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Inhibition of pancreatic lipase in vitro by the covalent inhibitor tetrahydrolipstatin.


ABSTRACT: Tetrahydrolipstatin inhibits pancreatic lipase from several species, including man, with comparable potency. The lipase is progressively inactivated through the formation of a long-lived covalent intermediate, probably with a 1:1 stoichiometry. The lipase substrate triolein and also a boronic acid derivative, which is presumed to be a transition-state-form inhibitor, retard the rate of inactivation. Therefore, in all probability, tetrahydrolipstatin reacts with pancreatic lipase at, or near, the substrate binding or active site. Tetrahydrolipstatin is a selective inhibitor of lipase; other hydrolases tested were at least a thousand times less potently inhibited.

SUBMITTER: Hadvary P 

PROVIDER: S-EPMC1135417 | biostudies-other | 1988 Dec

REPOSITORIES: biostudies-other

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