotide synthase, glutamate synthase NADH , L glutamate synthetase, NADH dependent glutamate synthase, NADH glutamate synthase, and NADH GOGAT, L glutamate synthase NADH . References reflist 1 cite journal author Boland MJ, Benny AG date 1977 title Enzymes of nitrogen metabolism in legume nodules. Purification and properties of NADH dependent glutamate synthase from lupin nodules journal Eur. J. Biochem. volume 79 pages 355&ndash 62 pmid 21790 doi 10.1111 j.1432 1033.1977.tb11816.x issue 2 1.4 enzyme stub Category EC 1.4.1 Category NADH dependent enzymes Category Flavin enzymes Category Enzymes of unknown structure it Glutammato sintasi NAD ja NADH ... 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
enzyme Name glutamate N acetyltransferase EC number 2.3.1.35 CAS number 37257 14 0 IUBMB EC number 2 3 1 35 GO code 0004358 image width caption In enzymology , a glutamate N acetyltransferase EC number 2.3.1.35 is an enzyme that catalysis catalyzes the chemical reaction N sub 2 sub acetyl L ornithine L glutamate math rightleftharpoons math L ornithine N acetyl L glutamate Thus, the two substrate biochemistry substrates of this enzyme are N2 acetyl L ornithine and L glutamate , whereas its two product chemistry products are L ornithine and N acetyl L glutamate . This enzyme belongs to the family of transferase s, specifically those acyltransferase s transferring groups other than aminoacyl groups. The systematic name of this enzyme class is N2 acetyl L ornithine L glutamate N acetyltransferase . Other names in common use include ornithine transacetylase , alpha N acetyl L ornithine L glutamate N acetyltransferase , acetylglutamate synthetase , acetylglutamate acetylornithine transacetylase , acetylglutamic synthetase , acetylglutamic acetylornithine transacetylase , acetylornithinase , acetylornithine glutamate acetyltransferase , glutamate acetyltransferase , N acetyl L glutamate synthetase , N acetylglutamate synthase , N acetylglutamate synthetase , ornithine acetyltransferase , and 2 N acetyl L ornithine L glutamate N acetyltransferase . This enzyme participates in urea cycle and metabolism of amino groups . 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 1VRA , PDB link 1VZ6 , PDB link 1VZ7 , and PDB link 1VZ8 . References reflist 1 cite journal author Staub M, Denes G date 1966 title Mechanism of arginine biosynthesis in Chlamydomonas reinhardti. I Purification and properties of ornithine acetyltransferase journal Biochim. Biophys. Acta. volume 128 pages 82&ndash 91 pmid 5972370 issue 1 transferase stub Category EC 2.3.1 Category Enzymes of known structure ... more details
In biochemistry , the glutamate glutamine cycle is a sequence of events by which an adequate supply of the neurotransmitter glutamate is maintained in the central nervous system . ref name Purves cite book author Purves, Dale, George J. Augustine, David Fitzpatrick, William C. Hall, Anthony Samuel LaMantia, James O. McNamara, and Leonard E. White title Neuroscience. 4th ed. publisher Sinauer Associates pages 128 9 year 2008 isbn 978 0 87893 697 7 ref Initially, glial cell s release glutamine , which is then taken up into presynaptic terminal s and metabolized into glutamate by glutaminase a mitochondria l enzyme . Glutamate can also be produced by transamination of 2 oxoglutarate , an intermediate in the Citric acid cycle . ref name Purves The glutamate that is synthesized in the presynaptic terminal is packaged into synaptic vesicle s by the transporter VGLUT . Once the vesicle is released, glutamate is removed from the synaptic cleft by excitatory amino acid transporter s EAATs , of which there are five types. Glutamate taken up by glial cells is then converted into glutamine by glutamine synthetase , and transported out of the cells into the nerve terminal. This allows synaptic terminals and glial cells to work together in order to