The Key Laboratory of Industrial Biotechnology, Ministry of Education, School of Biotechnology, Jiangnan University, Wuxi, Jiangsu, China.
College of Life Sciences, Northwest University, Xi'an, Shanxi, China.
Biotechnol Appl Biochem. 2022 Dec;69(6):2530-2539. doi: 10.1002/bab.2302. Epub 2021 Dec 24.
A novel short-chain alcohol dehydrogenase from Tarenaya hassleriana labeled as putative tropinone reductase was heterologously expressed in Escherichia coli. Purified recombinant protein had molecular weight of approximately 30 kDa on 12% sodium dodecyl sulfate-polyacrylamide gel electrophoresis. T. hassleriana tropinone reductase-like enzyme (ThTRL) had not detected oxidative activity. The optimum pH for enzyme activity of ThTRL was weakly acidic (pH 5.0). 50°C was the optimum temperature for ThTRL. The highest catalytic efficiency and substrate affinity for recombinant ThTRL were observed with (+)-camphorquinone (k /K = 814.3 s mM , K = 44.25 μM). ThTRL exhibited a broad substrate specificity and reduced various carbonyl compounds, including small lipophilic aldehydes and ketones, terpene ketones, and their structural analogs.
从垂果堇菜中鉴定出的一种新型短链醇脱氢酶，被标记为可能的托品酮还原酶，在大肠杆菌中异源表达。纯化的重组蛋白在 12%十二烷基硫酸钠-聚丙烯酰胺凝胶电泳中分子量约为 30 kDa。垂果堇菜托品酮还原酶样酶（ThTRL）未检测到氧化活性。ThTRL 的最适 pH 值为弱酸性（pH 5.0）。50°C 是 ThTRL 的最适温度。重组 ThTRL 的最高催化效率和底物亲和力是用 (+)-樟脑醌（k /K = 814.3 s mM，K = 44.25 μM）观察到的。ThTRL 表现出广泛的底物特异性，并还原各种羰基化合物，包括小疏水性醛和酮、萜烯酮及其结构类似物。
