A pancreatic lipase with a phospholipase A1 activity: crystal structure of a chimeric pancreatic lipase-related protein 2 from guinea pig.
Withers-Martinez, C., Carriere, F., Verger, R., Bourgeois, D., Cambillau, C.(1996) Structure 4: 1363-1374
- PubMed: 8939760 
- DOI: https://doi.org/10.1016/s0969-2126(96)00143-8
- Primary Citation of Related Structures:  
1GPL - PubMed Abstract: 
The guinea pig pancreatic lipase-related protein 2 (GPLRP2) differs from classical pancreatic lipases in that it displays both lipase and phospholipase A1 activities; classical pancreatic lipases have no phospholipase activity. The sequence of GPLRP2 is 63 % identical to that of human pancreatic lipase (HPL), but the so-called lid domain, is much reduced in GPLRP2. A phospholipase A1 from hornet venom (Dolml PLA1) is very similar to HPL and GPLRP2 but is devoid of lipase activity; Dolml PLA1 also contains a reduced lid domain and lacks a region termed the beta9 loop, which is located in the vicinity of the HPL and GPLRP2 active sites. The structure determination of a chimera of GPLRP2 and HPL and domain building of Dolml PLA1 were undertaken to gain a better understanding of the structural parameters responsible for the differences in lipase versus phospholipase activity among these structurally related enzymes.
Organizational Affiliation: 
Architecture et Fonction des Macromolécules Biologiques, CNRS-IFR1 UPR9039, 31 chemin Joseph Aiguier, 13402 Marseille cedex 20, France. cambilau@afmb.cnrs-mrs.fr