maintain a proper supply of glutamate. ref name Purves At GABAergic synapses, the cycle is called the GABA glutamine cycle. Here the glutamine taken up by neurons is converted to glutamate, which is then metabolized into GABA by glutamate decarboxylase . Upon release, GABA is taken up by glial cells via GABA transporters , metabolized into succinate, then in a series of steps to alpha ketoglutarate and then back to glutamine via glutamate. ref cite journal author Bak LK, Schousboe A, Waagepetersen HS title The glutamate GABA glutamine cycle aspects of transport, neurotransmitter homeostasis and ammonia transfer journal J. Neurochem. volume ... url ref References reflist 1 Category Molecular biology molecular cell biology stub ... more details
17beta dehydrogenase or 17 dehydrogenase may refer to Estradiol 17beta dehydrogenase Testosterone 17beta dehydrogenase 17Beta Hydroxysteroid dehydrogenase dab ... more details
enzyme Name methylamine glutamate N methyltransferase EC number 2.1.1.21 CAS number 9045 32 3 IUBMB EC number 2 11 21 GO code 0047148 image width caption In enzymology , a methylamine glutamate N methyltransferase EC number 2.1.1.21 is an enzyme that catalysis catalyzes the chemical reaction methylamine L glutamate math rightleftharpoons math NH sub 3 sub N methyl L glutamate Thus, the two substrate biochemistry substrates of this enzyme are methylamine and L glutamate , whereas its two product chemistry products are ammonia NH sub 3 sub and N methyl L glutamate . This enzyme belongs to the family of transferase s, specifically those transferring one carbon group methyltransferases. The systematic name of this enzyme class is methylamine L glutamate N methyltransferase . Other names in common use include N methylglutamate synthase , and methylamine glutamate methyltransferase . This enzyme participates in methane metabolism . References reflist 1 cite journal author Shaw WV, Tsai L, Stadtman ER date 1966 title The enzymatic synthesis of N methylglutamic acid journal J. Biol. Chem. volume 241 pages 935&ndash 45 pmid 5905132 issue 4 transferase stub Category EC 2.1.1 Category Enzymes of unknown structure it Metilammina glutammato N metiltransferasi ... more details
enzyme Name D glutamate cyclase EC number 4.2.1.48 CAS number 37290 80 5 IUBMB EC number 4 2 1 48 GO code 0047820 image width caption In enzymology , a D glutamate cyclase EC number 4.2.1.48 is an enzyme that catalysis catalyzes the chemical reaction D glutamate math rightleftharpoons math 5 oxo D proline H sub 2 sub O Hence, this enzyme has one substrate biochemistry substrate , D glutamate , and two product chemistry products , 5 oxo D proline and water H sub 2 sub O . This enzyme belongs to the family of lyase s, specifically the hydro lyases, which cleave carbon oxygen bonds. The systematic name of this enzyme class is D glutamate hydro lyase cyclizing 5 oxo D proline forming . This enzyme is also called D glutamate hydro lyase cyclizing . This enzyme participates in d glutamine and d glutamate metabolism . References reflist 1 cite journal author MEISTER A, BUKENBERGER MW, STRASSBURGER M date 1963 title THE OPTICALLY SPECIFIC ENZYMATIC CYCLIZATION OF D GLUTAMATE journal Biochem. Z. volume 338 pages 217&ndash 29 pmid 14087295 4.2 enzyme stub Category EC 4.2.1 Category Enzymes of unknown structure ... more details
unreferenced date November 2010 protein name dihydropyrimidine dehydrogenase caption image width HGNCid 3012 Symbol DPYD AltSymbols EntrezGene 1806 OMIM 274270 RefSeq NM 000110 UniProt PDB ECnumber 1.3.1.2 Chromosome 1 Arm p Band 22 LocusSupplementaryData Dihydropyrimidine dehydrogenase DPD is an enzyme that is involved in pyrimidine degradation. It is the initial and rate limiting step in pyrimidine catabolism. It catalyzes the reduction of uracil and thymine . It is also involved in the degradation of the chemotherapeutic drugs 5 fluorouracil and Tegafur uracil . See also Dihydropyrimidine dehydrogenase deficiency External links enzyme stub Nucleotide metabolism de Dihydropyrimidin Dehydrogenase ... more details
