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THE STRUCTURE OF HUMAN PANCREATIC LIPASE SUGGESTS A LOCALLY INVERTED, TRYPSIN-LIKE MECHANISM
Gubernator, Klaus Müller, Klaus Winkler, Fritz K.
Gubernator, Klaus
Müller, Klaus
Winkler, Fritz K.
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Issue Date
1991
Submitted date
2024-03-06
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Abstract
Furthercrystallographic refinement of the structure of human pancreatic lipase hasled to an improved model which has been used for modelling studies of the hydrolysis of triglyceride substrates. In addition to the removalof the flap, further changesin the protein structure around the active site appear necessary to formulate a stereochemically plausible mechanism. A locally inverted trypsin-like mechanism is presently favoured and demands relatively modest changes of the X-ray structure. Additional new findings include the interpretation of the difference density for a butylboronic acid derivative and the location of a Ca2+ bindingsite.
Citation
Lipases : structure, mechanism and genetic engineering, 9 - 16
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Book chapter
conference paper
conference paper
Language
en
Description
Series/Report no.
GBF monographs ; Volume 16
ISSN
0930-4320
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ISBN
156081165X
3527283323
3527283323
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Attribution-NonCommercial-ShareAlike 4.0 International