Malate dehydrogenase (Escherichia coli) (MDH)

Malate dehydrogenase (MDH) from Escherichia coli is a fundamental metabolic enzyme that catalyzes the reversible conversion of L-malate to oxaloacetate, utilizing NAD+ as a cofactor [1]. It is an essential component of the tricarboxylic acid (TCA) cycle and plays a vital role in gluconeogenesis and the maintenance of the cellular redox state by regulating the NAD+/NADH ratio [2]. Because it is central to bacterial energy production and carbon metabolism, E. coli MDH is a target of interest for the development of novel antibacterial agents, particularly to combat multi-drug resistant infections [3]. Although it shares structural similarities with eukaryotic MDHs, specific differences in its active site architecture and allosteric regulation allow for the possibility of developing selective inhibitors [4]. Most current research focuses on experimental small molecules designed to disrupt bacterial metabolic pathways without affecting the host's mitochondrial or cytosolic MDH functions [5].

Other names

L-malate dehydrogenaseNAD-dependent malate dehydrogenaseMdhMalic dehydrogenase

Inhibition of the enzyme's catalytic activity by competing with the NAD+ cofactor or the L-malate substrate for binding at the active site, thereby disrupting the tricarboxylic acid (TCA) cycle.