ChemBioChem

Cover image for Vol. 15 Issue 12

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, 2014

Very Important Paper: Computational Library Design for Increasing Haloalkane Dehalogenase Stability

Robert J. Floor, Hein J. Wijma, Dana I. Colpa, Aline Ramos-Silva, Peter A. Jekel, Wiktor Szymański, Ben L. Feringa, Siewert J. Marrink, Dick B. Janssen*

Enzyme stability is of key importance for the development of biocatalytic processes. A new strategy termed "framework for rapid enzyme stabilization by computation" (FRESCO) was applied by Dick B. Janssen (University of Groningen, The Netherlands) and co-workers towards stabilizing the enzyme, haloalkane dehalogenase. Using computational design methods, a small mutant library was obtained from which a set of stabilizing mutations were discovered. The best mutations were combined, providing an enzyme that was more thermostable and resistant to high concentrations of organic co-solvent. The latter made it possible to use this enzyme for dehalogenation and kinetic resolution of hydrophobic substrates that are only highly soluble in the presence of organic co-solvents.

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    Article first published online: 27 AUG 2014 | DOI: 10.1002/cbic.201402213

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    Let's transfer hydrides to imines. Biocatalytic preparation of chiral amines by imine reductases is an emerging technology but is limited to few described enzymes. Several hundred additional enantiocomplementary imine reductases sequences were collected in a database, and the biochemical potentials of three of them are reported. Site-directed mutagenesis revealed key amino acid residues for catalysis and stereoselectivity.

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