Journal
BIOCHEMISTRY-MOSCOW
Volume 70, Issue 9, Pages 1027-1030Publisher
MAIK NAUKA/INTERPERIODICA/SPRINGER
DOI: 10.1007/s10541-005-0220-2
Keywords
malate dehydrogenase; purification; Vulcanithermus medioatlanticus; oligomeric structure; catalytic properties; thermostability
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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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