Open AccessThe Role of a Tyrosyl Residue in the Mechanism of Action of Carboxypeptidase B: Luminescence Studies
Author(s) -
Nurith Shaklai,
Nava Zisapel,
Mordechai Sokolovsky
Publication year - 1973
Publication title -
proceedings of the national academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.70.7.2025
Subject(s) - carboxypeptidase a , carboxypeptidase , residue (chemistry) , chemistry , enzyme , active site , stereochemistry , luminescence , mechanism of action , zinc , biochemistry , organic chemistry , in vitro , materials science , optoelectronics
The luminescence spectra of carboxypeptidase B indicate specific differences between the zinc and apoenzyme due to the state of tyrosyl residues presumably at the active site. These differences disappear when enzyme-substrate or enzyme-inhibitor complexes are formed, suggesting that they may reflect the interaction of a tyrosyl residue in the native enzyme with the catalytically essential zinc atom. An interpretation of the role of that tyrosyl residue in the mechanism of action of carboxypeptidase B is presented.
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