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The Substrate Spectra of Pentaerythritol Tetranitrate Reductase, Morphinone Reductase, N-Ethylmaleimide Reductase and Estrogen-Binding Protein in the Asymmetric Bioreduction of Activated Alkenes
Article first published online: 9 FEB 2010
DOI: 10.1002/adsc.200900832
Copyright © 2010 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
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How to Cite
Mueller, Nicole J., Stueckler, C., Hauer, B., Baudendistel, N., Housden, H., Bruce, Neil C. and Faber, K. (2010), The Substrate Spectra of Pentaerythritol Tetranitrate Reductase, Morphinone Reductase, N-Ethylmaleimide Reductase and Estrogen-Binding Protein in the Asymmetric Bioreduction of Activated Alkenes. Adv. Synth. Catal., 352: 387–394. doi: 10.1002/adsc.200900832
Publication History
- Issue published online: 17 FEB 2010
- Article first published online: 9 FEB 2010
- Manuscript Revised: 13 JAN 2010
- Manuscript Received: 30 NOV 2009
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Keywords:
- alkene bioreduction;
- biotransformations;
- enoate reductase;
- estrogen-binding protein;
- morphinone reductase;
- NEM reductase;
- PETN reductase
Abstract
Four flavoproteins from the old yellow enzyme (OYE) family, pentaerythritol tetranitrate (PETNR) reductase, N-ethylmaleimide reductase (NEMR), morphinone reductase (MorR) and estrogen-binding protein (EBP1), exhibited a broad substrate tolerance by accepting conjugated enals, enones, imides, dicarboxylic acids and esters, as well as a nitroalkene and therefore can be employed for the asymmetric bioreduction of carbon-carbon double (C![[DOUBLE BOND]](http://onlinelibrarystatic.wiley.com/undisplayable_characters/00f8fe.gif)
C) bonds. In particular, morphinone reductase and estrogen-binding protein often showed a complementary stereochemical preference in comparison to that of previously investigated OYEs.