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.
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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