enzyme Name 3 Hydroxybutyrate dehydrogenase EC number 1.1.1.30 CAS number 9028 38 0 IUBMB EC number 111 30 GO code 0003858 image width caption In enzyme enzymology , a 3 hydroxybutyrate dehydrogenase EC number 1.1.1.30 is an enzyme that catalysis catalyzes the chemical reaction R 3 hydroxybutanoate NAD sup sup math rightleftharpoons math acetoacetate NADH H sup sup Thus, the two substrate biochemistry substrates of this enzyme are beta Hydroxybutyric acid R 3 hydroxybutanoate and nicotinamide adenine dinucleotide NAD sup sup , whereas its 3 product chemistry products are acetoacetic acid acetoacetate , nicotinamide adenine dinucleotide NADH , and hydrogen ion H sup sup . This enzyme belongs to the family of oxidoreductase s, to be specific, those acting on the CH OH group of donor with NAD or NADP as acceptor. The systematic name of this enzyme class is R 3 hydroxybutanoate NAD oxidoreductase . Other names in common use include NAD beta hydroxybutyrate dehydrogenase , hydroxybutyrate oxidoreductase , beta hydroxybutyrate dehydrogenase , D beta hydroxybutyrate dehydrogenase , D 3 hydroxybutyrate dehydrogenase , D 3 hydroxybutyrate dehydrogenase , beta hydroxybutyric acid dehydrogenase , 3 D hydroxybutyrate dehydrogenase , and beta hydroxybutyric dehydrogenase . This enzyme participates in ketone Biochemistry synthesis and degradation of ketone bodies and Butanoate Butanoate fermentation butanoate metabolism . Structural studies As of late 2007, two tertiary structure structures ... and PDB link 1X1T . See also BDH1 References reflist 1 cite journal author Bergmeyer HU, Gawehn ... hydroxybutyrate dehydrogenase from Rhodopseudomonas spheroides journal Biochem. J. volume 102 pages ... 1965 title beta Hydroxybutyric dehydrogenase and dimer hydrolase of Pseudomonas lemoignei journal ... HC and Wise JB date 1960 title D beta Hydroxybutyric dehydrogenase of mitochondria journal J. Biol ... dependent enzymes Category Enzymes of known structure de D beta Hydroxybutyrat Dehydrogenase it 3 idrossibutirrato ... more details
enzyme Name glutamate synthase NADPH EC number 1.4.1.13 CAS number 37213 53 9 IUBMB EC number 1 4 1 13 GO code 0004355 image width caption In enzymology , a glutamate synthase NADPH EC number 1.4.1.13 is an enzyme that catalysis catalyzes the chemical reaction L glutamine 2 oxoglutarate NADPH H sup sup math rightleftharpoons math 2 L glutamate NADP sup sup Thus, the four substrate biochemistry substrates of this enzyme are L glutamine , 2 oxoglutarate ketoglutarate , nicotinamide adenine dinucleotide phosphate NADPH , and hydrogen ion H sup sup , whereas the two product chemistry products are L glutamate and nicotinamide adenine dinucleotide phosphate NADP 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. This enzyme participates in glutamate metabolism and nitrogen metabolism . It has 5 ... reflist 1 Further reading refbegin cite journal author Miller RE, Stadtman ER year 1972 title Glutamate ... glutamate for the glutamine synthetase reaction. ref cite journal author Temple SJ, Vance CP, Gantt JS year 1998 title Glutamate synthase and nitrogen assimilation journal Trends in Plant Science ... journal author Vanoni MA, Curti B title Structure function studies of glutamate synthases a class of self ... The systematic name of this enzyme class is L glutamate NADP oxidoreductase transaminating . Other names in common use include div col colwidth 30em glutamate reduced nicotinamide adenine dinucleotide phosphate , synthase, glutamate synthase NADPH , glutamate synthetase NADP , glutamine amide 2 oxoglutarate aminotransferase oxidoreductase, NADP , glutamine ketoglutaric aminotransferase, L glutamate synthase, L glutamate synthetase, L glutamine 2 oxoglutarate aminotransferase, NADPH oxidizing, NADPH dependent glutamate synthase, NADPH glutamate synthase, and NADPH linked glutamate synthase. Div ... title Synthesis of glutamate in Aerobacter aerogenes by a hitherto unknown route journal Biochem ... more details
