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Quarter of a Century after: A Glimpse at the Conformation and Mechanism of Candida antarctica Lipase B
Crystals ( IF 2.7 ) Pub Date : 2020-05-16 , DOI: 10.3390/cryst10050404
Jarosław Błaszczyk , Piotr Kiełbasiński

Lipase B from Candida antarctica (CAL-B) belongs to the family of α/β-hydrolases, and is one from the most extensively used biocatalysts in the kinetic resolution of amines and alcohols in a racemic state, in the desymmetrization of diacetates or diols, and in the stereoselective synthesis of chiral intermediate compounds for obtaining the various pharmaceuticals and agents which protect plants. There are also many cases of promiscuous reactions catalyzed by CAL-B. The number of very important results appeared recently in the literature in the years 2015–2019, regarding the crystal structure and conformation of CAL-B molecule. Before 2015, there was a long period of a complete lack of information concerning this enzyme’s structure. The earlier reports about CAL-B structure were dated between 1994–1995, and did not provide enough conclusions about the mechanism of the enzyme. The recently solved structures give a hint of the enzyme mechanism in three dimensions.

中文翻译:

四分之一世纪之后:南极假丝酵母脂肪酶B的形成及其机制的一瞥

南极假丝酵母的脂肪酶B(CAL-B)属于α/β-水解酶家族,是在消旋状态下胺和醇的动力学拆分,双乙酸酯或二醇的去对称化以及立体选择性方面最广泛使用的生物催化剂之一合成手性中间体化合物以获得保护植物的各种药物和试剂。CAL-B催化的混杂反应也有很多情况。关于CAL-B分子的晶体结构和构象,最近非常重要的结果出现在2015-2019年的文献中。在2015年之前,长期以来完全缺乏有关该酶结构的信息。关于CAL-B结构的早期报道是在1994年至1995年之间,尚未提供有关该酶机制的足够结论。
更新日期:2020-05-16
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