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Malate dehydrogenases--structure and function Minarik P; Tomaskova N; Kollarova M; Antalik MGen Physiol Biophys 2002[Sep]; 21 (3): 257-65Malate dehydrogenases (MDH, L-malate:NAD oxidoreductase, EC 1.1.1.37), catalyze 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. They are homodimeric molecules in most organisms, including all eukaryots and the most bacterial species. 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 primary structure.|Animals[MESH]|Archaea/metabolism[MESH]|Bacteria/metabolism[MESH]|Catalysis[MESH]|Cytoplasm/*metabolism[MESH]|Enzyme Stability[MESH]|Isoenzymes/chemistry/classification/genetics/metabolism[MESH]|Malate Dehydrogenase/*chemistry/classification/genetics/*metabolism[MESH]|Mitochondria/*metabolism[MESH]|NAD/chemistry/metabolism[MESH]|Protein Conformation[MESH]|Species Specificity[MESH]|Structure-Activity Relationship[MESH] |
