Open AccessTransamidinase of Hog Kidney
Author(s) -
Grazi E.,
Vigi V.,
Rossi N.
Publication year - 1967
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1967.tb00061.x
Subject(s) - cysteine , hydroxylamine , amidine , chemistry , residue (chemistry) , arginine , enzyme , catalysis , glycine , biochemistry , amino acid , stereochemistry
The modification of one cysteine residue of transamidinase by reaction with 5,5′‐dithiobis‐2‐nitrobenzoic acid alters the catalytic properties of the enzyme. The Michaelis constant of transamidinase for arginine is increased and the capacity to utilize glycine and hydroxylamine as amidine acceptors is lost. Arginine, the amidine donor substrate, protects the cysteine residue and prevents the changes in catalytic activity induced by the treatment with 5,5′‐dithiobis‐2‐nitrobenzoic acid.