Minárik P, Tomásková N, Kollárová M, Antalík M
Institute of Molecular Biology, Slovak Academy of Sciences, Dúbravská cesta 21, 842 51 Bratislava 4, Slovakia.
Gen Physiol Biophys. 2002 Sep;21(3):257-65.
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.
苹果酸脱氢酶(MDH,L-苹果酸:NAD氧化还原酶,EC 1.1.1.37)催化苹果酸和草酰乙酸底物之间依赖NAD/NADH的相互转化。该反应在苹果酸/天冬氨酸穿梭穿过线粒体膜以及线粒体基质中的三羧酸循环中起关键作用。在大多数生物体中,包括所有真核生物和大多数细菌物种,它们都是同型二聚体分子。这些酶具有共同的催化机制,其动力学性质相似,这表明它们具有高度的结构相似性。尽管这些同工酶在一级结构水平上仅有微弱关联,但真核细胞中线粒体和细胞质形式的MDH之间催化所必需的三维结构和元件是保守的。