Exploring the active site cavity of human pancreatic lipase.
Biochem Biophys Res Commun
; 370(3): 394-8, 2008 Jun 06.
Article
in En
| MEDLINE
| ID: mdl-18353248
ABSTRACT
Within the scope of improving the efficiency of pancreatic enzyme replacement therapy in cystic fibrosis, the feasibility of shifting the pH-activity profile of pancreatic lipase toward acidic values was investigated by site specific mutagenesis in different regions of the catalytic cavity. We have shown that introducing a negative charge close to the catalytic histidine induced a shift of the pH optimum toward acidic values but strongly reduced the lipase activity. On the other hand, a negative charge in the entrance of the catalytic cleft gives rise to a lipase with improved properties and twice more active than the native enzyme at acidic pH.
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Lipase
Limits:
Humans
Language:
En
Journal:
Biochem Biophys Res Commun
Year:
2008
Document type:
Article
Affiliation country:
France