N‐terminal acetyl group is essential for the inhibitory function of carboxypeptidase Y inhibitor (I C )
In: FEBS Letters, Jg. 532 (2002), Heft 1-2, S. 207-210
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Zugriff:
Carboxypeptidase Y (CPY) inhibitor, I C , 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 I C (unaI C ). Circular dichroism and fluorescence measurements showed that unaI C and I C were structurally identical and produce identical complexes with CPY. However, the K i values for unaI C for anilidase and peptidase activity of CPY were much larger, by 700‐ and 60‐fold, respectively, than those of I C . The reactivities of phenylmethylsulfonyl fluoride and p ‐chloromercuribenzoic acid toward the CPY–unaI C complex were considerably higher than those toward the CPY–I C complex. Thus, the N‐terminal acetyl group of I C is essential for achieving a tight interaction with CPY and for its complete inactivation.
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N‐terminal acetyl group is essential for the inhibitory function of carboxypeptidase Y inhibitor (I C )
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Autor/in / Beteiligte Person: | Mima, Joji ; Kondo, Takahiro ; Hayashi, Rikimaru |
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Zeitschrift: | FEBS Letters, Jg. 532 (2002), Heft 1-2, S. 207-210 |
Veröffentlichung: | Wiley, 2002 |
Medientyp: | academicJournal |
ISSN: | 0014-5793 |
DOI: | 10.1016/s0014-5793(02)03676-1 |
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