enzyme Name glycerol dehydrogenase EC number 1.1.1.6 CAS number 9028 14 2 IUBMB EC number 111 6 GO code 0008888 image 1jqa assembly.png width caption Glycerol dehydrogenase from B. stearothermophilus with glycerol spheres Protein Data Bank PDB 1jqa In enzymology , a glycerol dehydrogenase EC number 1.1.1.6 is an enzyme that catalysis catalyzes the chemical reaction glycerol NAD sup sup math rightleftharpoons math glycerone NADH H sup sup Thus, the two substrate biochemistry substrates of this enzyme are glycerol and nicotinamide adenine dinucleotide NAD sup sup , whereas its three product chemistry products are glycerone , 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 glycerol NAD 2 oxidoreductase . Other names in common use include glycerin dehydrogenase , and NAD linked glycerol dehydrogenase . This enzyme participates in glycerolipid metabolism . Structural studies Structural studies have shown that the enzyme is zinc dependant with the active site lying between the two domains of the protein. The NAD binding site resembles the Rossmann fold ref Glycerol dehydrogenase. structure, specificity, and mechanism of a family III polyol dehydrogenase. Ruzheinikov et al. Structure ... for this class of enzyme can be found in the info box. See also Glycerol dehydrogenase NADP Glycerol dehydrogenase acceptor References reflist 1 cite journal author ASNIS RE, BRODIE AF year 1953 title A glycerol dehydrogenase from Escherichia coli journal J. Biol. Chem. volume 203 pages 153&ndash 9 pmid 13069498 issue 1 cite journal author Burton RM and Kaplan NO year 1953 title A DPN specific glycerol dehydrogenase from Aerobacter aerogenes journal J. Am. Chem. Soc. volume 75 pages 1005&ndash ... of glycerol dehydrogenase from Aerobacter aerogenes by monovalent cations journal J. Biol ... more details
Amine Dehydrogenase EC number 1.4.99.3 , also known as methylamine dehydrogenase MADH , is a tryptophan tryptophylquinone dependent TTQ dependent enzyme that catalysis catalyzes the oxidative deamination of a primary amine to an aldehyde and ammonia . The reaction occurs as follows RCH sub 2 sub NH sub 2 sub H sub 2 sub O Electron acceptor acceptor RCHO ammonia NH sub 3 sub redox reduced acceptor Amine dehydrogenase possesses an sub 2 sub sub 2 sub structure with each smaller subunit possessing a TTQ protein Cofactor biochemistry cofactor . Amine dehydrogenase, studied in Paracoccus denitrificans , at least transiently forms a ternary complex to catalyze methylamine dependent cytochrome c 551i reduction. Within this complex, electrons are transferred from the TTQ cofactor of MADH to the Type 1 copper center of amicyanin, and then to the heme of the cytochrome . References cite journal author Davidson VL title Electron transfer in quinoproteins journal Arch. Biochem. Biophys. volume 428 issue 1 pages 32 40 year 2004 pmid 15234267 doi 10.1016 j.abb.2004.03.022 External links MeshName methylamine dehydrogenase CH NH2 oxidoreductases Category Enzymes organic compound stub enzyme stub it Ammina deidrogenasi ja ... more details
