Co+2-Substituted Acylamino Acid Amido Hydrolase from Aspergillus oryzae
نویسندگان
چکیده
The inactivation of the Zn+2 metallo enzyme acylamino acid amido hydrolase from Aspergillus oryzae by ethylendiamine-tetraacetate (EDTA) and nitrilotriacetate (NTA) and the effects of Phe and His on this process were studied. Reactivation of the enzyme by Zn+2or Co+2-NTA buffer revealed a dissociation constant for the Zn+2-enzyme of 10~10 M and for the Co+2-enzyme of 10-7-5 m. The kinetic properties of the Zn+2 and Co+2 enzyme were compared for a series of substrates. Substitution of Co+2 for Zn+2 reduces substrate specificity of the enzyme.
منابع مشابه
Studies on the Zn2+/Co2+ exchange with acylamino acid amidohydrolase from pig kidney.
The kinetics of inactivation of the Zn2+-metalloenzyme acyl-amino acid amido hydrolase by chelating ligands were studied. The rate of inactivation by 1,10-phenanthroline is enhanced by histidine and inhibited in the presence of phenyl-alanine. Removal of the metal ion increases the heat stability and decreases the pH stability of the enzyme. Reactivation of the inactive metal free enzyme is pos...
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