malate dehydrogenase 1, nad

Malate dehydrogenases 1(MDH1 MDHA) is a soluble form of malate dehydrogenases. Malate dehydrogenases (MDH) is a group of multimeric enzymes consisting of identical subunits usually organized as either dimer or tetramers with subunit molecular weights of 30-35 kDa. MDH has been isolated from different sources including archaea, eubacteria, fungi, plants, and mammals. MDH catalyzes the NAD NADH-dependent interconversion of the substrates malate and oxaloacetate. This reaction plays a key part in the malate aspartate shuttle across the mitochondrial membrane, and in the tricarboxylic acid cycle within the mitochondrial matrix. The enzymes share a common catalytic mechanism and their kinetic properties are similar, which demonstrates a high degree of structural similarity. The three-dimensional structures and elements essential for catalysis are conserved between mitochondrial and cytoplasmic forms of MDH in eukaryotic cells even though these isoenzymes are only marginally related at the level of the primary structure.

Malate dehydrogenase, mitochondrial is a 338 amino acids protein that belongs to the LDH MDH superfamily. MDH type 1 family. MDH2 catalyzes the reversible oxidation of malate to oxaloacetate, utilizing the NAD NADH cofactor system in the citric acid cycle. MDH2 is localized to the mitochondria and takes part in the malate-aspartate shuttle that functions in the metabolic coordination between cytosol and mitochondria. MDH2 is highly expressed in the adrenal system, small intestine, heart and pancreas.