Substrate-induced hysteresis in the activity of Escherichia coli dihydrofolate reductase.
Full time course studies of the kinetic activity of Escherichia coli dihydrofolate reductase show that there is an increase in activity with time. The half-time for this hysteretic behavior is about 9 s. Preincubation of the enzyme with either of the substrates abolishes the lag and results in initial velocities which are 2-2.3-fold faster than those observed for the non-preincubated enzyme. The kinetic properties of the activated and nonactivated forms of the enzyme appear to be similar as measured by the full time course of the reaction. The results are consistent with observations for NADPH binding studies that the enzyme exists in two interconvertible forms, one of which is incapable of binding NADPH (Cayley, P. J., Dunn, S. M. J., and King, R. W. (1981) Biochemistry 20, 874-879).
D001665:Binding Sites; D004926:Escherichia coli / Q000201:enzymology*; D005492:Folic Acid / Q000031:analogs & derivatives / Q000378:metabolism; D007700:Kinetics; D009249:NADP / Q000378:metabolism; D013762:Tetrahydrofolate Dehydrogenase / Q000378:metabolism*; D013997:Time Factors
C010920:dihydrofolate; D009249:NADP; D005492:Folic Acid; D013762:Tetrahydrofolate Dehydrogenase