catalytic mechanism, malate is bound deeply in the active site, Mn2+ catalyzes the entire reaction, Lys183 is the general base for oxidation, Tyr112-Lys183 functions as the general acid-base pair to catalyze the tautomerization of the enolpyruvate product from decarboxylation to pyruvate, substrate and cofacor binding modes
isozyme NAD-ME2 and chimeric mutant NAD-ME1q follow a sequential ordered Bi-Ter mechanism, NAD+ being the leading substrate followed by (S)-malate. Hetereodimer NAD-MEH can bind both substrates randomly. Interaction between NAD-ME1 and -ME2 generates a heteromeric isozyme NAD-MEH with a particular kinetic behaviour
isozyme NAD-ME2 and chimeric mutant NAD-ME1q follow a sequential ordered Bi-Ter mechanism, NAD+ being the leading substrate followed by (S)-malate. Isozyme NAD-ME1 and hetereodimer NAD-MEH can bind both substrates randomly. However, NAD-ME1 shows a preferred route that involves the addition of NAD+ first. interaction between NAD-ME1 and -ME2 generates a heteromeric isozyme NAD-MEH with a particular kinetic behaviour