title: Malate dehydrogenase from the thermophilic bacterium Vulcanithermus medioatlanticus.
abstract: 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.
authors.affiliation: Voronezh State University, Voronezh, 394006, Russia. bsbc366@main.vsu.ru
authors.forename: A T
authors.initials: AT
authors.lastname: Eprintsev
authors.forename: M I
authors.initials: MI
authors.lastname: Falaleeva
authors.forename: N V
authors.initials: NV
authors.lastname: Parfyonova
mesh_terms: 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
chemical_list: D008291:Malate Dehydrogenase