About the enzyme that forms acetaldehyde the enzyme that feeds the citric acid cycle pyruvate dehydrogenase enzyme Name Pyruvatedecarboxylase 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 pyruvatedecarboxylase br pyruvate thiamine pyrophasphate TPP hydroxyethyl TPP CO sub 2 sub Pyruvatedecarboxylase .... Pyruvatedecarboxylase starts this process by converting pyruvate into acetaldehyde and carbon ... ref Pyruvatedecarboxylase depends on Cofactor biochemistry cofactors thiamine pyrophosphate TPP ... CoA . Yeast In yeast, pyruvatedecarboxylase acts independently during wikt anaerobic anaerobic fermentation and releases the 2 carbon fragment as acetaldehyde plus carbon dioxide. Pyruvatedecarboxylase ... F title Catalytic centers in the thiamin diphosphate dependent enzyme pyruvatedecarboxylase at 2.4 ... keto acid pyruvate to meet. ref name pmid8512926 Structure Pyruvatedecarboxylase occurs as a dimer ... B, Jordan F title Catalytic centers in the thiamin diphosphate dependent enzyme pyruvatedecarboxylase ... decarboxylase width 275 lines 3 Image 1pvd with TPP.jpg Cartoon diagram of pyruvatedecarboxylase monomer with TPP attached. Image 1pvd image.jpg Cartoon diagram of pyruvatedecarboxylase tetramer. Image PDC chimera cropped r3 c4.jpg Active site of pyruvatedecarboxylase with selected amino acids ... DHG title PyruvateDecarboxylase A Molecular Modeling Study of Pyruvate Decarboxylation and Acyloin ... at the substrate activation site of yeast pyruvatedecarboxylase inhibition by distortion ..., His 115, and Gln 477. ref name pmid9477950 The normal catalytic rate of pyruvatedecarboxylase is k ..., which is held by the enzyme pyruvatedecarboxylase. During the decarboxylation of pyruvate, the TPP ... is attached to the five membered TPP ring in its ylid form. File Pyruvatedecarboxylase mechanism.png ... acid carboxylase, alpha ketoacid carboxylase, and pyruvic decarboxylase. ref name urlENZYME entry ... more details
enzyme Name 2,2 dialkylglycine decarboxylasepyruvate 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 decarboxylasepyruvate 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 pyruvatedecarboxylase , alpha dialkyl amino acid transaminase , 2,2 dialkyl 2 amino acid pyruvate aminotransferase , L alanine alpha ketobutyrate aminotransferase , dialkylamino acid decarboxylasepyruvate , 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 DecarboxylasePyruvate Category EC 4.1.1 Category Pyridoxal phosphate enzymes Category Enzymes of known ... more details
About the enzyme that preceeds the citric acid cycle the enzyme that forms acetaldehyde pyruvatedecarboxylase ... 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 pyruvate into acetyl CoA by a process called pyruvate decarboxylation . Acetyl CoA may then be used 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 ... , NADH , and Acetyl CoA . Image 1400x1048 pdh regulation.png 400 px center alt Regulation of Pyruvate Dehydrogenase Mechanism File PyruvateDehydrgenaseMech1.gif Pyruvate Dehydrogenase Mechanism The ylide resonance form of thiamine pyrophosphate TPP begins by attacking the electrophilic ketone of pyruvate ... C2 carbanion, eventually. After the cofactor TPP decarboxylates pyruvate, the acetyl ... for flip flop action of thiamin pyrophosphate dependent enzymes revealed by human pyruvate dehydrogenase ... A, Chandrasekhar K, Sax M, Yan Y, Jordan F, Guest JR, Furey W. title Structure of the pyruvate ... more details
