大肠杆菌酮泛解酸羟甲基转移酶晶体结构的比较分析证实，它是（βα）8磷酸烯醇式丙酮酸/丙酮酸超家族的成员。
Comparative analysis of the Escherichia coli ketopantoate hydroxymethyltransferase crystal structure confirms that it is a member of the (betaalpha)8 phosphoenolpyruvate/pyruvate superfamily.
作者信息
Schmitzberger Florian, Smith Alison G, Abell Chris, Blundell Tom L
机构信息
Department of Biochemistry, University of Cambridge, Cambridge CB2 1GA, United Kingdom.
出版信息
J Bacteriol. 2003 Jul;185(14):4163-71. doi: 10.1128/JB.185.14.4163-4171.2003.
Escherichia coli ketopantoate hydroxymethyltransferase (KPHMT) catalyzes the first step in the biosynthesis pathway of pantothenate (vitamin B(5)), the transfer of a hydroxymethyl group onto alpha-ketoisovalerate. Here we describe a detailed comparative analysis of the KPHMT crystal structure and the identification of structural homologues, some of which have remarkable similarities in their active sites, modes of binding to substrates, and mechanisms. We show that KPHMT forms a family within the phosphoenolpyruvate/pyruvate superfamily. Based on the analysis, we propose that in this superfamily there should be a subdivision into two groups. This paper completes our structural analysis of the E. coli enzymes in the pantothenate pathway.
大肠杆菌酮泛解酸羟甲基转移酶（KPHMT）催化泛酸（维生素B5）生物合成途径的第一步，即将羟甲基转移到α-酮异戊酸上。在此，我们描述了KPHMT晶体结构的详细比较分析以及结构同源物的鉴定，其中一些在活性位点、与底物的结合模式和机制方面具有显著相似性。我们表明，KPHMT在磷酸烯醇丙酮酸/丙酮酸超家族中形成一个家族。基于该分析，我们提出在这个超家族中应细分为两组。本文完成了我们对泛酸途径中大肠杆菌酶的结构分析。
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