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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 1.2.4.4</title> <meta http-equiv="Content-Type" content="text/html; charset=iso-8859-1" /> <meta name="keywords" content="EC 1.2.4.4,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=1.2.4.4"> <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=1.2.4.4&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">1.2.4.4     </td> </tr> <tr> <td width="20%" align="right">Accepted name:</td> <td width="80%" colspan="1">3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring)</td> </tr> <tr> <td width="20%" align="right">Reaction:</td> <td width="80%" colspan="1">3-methyl-2-oxobutanoate + [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] lipoyllysine = [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylpropanoyl)dihydrolipoyllysine + CO2</td> </tr> <tr> <td width="20%" align="right"></td> <td width="80%">For diagram of oxo-acid-dehydrogenase complexes, <a target="new" href="reaction/misc/oxoacid.html">click here</a></td> </tr> <tr> <td width="20%" align="right">Glossary:</td> <td width="80%" colspan="1"><a target="new" href="glossary/lipoyl.html">dihydrolipoyl group</a> <a target="new" href="glossary/TPP.html">thiamine diphosphate</a> = 3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-5-(2-diphosphoethyl)-4-methyl-1,3-thiazolium</td> </tr> <tr> <td width="20%" align="right">Other name(s):</td> <td width="80%" colspan="1">2-oxoisocaproate dehydrogenase; 2-oxoisovalerate (lipoate) dehydrogenase; 3-methyl-2-oxobutanoate dehydrogenase (lipoamide); 3-methyl-2-oxobutanoate:lipoamide oxidoreductase (decarboxylating and acceptor-2-methylpropanoylating); α-keto-α-methylvalerate dehydrogenase; α-ketoisocaproate dehydrogenase; α-ketoisocaproic dehydrogenase; α-ketoisocaproic-α-keto-α-methylvaleric dehydrogenase; α-ketoisovalerate dehydrogenase; α-oxoisocaproate dehydrogenase; BCKDH (ambiguous); BCOAD; branched chain keto acid dehydrogenase; branched-chain (-2-oxoacid) dehydrogenase (BCD); branched-chain 2-keto acid dehydrogenase; branched-chain 2-oxo acid dehydrogenase; branched-chain α-keto acid dehydrogenase; branched-chain α-oxo acid dehydrogenase; branched-chain keto acid dehydrogenase; branched-chain ketoacid dehydrogenase; dehydrogenase, 2-oxoisovalerate (lipoate); dehydrogenase, branched chain α-keto acid</td> </tr> <tr valign="top"> <td width="20%" align="right">Systematic name: </td> <td width="80%" colspan="1">3-methyl-2-oxobutanoate:[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase]-lipoyllysine 2-oxidoreductase (decarboxylating, acceptor-2-methylpropanoylating)</td> </tr> <tr valign="top"> <td width="20%" align="right">Comments:</td> <td width="80%" colspan="1">Contains thiamine diphosphate. It acts not only on 3-methyl-2-oxobutanaoate, but also on 4-methyl-2-oxopentanoate and (S)-3-methyl-2-oxopentanoate, so that it acts on the 2-oxo acids that derive from the action of transaminases on valine, leucine and isoleucine. It is a component of the multienzyme 3-methyl-2-oxobutanoate dehydrogenase complex in which multiple copies of it are bound to a core of molecules of <a href="query.php?ec=2.3.1.168" target="new">EC 2.3.1.168</a>, dihydrolipoyllysine-residue (2-methylpropanoyl)transferase, which also binds multiple copies of <a href="query.php?ec=1.8.1.4" target="new">EC 1.8.1.4</a>, dihydrolipoyl dehydrogenase. It does not act on free lipoamide or lipoyllysine, but only on the lipoyllysine residue in <a href="query.php?ec=2.3.1.168" target="new">EC 2.3.1.168</a>.</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=1.2.4.4" target="new">BRENDA</a>, <a href="https://enzyme.expasy.org/EC/1.2.4.4" target="new">EXPASY</a>, <a href="https://www.ncbi.nlm.nih.gov/gene/?term=1.2.4.4%5BEC%5D" target="new">Gene</a>, <a href="https://www.kegg.jp/dbget-bin/www_bget?ec:1.2.4.4" target="new">KEGG</a>, <a href="http://biocyc.org/META/NEW-IMAGE?type=EC-NUMBER&object=EC-1.2.4.4" 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%221.2.4.4%22%5D%7D%7D%2C%22return_type%22%3A%22polymer_entity%22%7D" target="new">PDB</a>, CAS registry number: 9082-72-8</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>Bowden, J.A. and Connelly, J.L. Branched chain α-keto acid metabolism. II. Evidence for the common identity of α-ketoisocaproic acid and α-keto-β-methyl-valeric acid dehydrogenases. J. Biol. Chem. 243 (1968) 3526–3531. [PMID: <a href="https://pubmed.ncbi.nlm.nih.gov/5656388" target="new">5656388</a>] </td> </tr> </td></tr> <tr> <td>2. </td> <td>Connelly, J.L., Danner, D.J. and Bowden, J.A. Branched chain α-keto acid metabolism. I. Isolation, purification, and partial characterization of bovine liver α-ketoisocaproic:α-keto-β-methylvaleric acid dehydrogenase. J. Biol. Chem. 243 (1968) 1198–1203. [PMID: <a href="https://pubmed.ncbi.nlm.nih.gov/5689906" target="new">5689906</a>] </td> </tr> </td></tr> <tr> <td>3. </td> <td>Danner, D.J., Lemmon, S.K., Beharse, J.C. and Elsas, L.J., II Purification and characterization of branched chain α-ketoacid dehydrogenase from bovine liver mitochondria. J. Biol. Chem. 254 (1979) 5522–5526. [PMID: <a href="https://pubmed.ncbi.nlm.nih.gov/447664" target="new">447664</a>] </td> </tr> </td></tr> <tr> <td>4. </td> <td>Pettit, F.H., Yeaman, S.J. and Reed, L.J. Purification and characterization of branched chain α-keto acid dehydrogenase complex of bovine kidney. Proc. Natl. Acad. Sci. USA 75 (1978) 4881–4885. [<a href="https://doi.org/10.1073/pnas.75.10.4881" target="new">DOI</a>] [PMID: <a href="https://pubmed.ncbi.nlm.nih.gov/283398" target="new">283398</a>] </td> </tr> </td></tr> <tr> <td>5. </td> <td>Perham, R.N. Swinging arms and swinging domains in multifunctional enzymes: catalytic machines for multistep reactions. Annu. Rev. Biochem. 69 (2000) 961–1004. [<a href="https://doi.org/10.1146/annurev.biochem.69.1.961" target="new">DOI</a>] [PMID: <a href="https://pubmed.ncbi.nlm.nih.gov/10966480" target="new">10966480</a>] </td> </tr> </td></tr> </table></td></tr> </td></tr> <tr><td colspan="2"><center>[EC 1.2.4.4 created 1972 (EC 1.2.4.3 created 1972, incorporated 1978), modified 2003]</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>