Steady-state parameters of an enzyme from n.m.r. spin transfer with thermal variation.
N.m.r. spin-exchange analysis of enzymic reactions at chemical equilibrium is akin to radioactive-tracer-exchange analysis; unidirectional flux rates are obtained for the overall reaction. These data, by themselves, are not sufficient to define the values of all the individual rate constants or steady-state parameters. However, it is shown that, by measuring the dependence of the exchange rate constants on solute concentration and temperature, the individual rate constants, and hence the steady-state parameters, can be obtained for a simple enzyme system.
Kuchel
P W
PW
Department of Biochemistry, University of Sydney, N.S.W., Australia.
D004798:Enzymes / Q000378:metabolism*; D007700:Kinetics; D009682:Magnetic Resonance Spectroscopy; D008956:Models, Chemical; D013696:Temperature
D004798:Enzymes