The crystal structure of a triacylglycerol lipase from Pseudomonas cepacia reveals a highly open conformation in the absence of a bound inhibitor.

摘要: Abstract Background: Lipases, a family of enzymes which catalyze the hydrolysis triglycerides, are widely distributed in many organisms. True lipases distinguished from esterases by characteristic interfacial activation they exhibit at an oil–water interface. Lipases one most frequently used biocatalysts for organic reactions performed under mild conditions. Their biotechnological applications include food and oil processing preparation chiral intermediates synthesis enantiomerically pure pharmaceuticals. Recent structural studies on several have provided some clues towards understanding mechanisms hydrolytic activity, activation, stereoselectivity. This study was undertaken order to provide information bacterial lipases, is relatively limited comparison that other sources. Results: We determined crystal structure triacylglycerol lipase Pseudomonas cepacia (PcL) absence bound inhibitor using X-ray crystallography. The shows contain α / β -hydrolase fold catalytic triad comprising residues Ser87, His286 Asp264. enzyme shares features with homologous glumae (PgL) Chromobacterium viscosum (CvL), including calcium-binding site. present PcL reveals highly open conformation solvent-accessible active contrast structures PgL site buried closed or partially opened ‘lid', respectively. Conclusions: exhibits found lipases. presence Ser-His-Asp triad, oxyanion hole, opening helical lid suggest this same catalysis as observed likely reflect activated form suggests involves reorganization secondary large movement expose similar mechanism described well characterized fungal mammalian