Kinetics of the course of reactivation of aminoacylase reconstituted using Mn2+ ions.

The kinetic theory of the substrate reaction during irreversible change of enzyme activity previously described by Tsou [Tsou (1988), Adv. Enzymol Relat. Areas Mol. Biol. 61, 381-436] has been applied to a study of the kinetics of the course of reactivation during reconstitution of apo-aminoacylase using Mn2+ or Zn2+. The kinetic parameters for Mn(2+)- and Zn(2+)-reconstituted enzymes and the microscopic rate constants for reactivation during reconstitution were determined. The kinetic analysis suggests the presence of a second Mn2+ binding site in Mn(2+)-reconstituted aminoacylase.