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

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A MOFRL family glycerate kinase from the thermophilic crenarchaeon, Sulfolobus tokodaii, with unique enzymatic properties.

A glycerate kinase gene (ST2037) from the hyperthermophilic crenarchaeon Sulfolobus tokodaii was cloned and expressed in Escherichia coli. The purified homodimeric protein (45 kDa) specifically catalyzed the formation of 2-phosphoglycerate with D-glycerate as substrate. The thermostable enzyme displayed maximum activity (over 20 min) at 90 degrees C and pH 4. 5. The maximal activity was in the presence of Co(2+). The MOFRL family glycerate kinase used AMP as phosphate donor with maximal activity towards GTP. These characteristics of the enzyme suggested its potential in the catalytic production of 2-phosphoglycerate.[1]

References

  1. A MOFRL family glycerate kinase from the thermophilic crenarchaeon, Sulfolobus tokodaii, with unique enzymatic properties. Liu, B., Wu, L., Liu, T., Hong, Y., Shen, Y., Ni, J. Biotechnol. Lett. (2009) [Pubmed]
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