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 pr...

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Bibliographic Details
Published in:Biochemistry (Moscow) 2005-09, Vol.70 (9), p.1027-1030
Main Authors: Eprintsev, A T, Falaleeva, M I, Parfyonova, N V
Format: Article
Language:English
Subjects:
Bacteria
Bacteria - enzymology
Dehydrogenase
Enzyme Stability - physiology
Enzymes
Kinetics
Malate Dehydrogenase - chemistry
Malate Dehydrogenase - isolation & purification
Molecular Weight
Oligomers
Oxidoreductases
Protein Conformation
Rigidity
Temperature
Thermus - enzymology
Time Factors
Vulcanithermus medioatlanticus
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Summary: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.
ISSN:0006-2979
1608-3040
0320-9725
DOI:10.1007/s10541-005-0220-2