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一种新型嵌合胺脱氢酶与亲本酶相比表现出改变的底物特异性。

A novel chimeric amine dehydrogenase shows altered substrate specificity compared to its parent enzymes.

机构信息

Georgia Institute of Technology, School of Chemical & Biomolecular Engineering, Parker H. Petit Building, 315 Ferst Drive, Atlanta, GA 30332-0100, USA.

出版信息

Chem Commun (Camb). 2014 Dec 11;50(95):14953-5. doi: 10.1039/c4cc06527a.

DOI:10.1039/c4cc06527a
PMID:25347124
Abstract

We created a novel chimeric amine dehydrogenase (AmDH) via domain shuffling of two parent AmDHs ('L- and F-AmDH'), which in turn had been generated from leucine and phenylalanine DH, respectively. Unlike the parent proteins, the chimeric AmDH ('cFL-AmDH') catalyzes the amination of acetophenone to (R)-methylbenzylamine and adamantylmethylketone to adamantylethylamine.

摘要

我们通过对两个亲本胺脱氢酶('L-和 F-AmDH')的结构域改组创建了一种新型嵌合胺脱氢酶(AmDH),这两个亲本酶分别来自亮氨酸和苯丙氨酸脱氢酶。与亲本蛋白不同,嵌合胺脱氢酶('cFL-AmDH')可催化苯乙酮氨化为(R)-甲基苄基胺和金刚烷甲基酮为金刚烷乙基胺。

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