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卤醇脱卤酶的研究进展

Advances on halohydrin dehalogenases
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摘要 卤醇脱卤酶(halohydrin dehalogenases,HHDHs)是微生物代谢卤代醇的重要酶类,它既能催化邻卤代醇脱卤成环又能催化逆反应环氧化物开环。近年来,通过基于数据库的基因挖掘,HHDHs酶家族扩增至70多种,亚类也由A类发展至G类。通过酶表征,发现酶的底物范围不一,而且酶活力、稳定性以及立体选择性难以满足工业生产需求,通过分子改造改善了酶的性能,拓展了HHDHs在生物催化方面的应用。本文综述了近年来HHDHs的结构机制、来源分布、酶分子改造以及催化应用等方面的研究。 Halohydrin dehalogenases(HHDHs)are important enzymes involved in the metabolism of halohydrins in microorganisms,and they can catalyze the removal of a halide ion and a proton from a vicinal halo alcohol with formation of an epoxide ring and epoxide ring opening reaction.In recent years,the number of HHDHs has been expanded to more than 70 and subtybes have also been developed from A-type to G-type by database-based gene mining.The characterization of novel HHDHs reveals that their substrate ranges are different,and the enzyme activity,stability and stereo-selectivity are difficult to meet the industrial production requirements.The performances of HHDHs are improved by molecular modification and their application are expanded.This review highlights the structure and mechanism,source distribution,molecular modification and catalytic applications the of halohydrin dehalogenase.
作者 王龙兴 贾红华 韦萍 WANG Longxing;JIA Honghua;WEI Ping(College of Biotechnology and Pharmaceutical Engineering,Nanjing Tech University,Nanjing 211800,China)
出处 《生物加工过程》 CAS 2021年第5期505-513,共9页 Chinese Journal of Bioprocess Engineering
基金 国家自然科学基金面上项目(21878155)。
关键词 卤醇脱卤酶 环氧化物 稳定性 立体选择性 分子改造 halohydrin dehalogenases epoxide stability stereo-selectivity molecular modification
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