enzyme Name Acetylenedicarboxylate decarboxylase EC number 4.1.1.78 CAS number 72561 10 5 IUBMB EC number 4 1 1 78 GO code 0050476 image width caption In enzymology , an acetylenedicarboxylate decarboxylase EC number 4.1.1.78 is an enzyme that catalysis catalyzes the chemical reaction acetylenedicarboxylate H sub 2 sub O math rightleftharpoons math pyruvate CO sub 2 sub Thus, the two enzyme substrate substrates of this enzyme are acetylenedicarboxylic acid acetylenedicarboxylate and water H sub 2 sub O , whereas its two product chemistry products are pyruvate and carbon dioxide CO sub 2 sub . 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 acetylenedicarboxylate carboxy lyase pyruvate forming . Other names in common use include acetylenedicarboxylate hydratase , acetylenedicarboxylate hydrase , and acetylenedicarboxylate carboxy lyase . This enzyme participates in pyruvate metabolism . References reflist 1 cite journal author Yamada EW and Jakoby WB date 1958 title Enzymatic utilization of acetylenic compounds. I. An enzyme converting acetylenedicarboxylic acid to pyruvate journal J. Biol. Chem. volume 233 pages 706&ndash 711 pmid 13575441 issue 3 4.1 enzyme stub Category EC 4.1.1 Category Enzymes of unknown structure ... more details
enzyme Name indolepyruvate decarboxylase EC number 4.1.1.74 CAS number 9074 92 4 IUBMB EC number 4 1 1 74 GO code 0047434 image width caption In enzymology , an indolepyruvate decarboxylase EC number 4.1.1.74 is an enzyme that catalysis catalyzes the chemical reaction 3 indol 3 yl pyruvate math rightleftharpoons math 2 indol 3 yl acetaldehyde CO sub 2 sub Hence, this enzyme has one substrate biochemistry substrate , 3 indol 3 yl pyruvate , and two product chemistry products , 2 indol 3 yl acetaldehyde and carbon dioxide CO sub 2 sub . 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 3 indol 3 yl pyruvate carboxy lyase 2 indol 3 yl acetaldehyde forming . Other names in common use include indol 3 yl pyruvate carboxy lyase , and 3 indol 3 yl pyruvate carboxy lyase . This enzyme participates in tryptophan 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 1OVM . References reflist 1 cite journal author Koga J date 1995 title Structure and function of indolepyruvate decarboxylase, a key enzyme in indole 3 acetic acid biosynthesis journal Biochim. Biophys. Acta. volume 1249 pages 1&ndash 13 pmid 7766676 issue 1 doi 10.1016 0167 4838 95 00011 I 4.1 enzyme stub Category EC 4.1.1 Category Enzymes of known structure ... more details
enzyme Name phosphatidylserine decarboxylase EC number 4.1.1.65 CAS number 9054 78 8 IUBMB EC number 4 1 1 65 GO code 0004609 image width caption In enzymology , a phosphatidylserine decarboxylase EC number 4.1.1.65 is an enzyme that catalysis catalyzes the chemical reaction phosphatidyl L serine math rightleftharpoons math phosphatidylethanolamine CO sub 2 sub Hence, this enzyme has one substrate biochemistry substrate , phosphatidyl L serine , and two product chemistry products , phosphatidylethanolamine and carbon dioxide CO sub 2 sub . 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 phosphatidyl L serine carboxy lyase phosphatidylethanolamine forming . Other names in common use include PS decarboxylase , and phosphatidyl L serine carboxy lyase . This enzyme participates in glycine, serine and threonine metabolism and glycerophospholipid metabolism . It has 2 cofactor biochemistry cofactors pyridoxal phosphate , and Pyruvate . References reflist 1 refbegin cite journal author KANFER J, KENNEDY EP date 1964 title METABOLISM AND FUNCTION OF BACTERIAL LIPIDS. II. BIOSYNTHESIS OF PHOSPHOLIPIDS IN ESCHERICHIA COLI journal J. Biol. Chem. volume 239 pages 1720&ndash 6 pmid 14213340 cite journal author Satre M, Kennedy EP date 1978 title Identification of bound pyruvate essential for the activity of phosphatidylserine decarboxylase of Escherichia coli journal J. Biol. Chem. volume 253 pages 479&ndash 83 pmid 338609 issue 2 refend 4.1 enzyme stub Category EC 4.1.1 Category Pyridoxal phosphate enzymes Category Pyruvate enzymes Category Enzymes of unknown structure ... more details
