Accueil > Publications > Recherche par années > Années 1990 > 1999

Canaan, S ; Roussel, L ; Verger, R ; Cambillau, C

Gastric lipase : crystal structure and activity

Biochimica et Biophysica Acta-Molecular and Cell Biology of Lipids 1441 (2-3) 197-204

par Administrateur - publié le

Abstract :

Fat digestion in humans requires not only the classical pancreatic lipase but also gastric lipase, which is stable and active despite the highly acidic stomach environment. We have solved the structure of recombinant human gastric lipase at 3.0 Angstrom resolution, the first structure to be described within the mammalian acid lipase family. This globular enzyme (379 residues) consists of a core domain, belonging to the a/ß hydrolase fold family, and an extrusion domain. It possesses a classical catalytic triad (Ser 153, His 353, Asp 324) and an oxyanion hole (NH groups of Gln 154 and Leu 67). Four N-glycosylation sites were identified on the electron density maps.