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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Gene cloning, heterologous overexpression and optimized refolding of the NAD-glutamate dehydrogenase from Haloferax mediterranei.

The NAD-dependent glutamate dehydrogenase ( GDH) gene from the halophilic archaeon Haloferax mediterranei has been cloned. The analysis of the nucleotide sequence revealed an open reading frame of 1323 bp that encodes a NAD- GDH. The amino acid sequence displayed high homology with those from other sources, especially the highly conserved residues involved in 2-oxoglutarate binding. The expression of this gene in Escherichia coli, the refolding and further characterization, yielded a fully active NAD- GDH with the same features than those found for the wild-type enzyme. This halophilic NAD- GDH showed a highly dependence on salts for both stability and activity, being essential for the refolding of the recombinant enzyme.[1]

References

  1. Gene cloning, heterologous overexpression and optimized refolding of the NAD-glutamate dehydrogenase from Haloferax mediterranei. Díaz, S., Pérez-Pomares, F., Pire, C., Ferrer, J., Bonete, M.J. Extremophiles (2006) [Pubmed]
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