Malate dehydrogenases--structure and function.
2002; National Institutes of Health; Volume: 21; Issue: 3 Linguagem: Inglês
Autores
Peter Minárik, Nataša Tomášková, Marta Kollárová, Marián Antalı́k,
Tópico(s)Amino Acid Enzymes and Metabolism
ResumoMalate 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.
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