Active site geometry of porcine pancreatic lipase: an interesting switchover from Jones' to Seebach's model.
Porcine pancreatic lipase (PPL)-catalyzed hydrolysis of cis 3-acetoxyethyl-1,4-diphenyl and cis 3-acetoxyethyl-1-phenyl-4-(2-furyl) beta-lactams 1a and 1b proceeded with opposite stereoselectivity while the corresponding thienyl beta-lactam 1c showed no selectivity at all. An explanation based upon the dominance of hydrophobic and polar pockets in governing the stereoselectivity has been proposed.
Basak
A
A
Department of Chemistry, Indian Institute of Technology, Kharagpur, India. absk@chem.iitkgp.ernet.in
Rudra
K R
KR
Bdour
H M
HM
Dasgupta
J
J
D000818:Animals; D020134:Catalytic Domain; D007769:Lactams / Q000378:metabolism; D008049:Lipase / Q000737:chemistry* / Q000378:metabolism; D008958:Models, Molecular; D010179:Pancreas / Q000201:enzymology; D011485:Protein Binding; D055672:Static Electricity; D013237:Stereoisomerism; D013329:Structure-Activity Relationship; D013379:Substrate Specificity; D013552:Swine
D007769:Lactams; D008049:Lipase