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.
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Translated from Biokhimiya, Vol. 70, No. 9, 2005, pp. 1245–1249.
Original Russian Text Copyright © 2005 by Eprintsev, Falaleeva, Parfyonova.
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Eprintsev, A.T., Falaleeva, M.I. & Parfyonova, N.V. Malate Dehydrogenase from the Thermophilic Bacterium Vulcanithermus medioatlanticus . Biochemistry (Moscow) 70, 1027–1030 (2005). https://doi.org/10.1007/s10541-005-0220-2
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DOI: https://doi.org/10.1007/s10541-005-0220-2