Role of the anion-binding site in catalysis and regulation of Mycobacterium tuberculosis D-3-phosphoglycerate dehydrogenase

A simulation of transient kinetic data is used to demonstrate the allosteric mechanism for Mycobacterium tuberculosis D-3-phosphoglycerate dehydrogenaserelated regulation mediated by to interaction of substrate at second site called the anion-binding site. The result indicated that a ligand bound to the anion-binding site of L-serine inhibition provide a potential mechanism for low levels of activity in the presence of high levels of inhibitor.