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Zinc regulation of aminopeptidase B involved in neuropeptide production
Author(s) -
Hwang Shin-Rong,
Hook Vivian
Publication year - 2008
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2008.06.017
Subject(s) - zinc , aminopeptidase , enzyme , biochemistry , chemistry , vesicle , trypsin , neuropeptide , incubation , biology , amino acid , leucine , receptor , membrane , organic chemistry
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.