Malate dehydrogenase from the thermophilic bacterium Vulcanithermus medioatlanticus.
Thermostable dimeric malate dehydrogenase (MDH) was isolated from the microorganism of hydrothermal vents Vulcanithermus medioatlanticus. The enzyme was electrophoretically homogeneous and possessed the specific activity of 6.9 U/mg. The large molecular weight of the subunits (55 kD) is likely to provide the rigidity of the enzyme structure (the activation energy of the enzymatic reaction is 32.6 kJ/mol). The thermophilic MDH differs little from the mesophilic enzyme in terms of kinetic and regulatory characteristics.
Eprintsev
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Voronezh State University, Voronezh, 394006, Russia. bsbc366@main.vsu.ru
Falaleeva
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MI
Parfyonova
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NV
D001419:Bacteria / Q000201:enzymology*; D004795:Enzyme Stability / Q000502:physiology; D007700:Kinetics; D008291:Malate Dehydrogenase / Q000737:chemistry / Q000302:isolation & purification*; D008970:Molecular Weight; D011487:Protein Conformation; D013696:Temperature; D013824:Thermus / Q000201:enzymology*; D013997:Time Factors
D008291:Malate Dehydrogenase