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- Title
N-terminal acetyl group is essential for the inhibitory function of carboxypeptidase Y inhibitor (I<sup>C</sup>)
- Authors
Mima, Joji; Kondo, Takahiro; Hayashi, Rikimaru
- Abstract
Carboxypeptidase Y (CPY) inhibitor, IC, a yeast cytoplasmic inhibitor in which the N-terminal amino acid is acetylated, was expressed in Escherichia coli and produced as an unacetylated form of IC (unaIC). Circular dichroism and fluorescence measurements showed that unaIC and IC were structurally identical and produce identical complexes with CPY. However, the Ki values for unaIC for anilidase and peptidase activity of CPY were much larger, by 700- and 60-fold, respectively, than those of IC. The reactivities of phenylmethylsulfonyl fluoride and p-chloromercuribenzoic acid toward the CPY–unaIC complex were considerably higher than those toward the CPY–IC complex. Thus, the N-terminal acetyl group of IC is essential for achieving a tight interaction with CPY and for its complete inactivation.
- Subjects
CARBOXYPEPTIDASES; ESCHERICHIA coli
- Publication
FEBS Letters, 2002, Vol 532, Issue 1/2, p207
- ISSN
0014-5793
- Publication type
Article
- DOI
10.1016/S0014-5793(02)03676-1