A hexokinase with broad sugar specificity from a thermophilic bacterium

Jungdon Bae, Dooil Kim, Yongseok Choi, Sukhoon Koh, Eun Park Jung, Su Kim Joong, Hoon Moon Seong, Bo Hyun Park, Miri Park, Hye Eun Song, Suk In Hong, Dae Sil Lee

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9 Citations (Scopus)

Abstract

A recombinant thermophilic Thermus caldophilus GK24 hexokinase, one of the ROK-type (repressor protein, open reading frames, and sugar kinase) proteins, exists uniquely as a 120 kDa molecule with four subunits (31 kDa), in contrast to eukaryotic and bacterial sugar kinases which are monomers or dimers. The optimal temperature and pH for the enzyme reaction are 70-80°C and 7.5, respectively. This enzyme shows broad specificity toward glucose, mannose, glucosamine, allose, 2-deoxyglucose, and fructose. To understand the sugar specificity at a structural level, the enzyme-ATP/Mg2+-sugar binding complex models have been constructed. It has been shown that the sugar specificity is probably dependent on the interaction energy occurred by the positional proximity of sugars bound in the active site of the enzyme, which exhibits a tolerance to modification at C2 or C3 of glucose.

Original languageEnglish
Pages (from-to)754-763
Number of pages10
JournalBiochemical and Biophysical Research Communications
Volume334
Issue number3
DOIs
Publication statusPublished - 2005 Sep 2
Externally publishedYes

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Keywords

  • Glycolysis
  • Hexokinase
  • Molecular modeling
  • ROK
  • Substrate specificity
  • Thermus

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Bae, J., Kim, D., Choi, Y., Koh, S., Jung, E. P., Joong, S. K., Seong, H. M., Park, B. H., Park, M., Song, H. E., Hong, S. I., & Lee, D. S. (2005). A hexokinase with broad sugar specificity from a thermophilic bacterium. Biochemical and Biophysical Research Communications, 334(3), 754-763. https://doi.org/10.1016/j.bbrc.2005.06.160