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

被引：84
作者：
Bommarius, Bettina R. [1 ]
Schuermann, Martin [2 ]
Bommarius, Andreas S. [1 ,3 ]
机构：
[1] Georgia Inst Technol, Sch Chem & Biomol Engn, Atlanta, GA 30332 USA
[2] DSM Innovat Synth BV, NL-6160 MD Geleen, Netherlands
[3] Georgia Inst Technol, Sch Chem & Biochem, Atlanta, GA 30332 USA
来源：
CHEMICAL COMMUNICATIONS | 2014年 / 50卷 / 95期
基金：
美国国家科学基金会;
关键词：
PHENYLALANINE DEHYDROGENASE; LEUCINE DEHYDROGENASE; CHIRAL AMINES; P450;
D O I：
10.1039/c4cc06527a
中图分类号：
O6 [化学];
学科分类号：
0703 ;
摘要：
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 adamantylmethylketoneto adamantylethylamine.
引用
收藏
页码：14953 / 14955
页数：3
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