STRUCTURE OF ENZYME SUBSTRATE COMPLEX FOR GENERATION OF UDP N ACETYLMURAMIC ACID

$143,176P41FY2002RRNIH

Stanford University, Stanford CA

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Abstract

UDP-N-acetylenolpyruvylglucosamine reductase (MurB) is an enzyme in the peptidoglycan biosynthetic pathway of bacteria. It is responsible for the second committed step, namely the reduction of enolpyruvyl-UDP-N-acetylglucosamine (EP-UDPGlcNAc) to UDP-N-acetylmurammic acid (UDPMurNAc) by NADPH via a tightly bound flavin adenine dinucleotide cofactor. This resulting sugar is then the foundation for the addition of the five amino acids comprising the peptide chain and subsequently will be linked with N-acetylglucosamine to form the repeating disaccharide-pentapeptide subunit. Because of the essential nature of this enzyme in the synthesis of peptidoglycan to maintain osmotic integrity, this enzyme is a novel drug target for design of new antibacterial agents.

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