Determination of rapid-equilibrium kinetic parameters of ordered and random enzyme-catalyzed reaction A+B=P+Q.
This article deals with the rapid-equilibrium kinetics of the forward and reverse reactions together for the ordered and random enzyme-catalyzed A+B=P+Q and emphasizes the importance of reporting the values of the full set of equilibrium constants. Equilibrium constants that are not in the rate equation can be calculated for random mechanisms using thermodynamic cycles. This treatment is based on the use of a computer to derive rate equations for three mechanisms and to estimate the kinetic parameters with the minimum number of velocity measurements. The most general of these three programs is the one to use first when the mechanism for A+B=P+Q is studied for the first time. This article shows the effects of experimental errors in velocity measurements on the values of the kinetic parameters and on the apparent equilibrium constant calculated using the Haldane relation.
Alberty
Robert A
RA
Department of Chemistry, Massachusetts Institute of Technology, Room 6-215, 77 Massachusetts Avenue, Cambridge, Massachusetts 02138, USA. alberty@mit.edu
D055162:Biocatalysis; D003198:Computer Simulation; D004798:Enzymes / Q000378:metabolism*; D007700:Kinetics; D013816:Thermodynamics
D004798:Enzymes