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Updated: Aug 13, 2026

Mapping Metabolism: Monitoring Lactate Dehydrogenase Activity Directly in Tissue
Published on: June 21, 2018
Malate dehydrogenase from the thermophilic bacterium Vulcanithermus medioatlanticus
A T Eprintsev1, M I Falaleeva, N V Parfyonova
1Voronezh State University, Voronezh, 394006, Russia. bsbc366@main.vsu.ru
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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