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

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Abstract

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°C and pH 4.5. The maximal activity was in the presence of Co2+. 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.

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Acknowledgements

This work was supported by grants from the National Basic Research Program (2004CB719604) and the State Key Laboratory of Microbial Technology of China.

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Authors and Affiliations

  1. College of Food and Bioengineering, Shandong Institute of Light Industry, Jinan, 250353, People’s Republic of China

    Bo Liu & Tianming Liu

  2. State Key Laboratory of Microbial Technology, Shandong University, Jinan, 250100, People’s Republic of China

    Lei Wu, Ye Hong, Yulong Shen & Jinfeng Ni

Authors
  1. Bo Liu
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  2. Lei Wu
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  3. Tianming Liu
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  4. Ye Hong
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  5. Yulong Shen
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  6. Jinfeng Ni
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Corresponding author

Correspondence to Jinfeng Ni.

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10529_2009_89_MOESM1_ESM.docx

Supplementary Fig. 1 Alignment of the amino acid sequences of S. tokodaii GK with some of its homologous proteins. Numbering of the amino acids is indicated on the right. Conserved residues are indicated by an asterisk above the alignment, single and double dots represent amino acids with semi-conservative and conservative substitutions. Gaps are indicated as dashes. The residues of conserved glycine rich loop are underlined in bold. The MOFRL domain of GKPh is underlined. Seven conserved amino acids of the presumed active site are boxed. Sto S. tokodaii, Mse M. sedula, Cma C. Maquilingensis, Pho P. horikoshii, Tte T. tenax, Tma Thermotoga maritima. Accession numbers for these sequences are stated in “Sequence and primary structure features” in Results (DOCX 147 kb)

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Liu, B., Wu, L., Liu, T. et al. A MOFRL family glycerate kinase from the thermophilic crenarchaeon, Sulfolobus tokodaii, with unique enzymatic properties. Biotechnol Lett 31, 1937–1941 (2009). https://doi.org/10.1007/s10529-009-0089-z

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  • DOI: https://doi.org/10.1007/s10529-009-0089-z

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