Article Abstract:
Previous research demonstrated a homology between the genetic sequence of the human inositol monophosphatase (I-1-Pase) and the MJ109 gene product of Methanococcus jannaschii. This has prompted efforts to clone and express the gene in the Escherichia coli in order to characterize the enzyme. Kinetic characterization of the M. jannaschii I-1-Pase found that magnesium ions are required for optimal activity. On the other hand, lithium ions were found to inhibit its activity. Further tests also revealed that the methanogen I-1-Pase hydrolyzed a broader substrate range.
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Article Abstract:
A study was conducted on the influence of osmolyte precursors on compatible solute distribution in the halophilic methanogen Methanohalophilus portucalensis. Results reveal that Beta-glutamate and alpha-lysine precursors have minimal effects on Beta-amino acid accumulation. The most significant effect was exhibited by L-alpha-glutamine, indicating the role of nitrogen assimilation in osmolyte distribution.
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Article Abstract:
The glutamine synthetase from Methanohalophilus portucalensis can convert beta-glutamate to beta-glutamine, which is used as an osmolyte in high-NaCl environments. Most bacterial synthetases prefer alpha-glutamate over beta-glutamate.
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