enzyme Name 12 alpha hydroxysteroid dehydrogenase EC number 1.1.1.176 CAS number 61642 40 8 IUBMB EC number 111 176 GO code 0047013 image width caption In enzymology , a 12alpha hydroxysteroid dehydrogenase EC number 1.1.1.176 is an enzyme that catalysis catalyzes the chemical reaction 3alpha,7alpha,12alpha trihydroxy 5beta cholanate NADP sup sup math rightleftharpoons math 3alpha,7alpha dihydroxy 12 oxo 5beta cholanate NADPH H sup sup Thus, the two substrate biochemistry substrates of this enzyme are 3alpha,7alpha,12alpha trihydroxy 5beta cholanate and nicotinamide adenine dinucleotide phosphate NADP sup sup , whereas its 3 product chemistry products are 3alpha,7alpha dihydroxy 12 oxo 5beta cholanate , 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 OH group of donor with NAD or NADP as acceptor. The systematic name of this enzyme class is 12alpha hydroxysteroid NADP 12 oxidoreductase . Other names in common use include 12alpha hydroxy steroid dehydrogenase , 12alpha hydroxy steroid dehydrogenase , NAD dependent 12alpha hydroxysteroid dehydrogenase , and NADP 12alpha hydroxysteroid dehydrogenase . This enzyme is involved in a metabolic pathway that degrades bile acid s into cholesterol . References reflist 1 cite journal author MacDonald IA, Mahony DE, Jellet JF, Meier CE date 1977 title NAD dependent 3alpha and 12alpha hydroxysteroid dehydrogenase activities from Eubacterium lentum ATCC no. 25559 journal Biochim. Biophys. Acta. volume 489 pages 466&ndash 76 pmid 201289 issue 3 cite journal author Mahony DE, Meier CE, Macdonald IA, Holdeman LV date 1977 title Bile salt degradation by nonfermentative clostridia journal Appl. Environ. Microbiol. volume 34 pages 419&ndash 23 pmid 921266 issue 4 pmc 242673 1.1.1 enzyme stub Category EC 1.1.1 Category NADPH dependent enzymes Category Enzymes of unknown structure it 12alfa idrossisteroide deidrogenasi ... more details
enzyme Name dehydrogluconate dehydrogenase EC number 1.1.99.4 CAS number 9028 82 4 IUBMB EC number 11 99 4 GO code 0047843 image width caption In enzymology , a dehydrogluconate dehydrogenase EC number 1.1.99.4 is an enzyme that catalysis catalyzes the chemical reaction 2 dehydro D gluconate acceptor math rightleftharpoons math 2,5 didehydro D gluconate reduced acceptor Thus, the two substrate biochemistry substrates of this enzyme are 2 dehydro D gluconate and Electron acceptor acceptor , whereas its two product chemistry products are 2,5 didehydro D gluconate and reduced acceptor . This enzyme belongs to the family of oxidoreductase s, specifically those acting on the CH OH group of donor with other acceptors. The systematic name of this enzyme class is 2 dehydro D gluconate acceptor 2 oxidoreductase . Other names in common use include ketogluconate dehydrogenase , alpha ketogluconate dehydrogenase , 2 keto D gluconate dehydrogenase , and 2 oxogluconate dehydrogenase . It has 2 cofactor biochemistry cofactors FAD , and Flavoprotein . References reflist 1 cite journal author DATTA AG, KATZNELSON H date 1956 title The oxidation of 2 ketogluconate by a partially purified enzyme from Acetobactor melanogenum journal Arch. Biochem. Biophys. volume 65 pages 576&ndash 8 pmid 13395514 doi 10.1016 0003 9861 56 90218 1 issue 2 cite journal author Shinagawa E and Ameyama M date 1982 title 2 Keto D gluconate dehydrogenase from Gluconobacter melanogenus, membrane bound journal Methods Enzymol. volume 89 pages 194&ndash 198 doi 10.1016 S0076 6879 82 89034 4 1.1 enzyme stub Category EC 1.1.99 Category Flavin enzymes Category Flavoprotein enzymes Category Enzymes of unknown structure it Deidrogluconato deidrogenasi ja ... 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 glutamate methylamine ligase EC number 6.3.4.12 CAS number 37318 69 7 IUBMB EC number 6 3 4 12 GO code 0047943 image width caption In enzymology , a glutamate methylamine ligase EC number 6.3.4.12 is an enzyme that catalysis catalyzes the chemical reaction ATP L glutamate methylamine math rightleftharpoons math ADP phosphate N sub 5 sub methyl L glutamine The 3 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , L glutamate , and methylamine , whereas its 3 product chemistry products are adenosine diphosphate ADP , phosphate , and N5 methyl L glutamine . This enzyme belongs to the family of ligase s, specifically those forming generic carbon nitrogen bonds. The systematic name of this enzyme class is L glutamate methylamine ligase ADP forming . This enzyme is also called gamma glutamylmethylamide synthetase . References reflist 1 cite journal author Kung HF, Wagner C date 1969 title Gamma glutamylmethylamide. A new intermediate in the metabolism of methylamine journal J. Biol. Chem. volume 244 pages 4136&ndash 40 pmid 5800436 issue 15 ligase stub Category EC 6.3.4 Category Enzymes of unknown structure ... more details
