腈水合酶
热稳定性
红球菌
烟酰胺
化学
饱和突变
腈
丙烯酰胺
基质(水族馆)
组合化学
蛋白质工程
活动站点
残留物(化学)
立体化学
酶
有机化学
生物化学
突变体
单体
红球菌
生物
聚合物
基因
生态学
作者
Yuanyuan Xia,Meng Yin,Łukasz Pepłowski,Zhongyi Cheng,Zhemin Zhou
标识
DOI:10.1002/slct.202201941
摘要
Abstract Nicotinamide is a high‐value chemical that has been widely applied in various aspects of daily life. Nitrile hydratase (NHase) is capable of carrying out biotransformation of nitriles to amides and has shown great potential in the green synthesis of nicotinamide. The high‐molecular mass NHase (H‐NHase) from Rhodococcus rhodochrous J1 has been applied in the industrial‐scale production of acrylamide; however, its activity is not ideal towards aromatic 3‐cyanopyridines, resulting in its substrate preference towards aliphatic nitriles. In this study, a hinge residue at the entrance of the substrate access tunnel of H‐NHase was identified through substrate access tunnel calculations, site‐saturation mutagenesis, molecular docking and molecular dynamics simulations. The corresponding mutant βW48Y showed a 5.9‐fold higher specific activity towards 3‐cyanopyridine than that of its parental enzyme, with better thermostability, proving itself to be a competitive candidate for the industrial production of nicotinamide.
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