The Substrate Spectra of Pentaerythritol Tetranitrate Reductase, Morphinone Reductase, N-Ethylmaleimide Reductase and Estrogen-Binding Protein in the Asymmetric Bioreduction of Activated Alkenes

Nicole J. Mueller; Clemens Stueckler; Bernhard Hauer; Nina Baudendistel; Hazel Housden; Neil C. Bruce; Kurt Faber

doi:10.1002/adsc.200900832

The Substrate Spectra of Pentaerythritol Tetranitrate Reductase, Morphinone Reductase, N-Ethylmaleimide Reductase and Estrogen-Binding Protein in the Asymmetric Bioreduction of Activated Alkenes

Nicole J. Mueller, Clemens Stueckler, Bernhard Hauer, Nina Baudendistel, Hazel Housden, Neil C. Bruce, Kurt Faber

CNAP

Research output: Contribution to journal › Article › peer-review

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.

Original language	English
Pages (from-to)	387-394
Number of pages	8
Journal	Advanced Synthesis and Catalysis
Volume	352
Issue number	2-3
DOIs	https://doi.org/10.1002/adsc.200900832
Publication status	Published - 15 Feb 2010

Keywords

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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10.1002/adsc.200900832

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Mueller, N. J., Stueckler, C., Hauer, B., Baudendistel, N., Housden, H., Bruce, N. C., & 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. Advanced Synthesis and Catalysis, 352(2-3), 387-394. https://doi.org/10.1002/adsc.200900832

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title = "The Substrate Spectra of Pentaerythritol Tetranitrate Reductase, Morphinone Reductase, N-Ethylmaleimide Reductase and Estrogen-Binding Protein in the Asymmetric Bioreduction of Activated Alkenes",

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.",

keywords = "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",

author = "Mueller, {Nicole J.} and Clemens Stueckler and Bernhard Hauer and Nina Baudendistel and Hazel Housden and Bruce, {Neil C.} and Kurt Faber",

year = "2010",

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day = "15",

doi = "10.1002/adsc.200900832",

language = "English",

volume = "352",

pages = "387--394",

journal = "Advanced Synthesis and Catalysis",

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Mueller, NJ, Stueckler, C, Hauer, B, Baudendistel, N, Housden, H , Bruce, NC & 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', Advanced Synthesis and Catalysis, vol. 352, no. 2-3, pp. 387-394. https://doi.org/10.1002/adsc.200900832

The Substrate Spectra of Pentaerythritol Tetranitrate Reductase, Morphinone Reductase, N-Ethylmaleimide Reductase and Estrogen-Binding Protein in the Asymmetric Bioreduction of Activated Alkenes. / Mueller, Nicole J.; Stueckler, Clemens; Hauer, Bernhard et al.
In: Advanced Synthesis and Catalysis, Vol. 352, No. 2-3, 15.02.2010, p. 387-394.

Research output: Contribution to journal › Article › peer-review

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AU - Mueller, Nicole J.

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KW - ENOATE REDUCTASES

KW - C=C-BONDS

KW - CANDIDA-MACEDONIENSIS

KW - CRYSTAL-STRUCTURE

KW - BAKERS-YEAST

KW - REDUCTIONS

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SN - 1615-4150

VL - 352

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EP - 394

JO - Advanced Synthesis and Catalysis

JF - Advanced Synthesis and Catalysis

IS - 2-3

ER -

The Substrate Spectra of Pentaerythritol Tetranitrate Reductase, Morphinone Reductase, N-Ethylmaleimide Reductase and Estrogen-Binding Protein in the Asymmetric Bioreduction of Activated Alkenes

Abstract

Keywords

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Advance optical waveguide biosensors for the detection of illicit drugs and explosives

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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

Abstract

Keywords

Access to Document

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Advance optical waveguide biosensors for the detection of illicit drugs and explosives

Cite this