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Gene Review:

MJ_0490 - malate dehydrogenase

Methanocaldococcus jannaschii DSM 2661

Lee, B.I. et al., Madern, D., Graupner, M. et al.

Madern,

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High impact information on MJ0490

The putative L-lactate dehydrogenase from Methanococcus jannaschii is an NADPH-dependent L-malate dehydrogenase [1].
It was shown to be an NADPH-dependent [lactate dehydrogenase (LDH)-like] L-malate dehydrogenase (MalDH) and not an L-lactate dehydrogenase, as had been suggested previously on the basis of amino acid sequence similarity [1].
Crystal structure of the MJ0490 gene product of the hyperthermophilic archaebacterium Methanococcus jannaschii, a novel member of the lactate/malate family of dehydrogenases [2].
The MJ0490 gene, one of the only two genes of Methanococcus jannaschii showing sequence similarity to the lactate/malate family of dehydrogenases, was classified initially as coding for a putative l-lactate dehydrogenase (LDH) [2].
The enzymatic assay showed that the MJ0490 protein possesses the fructose-1,6-bisphosphate-activated LDH activity (reduction) [2].

Associations of MJ0490 with chemical compounds

Both the MJ1425-encoded enzyme and the MJ0490-encoded enzyme were found to function to different degrees as malate dehydrogenases, reducing oxalacetate to (S)-malate using either NADH or NADPH as a reductant [3].

References

The putative L-lactate dehydrogenase from Methanococcus jannaschii is an NADPH-dependent L-malate dehydrogenase. Madern, D. Mol. Microbiol. (2000) [Pubmed]
Crystal structure of the MJ0490 gene product of the hyperthermophilic archaebacterium Methanococcus jannaschii, a novel member of the lactate/malate family of dehydrogenases. Lee, B.I., Chang, C., Cho, S.J., Eom, S.H., Kim, K.K., Yu, Y.G., Suh, S.W. J. Mol. Biol. (2001) [Pubmed]
Identification of an archaeal 2-hydroxy acid dehydrogenase catalyzing reactions involved in coenzyme biosynthesis in methanoarchaea. Graupner, M., Xu, H., White, R.H. J. Bacteriol. (2000) [Pubmed]

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