Observation of an acryloyl-thiamin diphosphate adduct in the first step of clavulanic acid biosynthesis

M Merski, CA Townsend

Index: Merski, Matthew; Townsend, Craig A. Journal of the American Chemical Society, 2007 , vol. 129, # 51 p. 15750 - 15751

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Citation Number: 29

Abstract

The first committed biosynthetic step toward clavulanic acid, the clinically important β- lactamase inhibitor, is catalyzed by the thiamin diphosphate (ThDP)-dependent enzyme N 2- (2-carboxyethyl) arginine synthase (CEAS). This protein carries out a unique reaction among ThDP-dependent processes in which a CN bond is formed, and an electrophilic acryloyl-thiazolium intermediate of ThDP is proposed to be involved, unlike the ...