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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 1.1.3.15</title> <meta http-equiv="Content-Type" content="text/html; charset=iso-8859-1" /> <meta name="keywords" content="EC 1.1.3.15,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=1.1.3.15"> <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=1.1.3.15&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">1.1.3.15     </td> </tr> <tr> <td width="20%" align="right">Accepted name:</td> <td width="80%" colspan="1">(S)-2-hydroxy-acid oxidase</td> </tr> <tr> <td width="20%" align="right">Reaction:</td> <td width="80%" colspan="1">an (S)-2-hydroxy carboxylate + O2 = a 2-oxo carboxylate + H2O2</td> </tr> <tr> <td width="20%" align="right">Other name(s):</td> <td width="80%" colspan="1">hydroxy-acid oxidase A; hydroxy-acid oxidase B; glycolate oxidase; L-2-hydroxy acid oxidase; hydroxyacid oxidase A; L-α-hydroxy acid oxidase</td> </tr> <tr valign="top"> <td width="20%" align="right">Systematic name: </td> <td width="80%" colspan="1">(S)-2-hydroxy carboxylate:oxygen 2-oxidoreductase</td> </tr> <tr valign="top"> <td width="20%" align="right">Comments:</td> <td width="80%" colspan="1">A flavoprotein (FMN). Exists as two major isoenzymes; the A form preferentially oxidizes short-chain aliphatic hydroxy acids, and was previously listed as EC 1.1.3.1, glycolate oxidase; the B form preferentially oxidizes long-chain and aromatic hydroxy acids. The rat isoenzyme B also acts as <a href="query.php?ec=1.4.3.2" target="new">EC 1.4.3.2</a>, L-amino-acid oxidase.</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=1.1.3.15" target="new">BRENDA</a>, <a href="https://enzyme.expasy.org/EC/1.1.3.15" target="new">EXPASY</a>, <a href="https://www.ncbi.nlm.nih.gov/gene/?term=1.1.3.15%5BEC%5D" target="new">Gene</a>, <a href="https://www.kegg.jp/dbget-bin/www_bget?ec:1.1.3.15" target="new">KEGG</a>, <a href="http://biocyc.org/META/NEW-IMAGE?type=EC-NUMBER&object=EC-1.1.3.15" 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%221.1.3.15%22%5D%7D%7D%2C%22return_type%22%3A%22polymer_entity%22%7D" target="new">PDB</a>, CAS registry number: 9028-71-1</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>Blanchard, M., Green, D.E., Nocito-Carroll, V. and Ratner, S. l-Hydroxy acid oxidase. J. Biol. Chem. 163 (1946) 137–144. [PMID: <a href="https://pubmed.ncbi.nlm.nih.gov/21023634" target="new">21023634</a>] </td> </tr> </td></tr> <tr> <td>2. </td> <td>Frigerio, N.A. and Harbury, H.A. Preparation and some properties of crystalline glycolic acid oxidase of spinach. J. Biol. Chem. 231 (1958) 135–157. [PMID: <a href="https://pubmed.ncbi.nlm.nih.gov/13538955" target="new">13538955</a>] </td> </tr> </td></tr> <tr> <td>3. </td> <td>Kun, E., Dechary, J.M. and Pitot, H.C. The oxidation of glycolic acid by a liver enzyme. J. Biol. Chem. 210 (1954) 269–280. [PMID: <a href="https://pubmed.ncbi.nlm.nih.gov/13201588" target="new">13201588</a>] </td> </tr> </td></tr> <tr> <td>4. </td> <td>Nakano, M. and Danowski, T.S. Crystalline mammalian L-amino acid oxidase from rat kidney mitochondria. J. Biol. Chem. 241 (1966) 2075–2083. [PMID: <a href="https://pubmed.ncbi.nlm.nih.gov/5946631" target="new">5946631</a>] </td> </tr> </td></tr> <tr> <td>5. </td> <td>Nakano, M., Ushijima, Y., Saga, M., Tsutsumi, Y. and Asami, H. Aliphatic L-α-hydroxyacid oxidase from rat livers: purification and properties. Biochim. Biophys. Acta 167 (1968) 9–22. [<a href="https://doi.org/10.1016/0005-2744(68)90273-8" target="new">DOI</a>] [PMID: <a href="https://pubmed.ncbi.nlm.nih.gov/5686300" target="new">5686300</a>] </td> </tr> </td></tr> <tr> <td>6. </td> <td>Phillips, D.R., Duley, J.A., Fennell, D.J. and Holmes, R.S. The self-association of L-α hydroxyacid oxidase. Biochim. Biophys. Acta 427 (1976) 679–687. [<a href="https://doi.org/10.1016/0005-2795(76)90211-7" target="new">DOI</a>] [PMID: <a href="https://pubmed.ncbi.nlm.nih.gov/1268224" target="new">1268224</a>] </td> </tr> </td></tr> <tr> <td>7. </td> <td>Schuman, M. and Massey, V. Purification and characterization of glycolic acid oxidase from pig liver. Biochim. Biophys. Acta 227 (1971) 500–520. [<a href="https://doi.org/10.1016/0005-2744(71)90003-9" target="new">DOI</a>] [PMID: <a href="https://pubmed.ncbi.nlm.nih.gov/5569122" target="new">5569122</a>] </td> </tr> </td></tr> <tr> <td>8. </td> <td>Jones, J.M., Morrell, J.C. and Gould, S.J. Identification and characterization of HAOX1, HAOX2, and HAOX3, three human peroxisomal 2-hydroxy acid oxidases. J. Biol. Chem. 275 (2000) 12590–12597. [<a href="https://doi.org/10.1074/jbc.275.17.12590" target="new">DOI</a>] [PMID: <a href="https://pubmed.ncbi.nlm.nih.gov/10777549" target="new">10777549</a>] </td> </tr> </td></tr> </table></td></tr> </td></tr> <tr><td colspan="2"><center>[EC 1.1.3.15 created 1972 (EC 1.1.3.1 created 1961, incorporated 1984)]</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>