serves to broaden the pH-optimum, at pH 7.5 approximately 4fold stimulation, the effect is more marked when HCO3 is also present, below pH 7 no effect on activity
serves to broaden the pH-optimum, at pH 7.5 approximately 4fold stimulation, the effect is more marked when HCO3 is also present, below pH 7 no effect on activity
Arabidopsis NAD-ME1 is strongly stimulated by fumarate. Fumarate binding turns NAD-ME1 into a hyperbolic and high substrate affinity enzyme. This effect is also observed when the allosteric site is either removed or altered. Hence, fumarate is not really an activator, but suppresses the inhibitory effect of L-malate. Binding of L-malate and fumarate at the same allosteric site
Arabidopsis NAD-ME1 is strongly stimulated by fumarate. Fumarate binding turns NAD-ME1 into a hyperbolic and high substrate affinity enzyme. This effect is also observed when the allosteric site is either removed or altered. Hence, fumarate is not really an activator, but suppresses the inhibitory effect of L-malate. Binding of L-malate and fumarate at the same allosteric site. Arg84 is essential for fumarate activation
activates in both reaction directions synergistically with L-malate both binding at separate allosteric sites different from the active site, R105 and K143 are involved
activates in both reaction directions synergistically with fumarate both binding at separate allosteric sites different from the active site, R105 and K143 are involved