Ellis Elizabeth M
Departments of Bioscience and Pharmaceutical Sciences, University of Strathclyde, 204 George Street, G1 1XW, Glasgow, UK.
FEMS Microbiol Lett. 2002 Nov 5;216(2):123-31. doi: 10.1111/j.1574-6968.2002.tb11425.x.
The aldo-keto reductases (AKR) are a superfamily of enzymes with diverse functions in the reduction of aldehydes and ketones. AKR enzymes are found in a wide range of microorganisms, and many open reading frames encoding related putative enzymes have been identified through genome sequencing projects. Established microbial members of the superfamily include the xylose reductases, 2,5-diketo-D-gluconic acid reductases and beta-keto ester reductases. The AKR enzymes share a common (alpha/beta)(8) structure, and conserved catalytic mechanism, although there is considerable variation in the substrate-binding pocket. The physiological function of many of these enzymes is unknown, but a variety of methods including gene disruptions, heterologous expression systems and expression profiling are being employed to deduce the roles of these enzymes in cell metabolism. Several microbial AKR are already being exploited in biotransformation reactions and there is potential for other novel members of this important superfamily to be identified, studied and utilized in this way.
醛酮还原酶（AKR）是一类在醛和酮还原反应中具有多种功能的酶超家族。AKR酶存在于多种微生物中，通过基因组测序项目已鉴定出许多编码相关假定酶的开放阅读框。该超家族已确定的微生物成员包括木糖还原酶、2,5-二酮-D-葡萄糖酸还原酶和β-酮酯还原酶。AKR酶具有共同的（α/β）8结构和保守的催化机制，尽管其底物结合口袋存在相当大的差异。这些酶中许多的生理功能尚不清楚，但目前正在采用多种方法，包括基因敲除、异源表达系统和表达谱分析，来推断这些酶在细胞代谢中的作用。几种微生物AKR已被用于生物转化反应，并且这个重要超家族的其他新成员有可能以这种方式被鉴定、研究和利用。
