Pancreatic Lipase-Related Protein Type 1: A Double Mutation Restores a Significant Lipase Activity

Besides the active pancreatic lipase (PL) which plays a major role in dietary fat digestion, the presence of a pancreatic lipase related protein 1 (PLRP1) displaying a very low lipolytic activity has been reported in vertebrates. It has been suggested that the reduced lipolytic activity of PLRP1 res...

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Bibliographic Details
Published in:Biochemical and biophysical research communications 1998-05, Vol.246 (2), p.513-517
Main Authors: Crenon, Isabelle, Jayne, Sandrine, Kerfelec, Brigitte, Hermoso, Juan, Pignol, David, Chapus, Catherine
Format: Article
Language:English
Subjects:
Animals
Base Sequence
Binding Sites - genetics
DNA Primers - genetics
Dogs
Horses
In Vitro Techniques
Kinetics
Lipase - chemistry
Lipase - genetics
Lipase - metabolism
Lipolysis - genetics
Models, Molecular
Mutagenesis, Site-Directed
Pancreas - enzymology
pancreatic lipase/related lipase/colipase
Point Mutation
Protein Conformation
Recombinant Proteins - chemistry
Recombinant Proteins - genetics
Recombinant Proteins - metabolism
Swine
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Summary:Besides the active pancreatic lipase (PL) which plays a major role in dietary fat digestion, the presence of a pancreatic lipase related protein 1 (PLRP1) displaying a very low lipolytic activity has been reported in vertebrates. It has been suggested that the reduced lipolytic activity of PLRP1 results from specific features of the N-terminal domain of the protein. Therefore, based on sequence comparison between PL and PLRP1 and modelling experiments, several residues located in the vicinity of the active site pocket of both enzymes have been mutated. In this paper, we report that, as regards to PL, two substitutions in positions 179 and 181 in PLRP1 account for the very low lipolytic activity of the protein. Indeed, substituting these residues (V179and A181) in PLRP1 for those found in PL (A179and P181), restores a significant lipolytic activity for PLRP1.
ISSN:0006-291X
1090-2104
DOI:10.1006/bbrc.1998.8651