enzyme Name oxaloacetate decarboxylase EC number 4.1.1.3 CAS number 9024 98 0 IUBMB EC number 4 1 1 3 GO code 0008948 image width caption Infobox protein family Symbol OAD beta Name Na transporting oxaloacetate decarboxylase beta subunit image width caption Pfam PF03977 Pfam clan CL0064 InterPro IPR005661 SMART PROSITE MEROPS SCOP TCDB 3.B.1 OPM family OPM protein CAZy CDD Infobox protein family Symbol OAD gamma Name Oxaloacetate decarboxylase, gamma chain image width caption Pfam PF04277 Pfam clan InterPro IPR005899 SMART PROSITE MEROPS SCOP TCDB 3.B.1 OPM family OPM protein CAZy CDD Oxaloacetate decarboxylase is a carboxy lyases carboxy lyase involved in the conversion of oxaloacetate into pyruvate . It is categorized under EC number 4.1.1.3 . In some bacteria this enzyme is a trimer , composed of alpha, beta and gamma Protein subunit subunits . ref name pmid9428714 cite journal author Bott M, Pfister K, Burda P, Kalbermatter O, Woehlke G, Dimroth P title Methylmalonyl CoA decarboxylase from Propionigenium modestum cloning and sequencing of the structural genes and purification of the enzyme complex journal Eur. J. Biochem. volume 250 issue 2 pages 590 9 year 1997 month December pmid 9428714 doi url ref ref name pmid2549031 cite journal author Laussermair E, Schwarz E, Oesterhelt D, Reinke H, Beyreuther K, Dimroth P title The sodium ion translocating oxaloacetate decarboxylase of Klebsiella pneumoniae. Sequence of the integral membrane bound subunits beta and gamma. journal J Biol Chem year 1989 volume 264 issue 25 pages 14710 5 pmid 2549031 doi pmc url ref The beta and gamma ... author Schmid M, Wild MR, Dahinden P, Dimroth P title Subunit gamma of the oxaloacetate decarboxylase ... prlinks&id 11802728 ref See also Pyruvate carboxylase References reflist Further reading cite journal author Dahinden P, Auchli Y, Granjon T et al. title Oxaloacetate decarboxylase of Vibrio cholerae ... links MeshName oxaloacetate decarboxylase Carbon carbon lyases enzyme stub InterPro content IPR005661 ... more details
P cite journal author Rognstad R title Pyruvate cycling involving possible oxaloacetate decarboxylase ...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 ... A pyruvate cycling pathway involving cytosolic NADP dependent isocitrate dehydrogenase regulates ... 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 ... more details
enzyme Name adenosylmethionine decarboxylase EC number 4.1.1.50 CAS number 9036 20 8 IUBMB EC number 4 1 1 50 GO code 0004014 image width caption protein Name adenosylmethionine decarboxylase 1 caption image width HGNCid 457 Symbol AMD1 AltSymbols EntrezGene 262 OMIM 180980 RefSeq NM 001634 UniProt P17707 PDB ECnumber 4.1.1.50 Chromosome 6 Arm q Band 21 LocusSupplementaryData q22 Infobox protein family Symbol AdoMet dc Name AdoMet decarboxylase image PDB 1tlu EBI.jpg width caption crystal structure of thermotoga maritima s adenosylmethionine decarboxylase Pfam PF02675 Pfam clan InterPro IPR003826 SMART PROSITE MEROPS SCOP TCDB OPM family OPM protein CAZy CDD Adenosylmethionine decarboxylase is an enzyme that catalyzes the conversion of S Adenosyl methionine S adenosyl methionine to S Adenosylmethioninamine S adenosylmethioninamine . Polyamine s such as spermidine and spermine are essential for cell biology cellular cell growth growth under most conditions, being implicated in a large number of cellular processes including DNA, RNA and protein biosynthesis protein synthesis . S adenosylmethionine decarboxylase AdoMetDC plays an essential regulatory role in the polyamine biosynthetic pathway by generating the n propylamine residue required for the synthesis of spermidine and spermine from putrescein. ref name pmid2197977 cite journal author van Poelje PD, Snell EE title Pyruvoyl dependent enzymes journal Annu. Rev. Biochem. volume 59 issue pages 29 59 year 1990 pmid 2197977 doi 10.1146 annurev.bi.59.070190.000333 url ref ref name pmid10047786 cite journal author Pegg AE, Xiong H, Feith DJ, Shantz LM title S adenosylmethionine decarboxylase structure, function and regulation by polyamines journal Biochem. Soc. Trans. volume 26 issue 4 pages 580 6 year 1998 month November pmid 10047786 doi url ref Unlike many amino acid decarboxylases AdoMetDC uses a covalently bound pyruvate ... precursor protein . This cleavage generates the pyruvate precursor from an internal serine ... more details
