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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

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JournalAdvanced Synthesis and Catalysis
DatePublished - 15 Feb 2010
Issue number2-3
Volume352
Number of pages8
Pages (from-to)387-394
Original languageEnglish

Abstract

Four flavoproteins from the old yellow enzyme (OYE) family, pentaerythritol tetranitrate (PETNR) reductase, N-ethylmalelimide reductase (NEMR), morphinone reductase (MorR) and estrogen-binding protein (EBPI), 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=C) bonds. In particular, morphinone reductase and estrogen-binding protein often showed a complementary stereochemical preference in comparison to that Of previously investigated OYEs.

    Research areas

  • alkene bioreduction, biotransformations, enoate reductase, estrogen-binding protein, morphinone reductase, NEM reductase, PETN reductase, OLD YELLOW ENZYME, ENOATE REDUCTASES, C=C-BONDS, CANDIDA-MACEDONIENSIS, CRYSTAL-STRUCTURE, BAKERS-YEAST, REDUCTIONS, FAMILY, BIOTRANSFORMATIONS, STEREOSELECTIVITY

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