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Biochem J. 1988 Dec 1;256(2):357-61.

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

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  • 1F. Hoffmann-La Roche & Co., Ltd., Pharmaceutical Research Department, Basel, Switzerland.


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.

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