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. Copyright © 1967, Wiley Blackwell. All rights reserved
Transamidinase of hog kidney VI Effects of the modification of cysteine residues on the catalytic activity
GRAZI, Enrico;
1967
Abstract
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. Copyright © 1967, Wiley Blackwell. All rights reservedFile in questo prodotto:
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