Accueil > Publications > Recherche par années > Années 1990 > 1998

Carriere, F ; Withers-Martinez, C ; van Tilberugh, H ; Roussel, A ; Cambillau, C ; Verger, R

Structural basis for the substrate selectivity of pancreatic lipases and some related proteins

Biochimica et Biophysica Acta-Reviews On Biomembranes 1376 (3) 417-432

par Administrateur - publié le

Abstract :

The classical human pancreatic lipase (HPL), the guinea pig pancreatic lipase-related protein 2 (GPLRP2) and the phospholipase A1 from hornet venom (DolmI PLA1) illustrate three interesting steps in the molecular evolution of the pancreatic lipase gene family towards different substrate selectivities. Based on the known 3D structures of HPL and a GPLRP2 chimera, as well as the modeling of DolmI PLA1, we review here the structural features and the kinetic properties of these three enzymes for a better understanding of their structure-function relationships. HPL displays significant activity only on triglycerides, whereas GPLRP2 displays high phospholipase and galactolipase activities, together with a comparable lipase activity. GPLRP2 shows high structural homology with HPL with the exception of the lid domain which is made of five amino acid residues (mini-lid) instead of 23 in HPL.