PMID: 7085655Jul 25, 1982Paper

Inhibition of leucine aminopeptidase by amino acid hydroxamates.

The Journal of Biological Chemistry
W W ChanK Brand

Abstract

Amino acid hydroxamates are strong competitive inhibitors of leucine aminopeptidase from porcine kidney. The side chain specificity for inhibition correlates well with substrate specificity. L-Leucine hydroxamate (Ki = 14 microM) protects the enzyme from inactivation by EDTA and is presumed to be a bidentate ligand of the zinc at the active site. A substituted beta-mercaptoketone which may bind in a similar way is also a potent inhibitor (Ki = approximately 1 microM). The binding of these inhibitors suggests a mechanism for this enzyme in which a zinc-bound hydroxide ion participates in concerted proton-transfer processes, while the coordination and charge field at the zinc atom remain unchanged.

Related Concepts

Amino Acids
Metazoa
Hydroxamic Acids
Kidney
Kinetics
Methoxyleucine Aminopeptidase
Microsomes
Structure-Activity Relationship
Warthogs

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