ExplorEnz: EC 1.2.5.1

<!DOCTYPE HTML PUBLIC "-//W3C//DTD HTML 4.0//EN" "http://www.w3.org/TR/REC-html40/strict.dtd"> <html> <head> <title>ExplorEnz: EC 1.2.5.1</title> <meta http-equiv="Content-Type" content="text/html; charset=iso-8859-1" /> <meta name="keywords" content="EC 1.2.5.1,ExplorEnz,IUBMB,Enzyme Nomenclature Database,Enzyme Classification" /> <meta name="description" content="Enzyme Nomenclature Database" /> <meta name="robots" content="noindex,nofollow"> <meta name="googlebot" content="noindex,nofollow" /> <link rel="stylesheet" type="text/css" href="print.css"> <link rel="shortcut icon" href="favicon.ico" /> <style type="text/css" media="screen">  </style> </head> <base href="//query.php?ec=1.2.5.1&pr=on"> <body> <table border="0" cellpadding="2" cellspacing="3" width="100%"> <tr valign="bottom"> <td width="20%" align="right"><a name="1"></a>EC</td> <td width="80%" colspan="1">1.2.5.1     </td> </tr> <tr> <td width="20%" align="right">Accepted name:</td> <td width="80%" colspan="1">pyruvate dehydrogenase (quinone)</td> </tr> <tr> <td width="20%" align="right">Reaction:</td> <td width="80%" colspan="1">pyruvate + ubiquinone + H2O = acetate + CO2 + ubiquinol</td> </tr> <tr> <td width="20%" align="right">Other name(s):</td> <td width="80%" colspan="1">pyruvate dehydrogenase (ambiguous); pyruvic dehydrogenase (ambiguous); pyruvic (cytochrome b1) dehydrogenase (incorrect); pyruvate:ubiquinone-8-oxidoreductase; pyruvate oxidase (ambiguous); pyruvate dehydrogenase (cytochrome) (incorrect)</td> </tr> <tr valign="top"> <td width="20%" align="right">Systematic name: </td> <td width="80%" colspan="1">pyruvate:ubiquinone oxidoreductase</td> </tr> <tr valign="top"> <td width="20%" align="right">Comments:</td> <td width="80%" colspan="1">Flavoprotein (FAD) [1]. This bacterial enzyme is located on the inner surface of the cytoplasmic membrane and coupled to the respiratory chain via ubiquinone [2,3]. Does not accept menaquinone. Activity is greatly enhanced by lipids [4,5,6]. Requires thiamine diphosphate [7]. The enzyme can also form acetoin [8].</td> </tr> <tr> <td width="20%" align="right" valign="top">References:</td> <td align="left" valign="top" colspan="1"> <table border="0" cellpadding="0"><tr> <td>1. </td> <td>Recny, M.A. and Hager, L.P. Reconstitution of native Escherichia coli pyruvate oxidase from apoenzyme monomers and FAD. J. Biol. Chem. 257 (1982) 12878–12886. [PMID: 6752142] </td> </tr> </td></tr> <tr> <td>2. </td> <td>Cunningham, C.C. and Hager, L.P. Reactivation of the lipid-depleted pyruvate oxidase system from Escherichia coli with cell envelope neutral lipids. J. Biol. Chem. 250 (1975) 7139–7146. [PMID: 1100621] </td> </tr> </td></tr> <tr> <td>3. </td> <td>Koland, J.G., Miller, M.J. and Gennis, R.B. Reconstitution of the membrane-bound, ubiquinone-dependent pyruvate oxidase respiratory chain of Escherichia coli with the cytochrome d terminal oxidase. Biochemistry 23 (1984) 445–453. [PMID: 6367818] </td> </tr> </td></tr> <tr> <td>4. </td> <td>Grabau, C. and Cronan, J.E., Jr. In vivo function of Escherichia coli pyruvate oxidase specifically requires a functional lipid binding site. Biochemistry 25 (1986) 3748–3751. [PMID: 3527254] </td> </tr> </td></tr> <tr> <td>5. </td> <td>Wang, A.Y., Chang, Y.Y. and Cronan, J.E., Jr. Role of the tetrameric structure of Escherichia coli pyruvate oxidase in enzyme activation and lipid binding. J. Biol. Chem. 266 (1991) 10959–10966. [PMID: 2040613] </td> </tr> </td></tr> <tr> <td>6. </td> <td>Chang, Y.Y. and Cronan, J.E., Jr. Sulfhydryl chemistry detects three conformations of the lipid binding region of Escherichia coli pyruvate oxidase. Biochemistry 36 (1997) 11564–11573. [PMID: 9305946] </td> </tr> </td></tr> <tr> <td>7. </td> <td>O'Brien, T.A., Schrock, H.L., Russell, P., Blake, R., 2nd and Gennis, R.B. Preparation of Escherichia coli pyruvate oxidase utilizing a thiamine pyrophosphate affinity column. Biochim. Biophys. Acta 452 (1976) 13–29. [PMID: 791368] </td> </tr> </td></tr> <tr> <td>8. </td> <td>Bertagnolli, B.L. and Hager, L.P. Role of flavin in acetoin production by two bacterial pyruvate oxidases. Arch. Biochem. Biophys. 300 (1993) 364–371. [PMID: 8424670] </td> </tr> </td></tr> </table></td></tr> </td></tr> <tr><td colspan="2"><center>[EC 1.2.5.1 created 2010]</center></td> </tr> <tr> <td> </td> <td></td> </tr> <tr> <td> </td> <td></td> </tr> </table> </body> </html>

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ExplorEnz: EC 1.2.5.1