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Cover Feature: Switching the Cofactor Specificity of an Imine Reductase (ChemCatChem 1/2018)
Author(s) -
Borlinghaus Niels,
Nestl Bettina M.
Publication year - 2018
Publication title -
chemcatchem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.497
H-Index - 106
eISSN - 1867-3899
pISSN - 1867-3880
DOI - 10.1002/cctc.201701983
Subject(s) - cofactor , mutagenesis , imine , reductase , chemistry , nicotinamide , stereochemistry , enzyme , biochemistry , mutant , gene , catalysis
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).