Abstract
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.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
More From: Biochemical and Biophysical Research Communications
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.