辅因子
突变
亚胺
还原酶
化学
烟酰胺
立体化学
酶
生物化学
突变体
基因
催化作用
作者
Niels Borlinghaus,Bettina M. Nestl
出处
期刊:Chemcatchem
[Wiley]
日期:2018-01-09
卷期号:10 (1): 3-3
标识
DOI:10.1002/cctc.201701983
摘要
The Cover Feature shows the switch of the cofactor specificity of an imine reductase from NADPH to NADH. In their Full Paper, N. Borlinghaus and B. M. Nestl demonstrate that by applying the CSR-SALAD, a tool for engineering enzymatic nicotinamide cofactor preference, and enlarging the mutant library by further amino acid substitutions, the NAPDH coenzyme preference of the imine reductase from Myxococcus stipitatus can be engineered. The mutagenesis of the nicotinamide binding pocket resulted in variants with reversed specificity and recovered activity. More information can be found in the Full Paper by N. Borlinghaus and B. M. Nestl on page 183 in Issue 1, 2018 (DOI: 10.1002/cctc.201701194).
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