Abstract
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 Mn2+-and Zn2+-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 Mn2+-reconstituted aminoacylase.
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Zhang, YX., Le, WP. & Zhou, HM. Kinetics of the course of reactivation of aminoacylase reconstituted using Mn2+ ions. J Protein Chem 14, 695–701 (1995). https://doi.org/10.1007/BF01886908
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DOI: https://doi.org/10.1007/BF01886908