A hexokinase with broad sugar specificity from a thermophilic bacterium

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dc.contributor.authorJungdon Bae-
dc.contributor.authorDooil Kim-
dc.contributor.authorYongseok Choi-
dc.contributor.authorSukhoon Koh-
dc.contributor.authorJung Eun Park-
dc.contributor.authorJoong Su Kim-
dc.contributor.authorSeong Hoon Moon-
dc.contributor.authorBo-Hyun Park-
dc.contributor.authorMi Ri Park-
dc.contributor.authorHye-Eun Song-
dc.contributor.authorSuk-In Hong-
dc.contributor.authorDae Sil Lee-
dc.date.accessioned2017-04-19T09:03:11Z-
dc.date.available2017-04-19T09:03:11Z-
dc.date.issued2005-
dc.identifier.issn0006291X-
dc.identifier.uri10.1016/j.bbrc.2005.06.160ko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/7045-
dc.description.abstractA 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.-
dc.publisherElsevier-
dc.titleA hexokinase with broad sugar specificity from a thermophilic bacterium-
dc.title.alternativeA hexokinase with broad sugar specificity from a thermophilic bacterium-
dc.typeArticle-
dc.citation.titleBiochemical and Biophysical Research Communications-
dc.citation.number3-
dc.citation.endPage763-
dc.citation.startPage754-
dc.citation.volume334-
dc.contributor.affiliatedAuthorJoong Su Kim-
dc.contributor.alternativeName배정돈-
dc.contributor.alternativeName김두일-
dc.contributor.alternativeName최용석-
dc.contributor.alternativeName고석훈-
dc.contributor.alternativeName박정은-
dc.contributor.alternativeName김중수-
dc.contributor.alternativeName문성훈-
dc.contributor.alternativeName박보현-
dc.contributor.alternativeName박미리-
dc.contributor.alternativeName송혜은-
dc.contributor.alternativeName홍석인-
dc.contributor.alternativeName이대실-
dc.identifier.bibliographicCitationBiochemical and Biophysical Research Communications, vol. 334, no. 3, pp. 754-763-
dc.identifier.doi10.1016/j.bbrc.2005.06.160-
dc.subject.keywordGlycolysis-
dc.subject.keywordHexokinase-
dc.subject.keywordMolecular modeling-
dc.subject.keywordROK-
dc.subject.keywordSubstrate specificity-
dc.subject.keywordThermus-
dc.subject.localGlycolysis-
dc.subject.localHexokinase-
dc.subject.localMolecular modeling-
dc.subject.localROK-
dc.subject.localSubstrate specificity-
dc.subject.localThermus-
dc.description.journalClassY-
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Division of Bio Technology Innovation > SME Support Center > 1. Journal Articles
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