Shaklai N, Zisapel N, Sokolovsky M
Proc Natl Acad Sci U S A. 1973 Jul;70(7):2025-8. doi: 10.1073/pnas.70.7.2025.
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.
羧肽酶B的发光光谱表明,由于活性位点处酪氨酸残基的状态,锌酶和脱辅基酶之间存在特定差异。当形成酶-底物或酶-抑制剂复合物时,这些差异消失,这表明它们可能反映了天然酶中酪氨酸残基与催化必需的锌原子之间的相互作用。本文对该酪氨酸残基在羧肽酶B作用机制中的作用进行了解释。