Transition-state analysis of a Vmax mutant of AMP nucleosidase by the application of heavy-atom kinetic isotope effects.

doi:10.1021/bi00232a032

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Article

Transition-state analysis of a Vmax mutant of AMP nucleosidase by the application of heavy-atom kinetic isotope effects.

Biochemistry - 7 May 1991

Parkin D W, Mentch F, Banks G A, Horenstein B A, Schramm V L

Abstract excerpt

The transition state of the Vmax mutant of AMP nucleosidase from Azotobacter vinelandii [Leung, H. B., & Schramm, V. L. (1981) J. Biol. Chem. 256, 12823-12829] has been characterized by heavy-atom kinetic isotope effects in the presence and absence of MgATP, the allosteric activator. The enzyme c...

Topics

Adenosine Monophosphate
Adenosine Triphosphate
Allosteric Regulation
Azotobacter
Binding, Competitive
Enzyme Activation
Hydrolysis
Isotopes
Kinetics
Mutation
N-Glycosyl Hydrolases
Substrate Specificity

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