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Kurt Faber - One of the best experts on this subject based on the ideXlab platform.
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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
Advanced Synthesis & Catalysis, 2010Co-Authors: Nicole J. Mueller, Clemens Stueckler, Bernhard Hauer, Nina Baudendistel, Hazel R. Housden, Neil C. Bruce, Kurt FaberAbstract: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=C) bonds. In particular, morphinone reductase and Estrogen-Binding protein often showed a complementary stereochemical preference in comparison to that of previously investigated OYEs.
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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
Advanced Synthesis & Catalysis, 2010Co-Authors: Nicole J. Mueller, Clemens Stueckler, Bernhard Hauer, Nina Baudendistel, Hazel R. Housden, Neil C. Bruce, Kurt FaberAbstract: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=C) bonds. In particular, morphinone reductase and Estrogen-Binding protein often showed a complementary stereochemical preference in comparison to that of previously investigated OYEs.
Nicole J. Mueller - One of the best experts on this subject based on the ideXlab platform.
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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
Advanced Synthesis & Catalysis, 2010Co-Authors: Nicole J. Mueller, Clemens Stueckler, Bernhard Hauer, Nina Baudendistel, Hazel R. Housden, Neil C. Bruce, Kurt FaberAbstract: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=C) bonds. In particular, morphinone reductase and Estrogen-Binding protein often showed a complementary stereochemical preference in comparison to that of previously investigated OYEs.
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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
Advanced Synthesis & Catalysis, 2010Co-Authors: Nicole J. Mueller, Clemens Stueckler, Bernhard Hauer, Nina Baudendistel, Hazel R. Housden, Neil C. Bruce, Kurt FaberAbstract: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=C) bonds. In particular, morphinone reductase and Estrogen-Binding protein often showed a complementary stereochemical preference in comparison to that of previously investigated OYEs.
Neil C. Bruce - One of the best experts on this subject based on the ideXlab platform.
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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
Advanced Synthesis & Catalysis, 2010Co-Authors: Nicole J. Mueller, Clemens Stueckler, Bernhard Hauer, Nina Baudendistel, Hazel R. Housden, Neil C. Bruce, Kurt FaberAbstract: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=C) bonds. In particular, morphinone reductase and Estrogen-Binding protein often showed a complementary stereochemical preference in comparison to that of previously investigated OYEs.
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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
Advanced Synthesis & Catalysis, 2010Co-Authors: Nicole J. Mueller, Clemens Stueckler, Bernhard Hauer, Nina Baudendistel, Hazel R. Housden, Neil C. Bruce, Kurt FaberAbstract: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=C) bonds. In particular, morphinone reductase and Estrogen-Binding protein often showed a complementary stereochemical preference in comparison to that of previously investigated OYEs.
Hazel R. Housden - One of the best experts on this subject based on the ideXlab platform.
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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
Advanced Synthesis & Catalysis, 2010Co-Authors: Nicole J. Mueller, Clemens Stueckler, Bernhard Hauer, Nina Baudendistel, Hazel R. Housden, Neil C. Bruce, Kurt FaberAbstract: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=C) bonds. In particular, morphinone reductase and Estrogen-Binding protein often showed a complementary stereochemical preference in comparison to that of previously investigated OYEs.
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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
Advanced Synthesis & Catalysis, 2010Co-Authors: Nicole J. Mueller, Clemens Stueckler, Bernhard Hauer, Nina Baudendistel, Hazel R. Housden, Neil C. Bruce, Kurt FaberAbstract: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=C) bonds. In particular, morphinone reductase and Estrogen-Binding protein often showed a complementary stereochemical preference in comparison to that of previously investigated OYEs.
Nina Baudendistel - One of the best experts on this subject based on the ideXlab platform.
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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
Advanced Synthesis & Catalysis, 2010Co-Authors: Nicole J. Mueller, Clemens Stueckler, Bernhard Hauer, Nina Baudendistel, Hazel R. Housden, Neil C. Bruce, Kurt FaberAbstract: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=C) bonds. In particular, morphinone reductase and Estrogen-Binding protein often showed a complementary stereochemical preference in comparison to that of previously investigated OYEs.
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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
Advanced Synthesis & Catalysis, 2010Co-Authors: Nicole J. Mueller, Clemens Stueckler, Bernhard Hauer, Nina Baudendistel, Hazel R. Housden, Neil C. Bruce, Kurt FaberAbstract: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=C) bonds. In particular, morphinone reductase and Estrogen-Binding protein often showed a complementary stereochemical preference in comparison to that of previously investigated OYEs.