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Identification of the THL binding site on human pancreatic lipase
Peng, Q. Hadvary, P. Maerki, H. P.
Peng, Q.
Hadvary, P.
Maerki, H. P.
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Issue Date
1991
Submitted date
2024-03-20
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Abstract
Pancreatic lipase is considered as a serine hydrolase that plays a key function in dietary fat absorption by hydrolysing triglycerides into diglycerides and subsequently into monoglycerides and free fatty acids. Although it has been assumed [1,2] that porcine pancreatic lipase has two functionally important sites: a catalytic site involving Serj109, and a topographically distinct interfacial "recognition site" or " substrate binding site" controlled by Serı52, the catalytic mechanism has not been demonstrated experimentally thus far. On the other hand, the X-ray structure of human pancreatic lipase [3] shows clearly that Serj52 forms a triad with His263 and Asp 176 which givesa spatial superposition with the catalytic triad of the serine protease trypsin (Fig.1). \ 1102 esp Recently Tetrahyrolipstatin exe (THL), a_ selective and irreversible inhibitor of er pancreatic lipase has been used to identify the THL binding site on porcine pancreatic lipase. The result showed that THL binds to Serı52 of the lipase covalently [4]. The same attempt was also made for human pancreatic lipase, the data indicate strongly that ee human and porcine pancreatic see lipases share high : similarity/identity not only in their primary structure and enzymatic characteristics, but also in their catalytic mechanism.
Citation
Lipases : structure, mechanism and genetic engineering, 141 - 144
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Book chapter
conference paper
conference paper
Language
en
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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