Article (Scientific journals)
Exploring The Active Site Cavity Of Human Pancreatic Lipase
Colin, Damien Yann; Deprez-Beauclair, Paule; Allouche, Maya et al.
2008In Biochemical and Biophysical Research Communications, 370 (3), p. 394-398
Peer reviewed
 

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Abstract :
[en] 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.
Disciplines :
Biochemistry, biophysics & molecular biology
Author, co-author :
Colin, Damien Yann
Deprez-Beauclair, Paule
Allouche, Maya
Brasseur, Robert ;  Université de Liège - ULiège > Gembloux Agro-Bio Tech
Kerfelec, Brigitte
Language :
English
Title :
Exploring The Active Site Cavity Of Human Pancreatic Lipase
Publication date :
2008
Journal title :
Biochemical and Biophysical Research Communications
ISSN :
0006-291X
eISSN :
1090-2104
Publisher :
Elsevier, Atlanta, United States - California
Volume :
370
Issue :
3
Pages :
394-398
394-8
Peer reviewed :
Peer reviewed
Available on ORBi :
since 23 June 2010

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