Structural analysis of substrate and effector binding in Mycobacterium tuberculosis D-3-phosphoglycerate dehydrogenase

The crystal structure characterization of Mycobacterium tuberculosis D-3-phosphoglycerate dehydrogenase (PGDH) was carried out by using bound effector, L-serine, and substrate, hydroxypyruvic acid phosphate. The results provided insights into the enzyme activity kinetics and the residues interacting with the effector molecule and subsequent changes involved in allosteric inhibition in PGDH Mycobacterium enzyme.