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Comparative Analysis of the Escherichia coli Ketopantoate Hydroxymethyltransferase Crystal Structure Confirms that It Is a Member of the (ß)₈ Phosphoenolpyruvate/Pyruvate Superfamily

Department of Biochemistry, University of Cambridge, Cambridge CB2 1GA,¹ Department of Plant Sciences, Cambridge CB2 3EA,² University Chemical Laboratory, Cambridge CB2 1EW, United Kingdom³

Received 3 February 2003/ Accepted 18 April 2003

Escherichia coli ketopantoate hydroxymethyltransferase (KPHMT) catalyzes the first step in the biosynthesis pathway of pantothenate (vitamin B₅), the transfer of a hydroxymethyl group onto -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.