Title : Gastric lipase: crystal structure and activity - Canaan_1999_Biochim.Biophys.Acta_1441_197
Author(s) : Canaan S , Roussel A , Verger R , Cambillau C
Ref : Biochimica & Biophysica Acta , 1441 :197 , 1999
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 A 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 alpha/beta 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. The catalytic serine is deeply buried under the extrusion domain, which is composed of a 'cap' domain and a segment consisting of 30 residues, which can be defined as a lid. Its displacement is necessary for the substrates to access the active site. A phosphonate inhibitor was positioned in the active site which clearly suggests the location of the hydrophobic substrate binding site.

PubMedSearch : Canaan_1999_Biochim.Biophys.Acta_1441_197
PubMedID: 10570247
Gene_locus related to this paper: human-LIPF

Related information

Gene_locus human-LIPF
Family human-LIPF    Acidic_Lipase
Structure human-LIPF    Acidic_Lipase    1HLG

Citations formats

Canaan S, Roussel A, Verger R, Cambillau C (1999)
Gastric lipase: crystal structure and activity
Biochimica & Biophysica Acta 1441 :197

Canaan S, Roussel A, Verger R, Cambillau C (1999)
Biochimica & Biophysica Acta 1441 :197