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 pyruvate dehydrogenase 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 membrane. ref Raven et al. Biology, 8th edition. McGraw Hill, 2008. ISBN 978 0 07 110202 5 ref cellspacing 15 width 25 style border 1px solid a79c83 Enzymatic Reaction foward enzyme pyruvate dehydrogenase complex PDHC reverse enzyme substrate pyruvate Pyr product acetyl CoA Ac CoA reaction direction ... of glycolysis which are cytosol ic. The conversion of pyruvate to acetyl CoA by the pyruvate ... 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
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 ... pathway, which produces pyruvate molecules, the final product of aerobic glycolysis. However, in anaerobic ... dehydrogenase to reduce pyruvate to lactate. In humans, there are two pyruvate kinase isozymes type ... 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 ... or more occasions. In some cases, the same organism will have both Pyruvate kinase and PPDK. ref ... 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
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 ... gallery title Pyruvate Carboxylase Symmetry Comparison width 200 height 150 lines 2 Pyruvate Carboxylase 2QF7, sswilson7.png Rhizobium Rhizobium etli Rhizobium Rhizobium etli Pyruvate carboxylase 3HO8 ... more details
, Snell EE title Histidine decarboxylase of Lactobacillus 30a. IV. The presence of covalently bound pyruvate ...enzyme Name histidine decarboxylase EC number 4.1.1.22 CAS number 9024 61 7 IUBMB EC number 4 1 1 22 ... by histidine decarboxylase Infobox protein family Symbol HDC Name Histidine carboxylase PI chain image PDB 1ibt EBI.jpg width caption structure of the d53,54n mutant of histidine decarboxylase ... protein CAZy CDD PBB geneid 3067 Histidine decarboxylase HDC is the enzyme that catalyzes the reaction ... histidine decarboxylase from Cl. welchii Type A journal Biochem. J. volume 39 issue 1 pages 42 6 year ... J, Guirard BM, Chang GW, Snell EE title Purification and properties of histidine decarboxylase ... decarboxylase catechin , tritoqualine an atypical antihistaminic Hypostamin . histidine C ... dioxide CO sub 2 sub In humans, the histidine decarboxylase enzyme is encoded by the HDC gene . ref name entrez cite web title Entrez Gene histidine decarboxylase url http www.ncbi.nlm.nih.gov sites entrez ... decarboxylase HDC cDNA probe by PCR and assignment of the human HDC gene to chromosome 15 journal ... histidine is catalyzed by the enzyme L histidine decarboxylase. This homodimeric enzyme is a pyridoxal phosphate PLP dependent decarboxylase and is highly specific for its histidine substrate. ref name ... of Tourette syndrome. ref cite web title Online Mendelian Inheritance in Man histidine decarboxylase ... author Masini E, Fabbroni V, Giannini L, et al. title Histamine and histidine decarboxylase up regulation ..., Tang F, et al. title Expression of non mast cell histidine decarboxylase in tumor associated microvessels ... M, Wang TC title Kruppel like factor 4 KLF4 represses histidine decarboxylase gene expression through ... response element GAS RE3 in the human histidine decarboxylase gene promoter. journal Biochem. Biophys .... title Histidine decarboxylase, a pyridoxal phosphate dependent enzyme, is an autoantigen of gastric ... M title Differential activity of histidine decarboxylase in normal and pre eclamptic placentae. journal ... 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 2 oxoglutarate decarboxylase EC number 4.1.1.71 CAS number 37205 42 8 IUBMB EC number 4 1 1 71 GO code 0008683 image width caption In enzymology , a 2 oxoglutarate decarboxylase EC number 4.1.1.71 is an enzyme that catalysis catalyzes the chemical reaction 2 oxoglutarate math rightleftharpoons math succinate semialdehyde CO sub 2 sub Hence, this enzyme has one substrate biochemistry substrate , 2 oxoglutarate , and two product chemistry products , succinate semialdehyde and carbon dioxide CO sub 2 sub . 