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Dedicated to Prof. H. Zahn on the Ocassion of His 65th Birthday Zn+2/Co+2 Exchange, Microbial Acylamino Acid Amido Hydrolase, Aspergillus oryzae, Kinetic Properties 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+2-or Co+2-NTA buffer revealed a dissociation constant for the Zn+2-enzymedoi:10.1515/znc-1981-9-1010 fatcat:7bkleyzafbdxdnavexwpqvmaqq