THE CRYSTAL-STRUCTURE OF TRIACYLGLYCEROL LIPASE FROM PSEUDOMONAS-GLUMAE REVEALS A PARTIALLY REDUNDANT CATALYTIC ASPARTATE

The family of lipases (triacylglycerol-acyl-hydrolases, EC 3.1.1.3) co nstitutes an interesting class of enzymes because of their ability to interact with lipid-water interfaces, their wide range of substrate sp ecificities, and their potential industrial applications [1,2]. Here w e report the first crystal structure of a bacterial lipase, from Pseud omonas glumae. The structure is formed from three domains, the largest of which contains a subset of the alpha/beta hydrolase fold and a cal cium site. Asp263, the acidic residue in the catalytic triad, has prev iously been mutated into an alanine with only a modest reduction in ac tivity [3].