近平滑假丝酵母CCTCC M203011是一株高效转化手性苯乙二醇，具有自主知识产权的优良菌株。立体选择性氧化还原酶RCR和SCR催化底物2-羟基苯乙酮，产生不同空间对映性的产物(R)-和(S)-苯乙二醇。前期研究表明关键氨基酸位点突变直接影响SCR酶的催化功能和产物空间对映性(Protein Sci 17(2008)1412-23；Appl Environ Microbiol 75(2009)2176-83；Bioresour Technol 102 (2011)483-89)。本研究在此基础上，拟通过测定酶/底物（辅酶/产物）复合物的三维结构，从底物分子手性中心相邻基团的不对称定位出发，认识关键氨基酸位点与底物的对映体选择性识别以及酶与底物/产物的相互作用，揭示手性识别的分子催化机制，为理性设计酶分子活性中心和底物分子功能基团的空间结构，强化酶的催化性能或引入新的催化特性提供理论指导。

Candida parapsilosis CCTCC M203011 is an excellent strain for chiral alcohol production with independent intellectual property rights. Stereoselective redox enzymes RCR and SCR catalyze 2-hydroxyacetophenone to (R)- and (S)-1-phenyl-1,2-ethanediol. It was reported that the mutations of the key amino acid sites directly influence the catalytic function and product stereoselectivity of SCR enzyme (Protein Sci 17 (2008) 1412-23, Appl Environ Microbiol 75 (2009) 2176-83; Bioresour Technol 102 (2011) 483-89). Based on the above results, this project focus on understanding the stereo-recognition between the key amino acids of enzyme and substrate, and the interaction between the enzymes and substrate/product through the determination the three dimensional structures of enzyme/substrate (coenzyme/product) complex. From the asymmetric positioning of adjacent groups in the chiral center of substrate, we will reveal the molecular catalytic mechanism of stereo-cognition for rationally designing the molecular activity center of enzymes and the structure of function group of substrate, and provide theoretical guidance for strengthening the enzyme catalytic performance or introducing some new catalytic properties.