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 oxoglutarate carboxy lyase succinate semialdehyde forming . Other names in common use include oxoglutarate decarboxylase , alpha ketoglutarate decarboxylase , alpha ketoglutaric decarboxylase , oxoglutarate decarboxylase , pre 2 oxoglutarate decarboxylase , and 2 oxoglutarate carboxy lyase . It employs one cofactor biochemistry cofactor , thiamin diphosphate . References reflist 1 cite journal author Shigeoka S, Onishi T, Maeda K, Nakano Y and Kitaoka S date 1986 title Occurrence of thiamin pyrophosphate dependent 2 oxoglutarate decarboxylase in mitochondria of Euglena gracilis journal FEBS Lett. volume 195 pages 43&ndash 47 doi 10.1016 0014 5793 86 80126 0 4.1 enzyme stub Category EC 4.1.1 Category Thiamine enzymes Category Enzymes of unknown structure ... more details
enzyme Name sulfinoalanine decarboxylase EC number 4.1.1.29 CAS number 62213 10 9 IUBMB EC number 4 1 1 29 GO code 0004782 image width caption In enzymology , a sulfinoalanine decarboxylase EC number 4.1.1.29 is an enzyme that catalysis catalyzes the chemical reaction 3 sulfino L alanine math rightleftharpoons math hypotaurine CO sub 2 sub Hence, this enzyme has one substrate biochemistry substrate , 3 sulfino L alanine , and two product chemistry products , hypotaurine and carbon dioxide CO sub 2 sub . 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 3 sulfino L alanine carboxy lyase hypotaurine forming . Other names in common use include cysteine sulfinate decarboxylase , L cysteinesulfinic acid decarboxylase , cysteine sulfinate decarboxylase , CADCase CSADCase , CSAD , cysteic decarboxylase , cysteinesulfinic acid decarboxylase , cysteinesulfinate decarboxylase , sulfoalanine decarboxylase , and 3 sulfino L alanine carboxy lyase . This enzyme participates in taurine and hypotaurine metabolism . It employs one cofactor biochemistry cofactor , pyridoxal phosphate . 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 2JIS . References reflist 1 cite journal author Guion Rain M C, Portemer C, Chatagner F date 1975 title Rat liver cysteine sulfinate decarboxylase purification, new appraisal of the molecular weight and determination of catalytic properties journal Biochim. Biophys. Acta. volume 384 pages 265&ndash 76 pmid 236774 issue 1 cite journal author JACOBSEN JG, THOMAS LL, SMITH LH Jr date 1964 title PROPERTIES AND DISTRIBUTION OF MAMMALIAN L CYSTEINE SULFINATE CARBOXY LYASES journal Biochim. Biophys. Acta. volume 85 pages 103&ndash 16 pmid 14159288 4.1 enzyme stub Category EC 4.1.1 Category Pyridoxal phosphate enzymes Category Enzymes of known ... more details
enzyme Name 3 oxolaurate decarboxylase EC number 4.1.1.56 CAS number 37290 49 6 IUBMB EC number 4 1 1 56 GO code 0050410 image width caption In enzymology , a 3 oxolaurate decarboxylase EC number 4.1.1.56 is an enzyme that catalysis catalyzes the chemical reaction 3 oxododecanoate math rightleftharpoons math 2 undecanone CO sub 2 sub Hence, this enzyme has one substrate biochemistry substrate , 3 oxododecanoate , and two product chemistry products , 2 undecanone and carbon dioxide CO sub 2 sub . 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 3 oxododecanoate carboxy lyase 2 undecanone forming . Other names in common use include beta ketolaurate decarboxylase , beta ketoacyl decarboxylase , and 3 oxododecanoate carboxy lyase . References reflist 1 cite journal author FRANKE W, PLATZECK A, EICHHORN G date 1961 title On the knowledge of fatty acid catabolism by mold fungi. III. On a decarboxylase for average beta ketomonocarbonic acids beta ketolaurate decarboxylase journal Arch. Mikrobiol. volume 40 issue 1 pages 73&ndash 93 pmid 13701396 doi 10.1007 BF00408834 4.1 enzyme stub Category EC 4.1.1 Category Enzymes of unknown structure ... more details
