The role of a tyrosyl residue in the mechanism of action of carboxypeptidase B: luminescence studies.
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.
14 references, click to expand
-
Techniques for measuring fluorescence and phosphorescence of biological materials.Photochem Photobiol. 1968 Dec;8(6):589-99 PMID: 5715700
-
Porcine carboxypepticase B: multiple substrates binding modes.Biochem Biophys Res Commun. 1972 Jan 31;46(2):357-63 PMID: 5061924
-
Differences between the conformation of arsanilazotyrosine 248 of carboxypeptidase A in the crystalline state and in solution.Proc Natl Acad Sci U S A. 1971 Oct;68(10):2532-5 PMID: 5289887
-
The sequence around the active-center tyrosyl of porcine carboxypeptidase B.Eur J Biochem. 1971 Jan 1;18(1):79-85 PMID: 4924880
-
Effect of pH on the phosphorescence of tryptophan, tyrosine, and proteins.J Biol Chem. 1967 Jun 25;242(12):2979-85 PMID: 6027259
-
Isolation and sequence of peptides at the active center of bovine carboxypeptidase B.J Biol Chem. 1969 Oct 10;244(19):5246-53 PMID: 5344132
-
Evidence for tyrosine at the active center of bovine carboxypeptidase B.J Biol Chem. 1966 Apr 10;241(7):1648-50 PMID: 5946620
-
The kinetics of carboxypeptidase B activity.J Biol Chem. 1962 Oct;237:3094-9 PMID: 14001579
-
Porcine carboxypeptidase B. Nitration of the functional tyrosyl residue with tetranitromethane.Eur J Biochem. 1972 Feb 15;25(2):267-73 PMID: 5064743
-
EFFECT OF THE PHYSICAL ENVIRONMENT ON EXCITED STATES OF AMINO ACIDS AND PROTEINS.Biopolym Symp. 1964;13:441-52 PMID: 14210468
-
The tyrosyl residues at the active site of aminopeptidase M modifications by tetranitromethane.FEBS Lett. 1969 Aug;4(4):262-264 PMID: 11947198
-
ENERGY TRANSFER IN PROTEINS.Nature. 1964 Sep 12;203:1145-7 PMID: 14213662
-
On the nature of tyrosine phosphorescence from proteins.Biochem Biophys Res Commun. 1966 May 25;23(4):570-5 PMID: 5961095
-
Porcine carboxypeptidase B. Arsanilazocarboxypeptidase, spectral and functional consequences of modification of tyrosine-"248".Eur J Biochem. 1972 Feb;25(3):483-90 PMID: 5065075
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