A hexokinase with broad sugar specificity from a thermophilic bacterium

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Title
A hexokinase with broad sugar specificity from a thermophilic bacterium
Author(s)
Jungdon Bae; Dooil Kim; Yongseok Choi; Sukhoon Koh; Jung Eun Park; Joong Su Kim; Seong Hoon Moon; Bo-Hyun Park; Mi Ri Park; Hye-Eun Song; Suk-In Hong; Dae Sil Lee
Bibliographic Citation
Biochemical and Biophysical Research Communications, vol. 334, no. 3, pp. 754-763
Publication Year
2005
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.
Keyword
GlycolysisHexokinaseMolecular modelingROKSubstrate specificityThermus
ISSN
0006-291X
Publisher
Elsevier
DOI
http://dx.doi.org/10.1016/j.bbrc.2005.06.160
Type
Article
Appears in Collections:
Division of Bio Technology Innovation > SME Support Center > 1. Journal Articles
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