Citation

Funaki T, Takanohashi Y, Fukazawa H, Kuruma I. Biochim. Biophys. Acta 1991; 1078(1): 43-46.

Copyright

(Copyright © 1991, Elsevier Publishing)

DOI

10.1016/0167-4838(91)90090-m

PMID

2049382

Abstract

A method was developed to estimate the extended Michaelis constant and maximum velocity of a suicide substrate from the time-course of remaining enzyme activity with the use of simulation data calculated from the representative kinetic model for a suicide substrate proposed by Walsh et al. (Walsh, C., Cromartie, T., Marcotte, P. and Spencer, R. (1978) Methods Enzymol. 53, 437-448). For this purpose an analytical equation for the time-course of remaining enzyme activity, based on the suicide kinetic model, was derived by the steady-state method reported by Tatsunami et al. (Tatsunami, S., Yago, N. and Hosoe, M. (1981) Biochim. Biophys. Acta 662, 226-235). The accuracy of this analytical solution was proved by comparing the result with the exact solution obtained by numerical computation. A method was also developed to estimate the most important factor for a suicide substrate, the partition ratio, from the time-course of remaining enzyme activity.

Language: en

Keywords

Enzyme Inhibitors; Enzymes; Kinetics; Models, Chemical