| glutamine-pyruvate aminotransferase | <enzyme> Consider also glutamine transaminase k if cysteine conjugate beta-lyase activity is also present; l-methionine can act as donor; glyoxylate can act as acceptor Registry number: EC 2.6.1.15 Synonym: glutamine alpha-ketoacid transaminase, glutamine transaminase, glutamine transaminase l, glutamine oxo-acid aminotransferase, glutaminase II, glutamine aminotransferase, l-methionine aminotransferase (26 Jun 1999) |
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| chorismate pyruvate-lyase | <enzyme> Forms 4-hydroxybenzoic acid for ubiquinone biosynthesis; chorismate pyruvate-lyase (amino-accepting) is anthranilate synthase Registry number: EC 4.1.3.- Synonym: ubic gene product, chorismate lyase (26 Jun 1999) |
| serine-pyruvate aminotransferase | <enzyme> Do not confuse with alanine-glyoxylate aminotransferase (EC 2.6.1.44), even though they may be products of the same gene; index whichever is discussed or both Registry number: EC 2.6.1.51 Synonym: serine aminotransferase, serine-pyruvate transaminase (26 Jun 1999) |
| pyruvate | <biochemistry> Pyruvate is the final product of glycolysis. You get two molecules of pyruvate for every molecule of glucose that goes through glycolysis. (22 Aug 1998) |
| pyruvate decarboxylase | <enzyme> Catalyses the decarboxylation of an alpha keto acid to an aldehyde and carbon dioxide. Thiamine pyrophosphate is an essential cofactor. In lower organisms, which ferment glucose to ethanol and carbon dioxide, the enzyme irreversibly decarboxylates pyruvate to acetaldehyde. Registry number: EC 4.1.1.1 (12 Dec 1998) |
| pyruvate dehydrogenase | <enzyme> A complex multienzyme system that catalyses the conversion of (pyruvate + CoA + NAD) to (acetyl CoA + CO2 + NAD). (18 Nov 1997) |
| pyruvate dehydrogenase complex | <enzyme> A complex multienzyme system that catalyses the conversion of (pyruvate + CoA + NAD) to (acetyl CoA + CO2 + NAD). (18 Nov 1997) |
| pyruvate dehydrogenase complex inactivase | <enzyme> Pharmacological action: enzyme inhibitor Registry number: EC 3.4.- (26 Jun 1999) |
| pyruvate dehydrogenase (cytochrome) | An oxidoreductase catalyzing reaction between ferricytochrome b1 and pyruvate to yield acetate and CO2, and ferrocytochrome b1. (05 Mar 2000) |
| pyruvate dehydrogenase (lipoamide) | An oxidoreductase catalyzing conversion of pyruvate and (oxidised) lipoamide to CO2 and S6-acetyldihydrolipoamide in two successive reactions: the first between pyruvate and thiamin pyrophosphate to yield CO2 and alpha-hydroxyethylthiamin pyrophosphate (active pyruvate); the second between the last named and lipoamide to regain the thiamin pyrophosphate and yield S6-acetylhydrolipoamide. Compare: alpha-ketodecarboxylase. (05 Mar 2000) |
| pyruvate dehydrogenase (lipoamide)-phosphatase | <enzyme> (pyruvate dehydrogenase (lipoamide))-phosphate phosphohydrolase. A mitochondrial enzyme that catalyses the hydrolytic removal of a phosphate on a specific seryl hydroxyl group of pyruvate dehydrogenase, reactivating the enzyme complex. Registry number: EC 3.1.3.43 (12 Dec 1998) |
| pyruvate-formate-lyase-deactivase | <chemical> Encoded by adhe gene product from E coli; pfla (radical form) yields pfl (non-radical form) in presence of fe++, nad and CoA and the multienzyme complex consisting of alcohol plus acetaldehyde-CoA dehydrogenase activities Synonym: pfl-deactivase, adhe multienzyme, adhe gene product (26 Jun 1999) |
| pyruvate kinase | <enzyme> ATP:pyruvate 2-o-phosphotransferase. A phosphotransferase that catalyses reversibly the phosphorylation of pyruvate to phosphoenolpyruvate in the presence of ATP. It has four isozymes (l, r, m1, and m2). Deficiency of the enzyme results in haemolytic anaemia. Registry number: EC 2.7.1.40 (12 Dec 1998) |
| pyruvate kinase phosphatase | <enzyme> Reactivates pyruvate kinase Registry number: EC 3.1.3.- (26 Jun 1999) |
| pyruvate metabolism, inborn errors | Hereditary disorders of pyruvate metabolism. They are difficult to diagnose and describe because pyruvate is a key intermediate in glycolysis, gluconeogenesis, and the tricarboxylic acid cycle. Some inherited metabolic disorders may alter pyruvate metabolism indirectly. Disorders in pyruvate metabolism appear to lead to deficiencies in neurotransmitter synthesis and, consequently, to nervous system disorders. (12 Dec 1998) |