文献类型：期刊文献

英文题名：Biochemical and structural analysis of Gox2181, a new member of the SDR superfamily from Gluconobacter oxydans

作者：Liu, Xu[1];Yuan, Zuanning[2];Yuan, Y. Adam[2];Lin, Jinping[1];Wei, Dongzhi[1]

机构：[1]E China Univ Sci & Technol, State Key Lab Bioreactor Engn, NewWorld Inst Biotechnol, Shanghai 200237, Peoples R China;[2]Natl Univ Singapore, Dept Biol Sci, Singapore 117543, Singapore

年份：2011

卷号：415

期号：2

起止页码：410

外文期刊名：BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS

收录：;WOS:【SCI-EXPANDED(收录号:WOS:000297534800036)】；

语种：英文

外文关键词：Gluconobacter oxydans; Gox2181; SDR enzyme; Substrate spectrum; Crystal structure

摘要：Gluconobacter 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 1.8 angstrom. Gox2181 formed a homo-tetramer in the crystal that was coincident with the apparent molecular mass determined in the solution. Gox2181 displayed alpha/beta-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. (C) 2011 Elsevier Inc. All rights reserved.