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).

中文翻译：

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封面功能：切换亚胺还原酶的辅因子特异性（ChemCatChem 1/2018）

覆盖特征显示了亚胺还原酶的辅因子特异性从NADPH到NADH的转换。N. Borlinghaus和B.M. Nestl在其论文全文中证明，通过应用CSR-SALAD（一种用于工程化酶促烟酰胺辅因子偏爱的工具），并通过进一步的氨基酸取代来扩大突变体文库，可以从粘球菌中获得亚胺还原酶的NAPDH辅酶偏爱。stipitatus可以被设计。烟酰胺结合口袋的诱变导致特异性反转和活性恢复的变体。可以在2018年第1期的N.Borlinghaus和B.M.Nestl的第183页的全文中找到更多信息（DOI：10.1002 / cctc.201701194）。