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Properties and primary structure of the L-malate dehydrogenase from the extremely thermophilic archaebacterium Methanothermus fervidus
Article first published online: 3 MAR 2005
DOI: 10.1111/j.1432-1033.1990.tb15443.x
1742-4658/asset/cover.gif?v=1&s=fc98a9fc84ccc5e1b83463cabb40f397544364eb "European Journal of Biochemistry")
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How to Cite
HONKA, E., FABRY, S., NIERMANN, T., PALM, P. and HENSEL, R. (1990), Properties and primary structure of the L-malate dehydrogenase from the extremely thermophilic archaebacterium Methanothermus fervidus. European Journal of Biochemistry, 188: 623–632. doi: 10.1111/j.1432-1033.1990.tb15443.x
Publication History
- Issue published online: 3 MAR 2005
- Article first published online: 3 MAR 2005
- (Received September 11, 1989) – EJB 89 1102
- Abstract
- Article
- References
- Cited By
L-Malate dehydrogenase from the extremely thermophilic mathanogen Methanothermus fervidus was isolated and its phenotypic properties were characterized. The primary structure of the protein was deduced from the coding gene.
The enzyme is a homomeric dimer with a molecular mass of 70 kDa, possesses low specifity for NAD+ or NADP+ and catalyzes preferentially the reduction of oxalacetate. The temperature dependence of the activity as depicted in the Arrhenius and van't Hoff plots shows discontinuities near 52°C, as was found for glyceraldehyde-3-phosphate dehydrogenase from the same organism.
With respect to the primary structure, the archaebacterial L-malate dehydrogenase deviates strikingly from the eubacterial and eukaryotic enzymes. The sequence similarity is even lower than that between the L-malate dehydrogenases and L-lactate dehydrogenases of eubacteria and eukaryotes.
The phylogenetic meaning of this relationship is discussed.