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. 1973 Jul;70(7):2025–2028. doi: 10.1073/pnas.70.7.2025

The Role of a Tyrosyl Residue in the Mechanism of Action of Carboxypeptidase B: Luminescence Studies

Nurith Shaklai 1, Nava Zisapel 1, Mordechai Sokolovsky 1,*
PMCID: PMC433657  PMID: 4516202

Abstract

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.

Keywords: fluorescence, phosphorescence, enzyme mechanism

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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