Abstract 1143 pH dependence of Human Malate Dehydrogenase Kinetics

Human mitochondrial malate dehydrogenase (hMDH2) is a key enzyme in the Kreb's cycle; a central metabolic pathway. In this role, hMDH2 catalyzes the conversion of L-malate to oxaloacetate. hMDH2 can also catalyze the reverse reaction to replenish the stock of NAD+, making MDH a focal point of carbohydrate metabolism. hMDH2 is regulated through phosphorylation of the enzyme. If regulation fails, many issues can arise, including metabolic disorders and cancer.1 This regulation process can be replicated using phosphomimics, substituting serine and threonine residues with aspartic acid to mimic a phosphorylation site.