Lack of deviation from Michaelis–Menten kinetics for pig heart fumarase
- 1 September 1980
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 189 (3) , 653-654
- https://doi.org/10.1042/bj1890653
Abstract
Studies of steady-state kinetics of fumarase in the usual substrate-concentration range from 0.1 Km to 10 Km and in the high substrate-concentration range from 10 Km to 200 Km are described. The purpose is to investigate reports of substrate inhibition and oscillatory kinetics. In the normal substrate-concentration range, no deviations from hyperbolic kinetics were found, and in the extended concentration range, up to more than 200 times the Km value, no substrate inhibition was demonstrated. A discussion of the discrepancies between the mentioned reports of deviations from the hyperbolic kinetics and the present findings is given.This publication has 3 references indexed in Scilit:
- Does any enzyme follow the Michaelis—Menten equation?Molecular and Cellular Biochemistry, 1977
- Deviation from Michaelis-Menten kinetics for fumaraseBiochemical Journal, 1976
- A kinetic investigation of fumarase reaction at high substrate concentrationsArchives of Biochemistry and Biophysics, 1967