Zinc regulation of aminopeptidase B involved in neuropeptide production
Abstract
Aminopeptidase B (AP-B) is a metallopeptidase that removes basic residues from the N-termini of neuropeptide substrates in secretory vesicles. This study assessed zinc regulation of AP-B activity, since secretory vesicles contain endogenous zinc. AP-B was inhibited by zinc at concentrations typically present in secretory vesicles. Zinc effects were dependent on concentration, incubation time, and the molar ratio of zinc to enzyme. AP-B activity was recovered upon removal of zinc. AP-B with zinc became susceptible to degradation by trypsin, suggesting that zinc alters enzyme conformation. Zinc regulation demonstrates the metallopeptidase property of AP-B.
Abbreviations: AP-B, aminopeptidase B, ME, (Met)enkephalin
Keywords: Arg/Lys aminopeptidase, Zinc regulation, Inhibition, Neuropeptide, Secretory vesicle
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PII: S0014-5793(08)00507-3
doi:10.1016/j.febslet.2008.06.017
© 2008 Federation of European Biochemical Societies
