An enzymatic route to selenazolines

Koehnke, J. et al. (2013) An enzymatic route to selenazolines. ChemBioChem, 14(5), pp. 564-567. (doi: 10.1002/cbic.201300037) (PMID:23483642) (PMCID:PMC3625746)

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Abstract

Ringing the changes: Selenazolines have applications in medicinal chemistry, but their synthesis is challenging. We report a new convenient and less toxic route to these heterocycles that starts from commercially available selenocysteine. The new route depends on a heterocyclase enzyme that creates oxazolines and thiazolines from serines/threonines and cysteines.

Item Type:Articles
Status:Published
Refereed:Yes
Glasgow Author(s) Enlighten ID:Koehnke, Professor Jesko
Authors: Koehnke, J., Morawitz, F., Bent, A. F., Houssen, W. E., Shirran, S. L., Fuszard, M. A., Smellie, I. A., Botting, C. H., Smith, M. C. M., Jaspars, M., and Naismith, J. H.
College/School:College of Science and Engineering > School of Chemistry
Journal Name:ChemBioChem
Publisher:Wiley-VCH Verlag
ISSN:1439-4227
ISSN (Online):1439-7633

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