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Human Lipoprotein Lipase: Important Roles Of A Specific N-Linked Glycosylation Site And Specific Serines In Secretion And Enzyme Activity
Chan, Lawrence Faustinella, Fabrizia Semenkovich, Clay F. Smith, Louis C.
Chan, Lawrence
Faustinella, Fabrizia
Semenkovich, Clay F.
Smith, Louis C.
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Issue Date
1991
Submitted date
2024-03-27
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Abstract
Thestructure-function relationship of human lipoprotein lipase was studied by expressionof the cloned cDNAin transfected cells, using the wildtype construct and site-specific mutant constructs. Asparagine 43, of one ofthe two potential N-linked glycosylationsites in lipoprotein lipase, was found to be important for both enzymeactivity and secretion. Mutations involving someoftheserine residues also produced marked changes in enzymeactivity. The possible structural changes associated with these functionally altered mutantlipoprotein lipase molecules are discussed with reference to the crystal structure of human pancreatic lipase, a lipolytic enzyme with considerable sequence homology to lipoprotein lipase.
Citation
Lipases : structure, mechanism and genetic engineering, 303 - 308
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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