Please use this identifier to cite or link to this item: https://doi.org/10.1016/j.bbrc.2011.10.083
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dc.titleBiochemical and structural analysis of Gox2181, a new member of the SDR superfamily from Gluconobacter oxydans
dc.contributor.authorLiu, X.
dc.contributor.authorYuan, Z.
dc.contributor.authorAdam Yuan, Y.
dc.contributor.authorLin, J.
dc.contributor.authorWei, D.
dc.date.accessioned2014-10-27T08:22:50Z
dc.date.available2014-10-27T08:22:50Z
dc.date.issued2011-11-18
dc.identifier.citationLiu, X., Yuan, Z., Adam Yuan, Y., Lin, J., Wei, D. (2011-11-18). Biochemical and structural analysis of Gox2181, a new member of the SDR superfamily from Gluconobacter oxydans. Biochemical and Biophysical Research Communications 415 (2) : 410-415. ScholarBank@NUS Repository. https://doi.org/10.1016/j.bbrc.2011.10.083
dc.identifier.issn0006291X
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/100171
dc.description.abstractGluconobacter oxydans enable to oxidize sugars and polyols incompletely to corresponding materials with potential industrial applications, containing around 75 putative dehydrogenases. One of these putative dehydrogenases, Gox2181, was cloned and expressed in Escherichia coli BL21 (DE3), and its X-ray crystal structure was determined to a resolution of 1.8å. Gox2181 formed a homo-tetramer in the crystal that was coincident with the apparent molecular mass determined in the solution. Gox2181 displayed α/β-folding patterns, the conserved catalytic tetrad of Asn119-Ser147-Tyr162-Lys166, and the NAD-binding pocket, which aligned well with the 'classical' type of short-chain dehydrogenase/reductase (SDR) enzymes. Gox2181 was denoted SDR51C based on the SDR nomenclature system. The purified recombinant Gox2181 was demonstrated to be NAD(H)-dependent and active towards a wide range of substrates, including sugar alcohols, secondary alcohols, ketones, and ketoses. Among the substrates tested, Gox2181 displayed preference for secondary hydroxyl or carbonyl groups, showing low K m values with d-arabitol and butanedione. © 2011 Elsevier Inc..
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1016/j.bbrc.2011.10.083
dc.sourceScopus
dc.subjectCrystal structure
dc.subjectGluconobacter oxydans
dc.subjectGox2181
dc.subjectSDR enzyme
dc.subjectSubstrate spectrum
dc.typeArticle
dc.contributor.departmentBIOLOGICAL SCIENCES
dc.description.doi10.1016/j.bbrc.2011.10.083
dc.description.sourcetitleBiochemical and Biophysical Research Communications
dc.description.volume415
dc.description.issue2
dc.description.page410-415
dc.description.codenBBRCA
dc.identifier.isiut000297534800036
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