Cover image for Vol. 16 Issue 11

Editor: Peter Gölitz; Editorial Board Chairs: Thomas Carell, Donald Hilvert, Barbara Imperiali

Online ISSN: 1439-7633

Associated Title(s): ChemCatChem, ChemMedChem, ChemPhysChem, ChemSusChem

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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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