Malate dehydrogenases--structure and function.
Malate 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.
Minárik
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Institute of Molecular Biology, Slovak Academy of Sciences, Dúbravská cesta 21, 842 51 Bratislava 4, Slovakia.
Tomásková
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Kollárová
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Antalík
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M
D000818:Animals; D001105:Archaea / Q000378:metabolism; D001419:Bacteria / Q000378:metabolism; D002384:Catalysis; D003593:Cytoplasm / Q000378:metabolism*; D004795:Enzyme Stability; D007527:Isoenzymes / Q000737:chemistry / Q000145:classification / Q000235:genetics / Q000378:metabolism; D008291:Malate Dehydrogenase / Q000737:chemistry* / Q000145:classification / Q000235:genetics / Q000378:metabolism*; D008928:Mitochondria / Q000378:metabolism*; D009243:NAD / Q000737:chemistry / Q000378:metabolism; D011487:Protein Conformation; D013045:Species Specificity; D013329:Structure-Activity Relationship
D007527:Isoenzymes; D009243:NAD; D008291:Malate Dehydrogenase