enzyme Name Glutamate putrescine ligase EC number 6.3.1.11 CAS number 914090 78 1 IUBMB EC number 6 3 1 11 GO code image width caption In enzymology , a glutamate putrescine ligase EC number 6.3.1.11 is an enzyme that catalysis catalyzes the chemical reaction ATP L glutamate putrescine math rightleftharpoons math ADP phosphate gamma L glutamylputrescine The 3 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , L glutamate , and putrescine , whereas its 3 product chemistry products are adenosine diphosphate ADP , phosphate , and gamma L glutamylputrescine . This enzyme belongs to the family of ligase s, specifically those forming carbon nitrogen bonds as acid D ammonia or amine ligases amide synthases . The systematic name of this enzyme class is L glutamate putrescine ligase ADP forming . Other names in common use include gamma glutamylputrescine synthetase , and YcjK . This enzyme participates in urea cycle and metabolism of amino groups . References reflist 1 cite journal author Kurihara S, Oda S, Kato K, Kim HG, Koyanagi T, Kumagai H, Suzuki H date 2005 title A novel putrescine utilization pathway involves gamma glutamylated intermediates of Escherichia coli K 12 journal J. Biol. Chem. volume 280 pages 4602&ndash 8 pmid 15590624 doi 10.1074 jbc.M411114200 issue 6 ligase stub Category EC 6.3.1 Category Enzymes of unknown structure ... more details
enzyme Name IMP dehydrogenase EC number 1.1.1.205 CAS number 9028 93 7 IUBMB EC number 111 205 GO code 0003938 image PDB 1meh EBI.jpg width caption Structure of IMPDH ref name pmid12559919 cite journal ... 5 phosphate dehydrogenase of Aerobacter aerogenes journal J. Biol. Chem. volume 226 issue 1 pages ... dehydrogenase isozymes protein Name IMPDH1 IMP dehydrogenase1 caption image width HGNCid 6052 Symbol ... dehydrogenase in complex with substrate, cofactor and analogs a structural basis for the random in ordered ... February pmid 12559919 doi 10.1016 S0022 2836 02 01383 9 url ref IMP dehydrogenase EC number 1.1.1.205 Inosine 5 monophosphate dehydrogenase Inosinic acid dehydrogenaseis IMPDH an enzyme that converts ... Turner JF, King JE title Inosine 5 phosphate dehydrogenase of pea seeds journal Biochem. J. volume ... cite journal author Hedstrom L title IMP dehydrogenase structure, mechanism, and inhibition ... title Inosine 5 monophosphate dehydrogenase journal Adv. Enzymol. Relat. Areas Mol. Biol. volume 76 issue pages 1 53 year 2009 pmid 18990827 doi url issn ref inosine monophosphate inosine 5 phosphate ... title Cloning and sequence analysis of the human and Chinese hamster inosine 5 monophosphate dehydrogenase ... 2902093 doi url ref IMP dehydrogenase is associated with Cell growth cell proliferation and is a possible ... s of identical polymer chain s. There are two IMP dehydrogenase isozymes in Homo sapiens human s. ref ... title Two distinct cDNAs for human IMP dehydrogenase journal J. Biol. Chem. volume 265 issue 9 pages 5292 5 year 1990 month March pmid 1969416 doi url ref IMP dehydrogenase nearly always contains a long ... Chromosome 7 Arm q Band 31.3 LocusSupplementaryData q32 protein Name IMPDH2 IMP dehydrogenase ... See also Purine metabolism References reflist 1 Further reading refbegin cite journal author Wang ... stub InterPro content IPR001093 DEFAULTSORT Imp Dehydrogenase Category EC 1.1.1 de Inosinmonophosphat Dehydrogenase it IMP deidrogenasi ja IMP pl Dehydrogenaza IMP ... more details
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