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<!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="index,nofollow"> <meta name="googlebot" content="index,nofollow" /> <link rel="stylesheet" type="text/css" href="enzyme2.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"> <body> <a href="index.php"> <img src="images/banner_5.gif" alt="The Enzyme Database" width="920 px" height="" border="0" /></a> </div><table border="0" cellborder="0" cellspacing="0" cellpadding="0" width="100%" id="nav"> <tr> <td class="f" nowrap="nowrap" colspan="1" border="0"> <li><a href="./" alt="Home" title="Home">Home</a></li> <li><a href="search.php" alt="Simple Search" title="Search the database">Search</a></li> <li><a href="class.php" alt="Enzyme Classes" title="Hierarchical view of the Enzyme Classification system">Enzymes by Class</a></li> <li><a href="newenz.php" alt="New/Modified Enzymes" title="New/modified enzyme entries">New/Amended Enzymes</a></li> <li><a href="stats.php" alt="Enzyme Count" title="Enzyme count">Statistics</a></li> <li><a href="forms.php" alt="Forms" title="Submit data on a new enzyme, or report an error">Forms</a></li> <li><a href="news.php" alt="News" title="Reports on recent developments in enzyme classification or changes to nomenclature">News</a></li> <li><a href="about.php" alt="Help Files, Archives" title="Quick-start Guide, FAQ, Supplements">Information</a></li> <li><a href="downloads.php" alt="Downloads" title="Download the database">Downloads</a></li> <li></li> </td> </tr> </table> Your query returned 1 entry.    <a href="query.php?ec=1.2.5.1&pr=on" target="new"><img src="images/print.png" alt="printer_icon" align="center" border="0"></a>Printable version <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">Links to other databases:</td> <td width="80%" colspan="1"><a href="https://www.brenda-enzymes.org/enzyme.php?ecno=1.2.5.1" target="new">BRENDA</a>, <a href="https://enzyme.expasy.org/EC/1.2.5.1" target="new">EXPASY</a>, <a href="https://www.ncbi.nlm.nih.gov/gene/?term=1.2.5.1%5BEC%5D" target="new">Gene</a>, <a href="https://www.kegg.jp/dbget-bin/www_bget?ec:1.2.5.1" target="new">KEGG</a>, <a href="http://biocyc.org/META/NEW-IMAGE?type=EC-NUMBER&object=EC-1.2.5.1" target="new">MetaCyc</a>, <a href="https://www.rcsb.org/search?request=%7B%22query%22%3A%7B%22type%22%3A%22terminal%22%2C%22service%22%3A%22text%22%2C%22parameters%22%3A%7B%22attribute%22%3A%22rcsb_polymer_entity.rcsb_ec_lineage.id%22%2C%22operator%22%3A%22in%22%2C%22value%22%3A%5B%221.2.5.1%22%5D%7D%7D%2C%22return_type%22%3A%22polymer_entity%22%7D" target="new">PDB</a></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: <a href="https://pubmed.ncbi.nlm.nih.gov/6752142" target="new">6752142</a>] </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: <a href="https://pubmed.ncbi.nlm.nih.gov/1100621" target="new">1100621</a>] </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: <a href="https://pubmed.ncbi.nlm.nih.gov/6367818" target="new">6367818</a>] </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: <a href="https://pubmed.ncbi.nlm.nih.gov/3527254" target="new">3527254</a>] </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: <a href="https://pubmed.ncbi.nlm.nih.gov/2040613" target="new">2040613</a>] </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. [<a href="https://doi.org/10.1021/bi9709102" target="new">DOI</a>] [PMID: <a href="https://pubmed.ncbi.nlm.nih.gov/9305946" target="new">9305946</a>] </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. [<a href="https://doi.org/10.1016/0005-2744(76)90054-1" target="new">DOI</a>] [PMID: <a href="https://pubmed.ncbi.nlm.nih.gov/791368" target="new">791368</a>] </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. [<a href="https://doi.org/10.1006/abbi.1993.1049" target="new">DOI</a>] [PMID: <a href="https://pubmed.ncbi.nlm.nih.gov/8424670" target="new">8424670</a>] </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> <center>Data © 2001–2024 IUBMB Web site © 2005–2024 Andrew McDonald </center> </body> </html>