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.
Zhang
Y X
YX
Department of Chemistry, Capital University of Medical Science, Beijing, China.
Le
W P
WP
Zhou
H M
HM
D000581:Amidohydrolases / Q000378:metabolism*; D000817:Anilino Naphthalenesulfonates; D000818:Animals; D001051:Apoenzymes / Q000378:metabolism; D001665:Binding Sites; D004789:Enzyme Activation; D005456:Fluorescent Dyes; D006868:Hydrolysis; D007668:Kidney / Q000201:enzymology; D007700:Kinetics; D008345:Manganese / Q000494:pharmacology*; D013050:Spectrometry, Fluorescence; D013552:Swine; D015032:Zinc / Q000494:pharmacology
D000817:Anilino Naphthalenesulfonates; D001051:Apoenzymes; D005456:Fluorescent Dyes; D008345:Manganese; C027132:1-anilino-8-naphthalenesulfonate; D000581:Amidohydrolases; C019672:aminoacylase I; D015032:Zinc