© WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
July 03, 2015
Very Important Paper: Expanding the Imine Reductase Toolbox by Exploring the Bacterial Protein-Sequence Space
Dennis Wetzl, Marco Berrera, Nicolas Sandon, Dan Fishlock, Martin Ebeling, Michael Müller, Steven Hanlon, Beat Wirz, Hans Iding*
Recent investigations on imine reductases (IREDs) have enriched the toolbox of potential catalysts accessing chiral amines. Now, H. Iding and co-workers (F. Hoffmann-La Roche, Switzerland) describe the characterization of 20 new IREDs, which were identified by using a C-terminal domain clustering of the bacterial protein-sequence space. Each of the enzymes was characterized against a set of nine cyclic imine model substrates. A refined clustering towards putative active-site residues was performed that was consistent with the current screen and previously reported results. Finally, preparative (100 mg scale) experiments with two purified IREDs, IR_20 from Streptomyces tsukubaensis and IR_23 from Streptomyces vidiochromogenes, were carried out.
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