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The behaviour of leucine aminopeptidase towards thionopeptides
R E Beattie1, D T Elmore, C H Williams
1Department of Biochemistry, Queen's University, Belfast, Northern Ireland, U.K.
The Biochemical Journal
|July 1, 1987
Abstract:
Thionoleucine S-anilide (Leut-anilide), Leut-Gly-OEt and Leut-Phe-OMe were synthesized and shown to be competitive inhibitors of leucine aminopeptidase from pig kidney. The kinetics of inhibition were determined in the presence of leucine 4-methylcoumarin-7-amide as substrate. Although the compounds showed only moderate inhibitory potency, it was found that all were resistant to hydrolysis by the enzyme, in contrast with the reported behaviour of some thionopeptide analogues of substrates for other Zn2+-peptidases such as carboxypeptidase A and angiotensin-converting enzyme.