enzyme Name 6 methylsalicylate decarboxylase EC number 4.1.1.52 CAS number 37289 50 2 IUBMB EC number 4 1 1 52 GO code 0047596 image width caption In enzymology , a 6 methylsalicylate decarboxylase EC number 4.1.1.52 is an enzyme that catalysis catalyzes the chemical reaction 6 methylsalicylate math rightleftharpoons math 3 cresol CO sub 2 sub Hence, this enzyme has one substrate biochemistry substrate , 6 methylsalicylate , and two product chemistry products , 3 cresol and carbon dioxide CO sub 2 sub . 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 6 methylsalicylate carboxy lyase 3 cresol forming . Other names in common use include 6 methylsalicylic acid 2,6 cresotic acid decarboxylase , 6 MSA decarboxylase , and 6 methylsalicylate carboxy lyase . References reflist 1 cite journal author Light RJ date 1969 title 6 methylsalicylic acid decarboxylase from Penicillium patulum journal Biochim. Biophys. Acta. volume 191 pages 430&ndash 8 pmid 5354271 issue 2 doi 10.1016 0005 2744 69 90262 9 cite journal author Vogel G and Lynen F date 1970 title 6 Methylsalicylsaure Decarboxylase journal Naturwissenschaften volume 57 page 664 doi 10.1007 BF00598791 4.1 enzyme stub Category EC 4.1.1 Category Enzymes of unknown structure ... more details
enzyme Name diaminopimelate decarboxylase EC number 4.1.1.20 CAS number 9024 75 3 IUBMB EC number 4 1 1 20 GO code 0008836 image width caption In enzymology , a diaminopimelate decarboxylase EC number 4.1.1.20 is an enzyme that catalysis catalyzes the chemical reaction meso 2,6 diaminoheptanedioate math rightleftharpoons math L lysine CO sub 2 sub Hence, this enzyme has one substrate biochemistry substrate , meso 2,6 diaminoheptanedioate , and two product chemistry products , L lysine and carbon dioxide CO sub 2 sub . 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 meso 2,6 diaminoheptanedioate carboxy lyase L lysine forming . Other names in common use include diaminopimelic acid decarboxylase , meso diaminopimelate decarboxylase , DAP decarboxylase , and meso 2,6 diaminoheptanedioate carboxy lyase . This enzyme participates in lysine biosynthesis . It employs one cofactor biochemistry cofactor , pyridoxal phosphate . Structural studies As of late 2007, 8 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1HKV , PDB link 1HKW , PDB link 1KNW , PDB link 1KO0 , PDB link 1TUF , PDB link 1TWI , PDB link 2O0T , and PDB link 2P3E . References reflist cite doi 10.1016 0006 3002 55 90257 2 4.1 enzyme stub Category EC 4.1.1 Category Pyridoxal phosphate enzymes Category Enzymes of known structure ... more details
enzyme Name diphosphomevalonate decarboxylase EC number 4.1.1.33 CAS number 9024 66 2 IUBMB EC number 4 1 1 33 GO code 0004163 image width caption In enzymology , a diphosphomevalonate decarboxylase EC number 4.1.1.33 is an enzyme that catalysis catalyzes the chemical reaction ATP R 5 diphosphomevalonate math rightleftharpoons math ADP phosphate isopentenyl diphosphate CO sub 2 sub Thus, the two substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP and R 5 diphosphomevalonate , whereas its 4 product chemistry products are adenosine diphosphate ADP , phosphate , isopentenyl diphosphate , and carbon dioxide CO sub 2 sub . 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 ATP R 5 diphosphomevalonate carboxy lyase adding ATP isopentenyl diphosphate forming . Other names in common use include pyrophosphomevalonate decarboxylase , mevalonate 5 pyrophosphate decarboxylase , pyrophosphomevalonic acid decarboxylase , 5 pyrophosphomevalonate decarboxylase , mevalonate 5 diphosphate decarboxylase , and ATP R 5 diphosphomevalonate carboxy lyase dehydrating . This enzyme participates in biosynthesis of steroids . 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 1FI4 , PDB link 2HK2 , PDB link 2HK3 , and PDB link 2HKE . References reflist 1 cite journal author Bloch K, Chaykin S, Phillips AH and de Waard A date 1959 title Mevalonic acid pyrophosphate and isopentenyl pyrophosphate journal J. Biol. Chem. volume 234 pages 2595&ndash 2604 4.1 enzyme stub Category EC 4.1.1 Category Enzymes of known structure ... more details
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