Absolute configuration of a chiral CHD group via neutron diffraction: confirmation of the absolute stereochemistry of the enzymatic formation of malic acid

doi:https://doi.org/10.1016/S0006-291X(83)80041-2

Title: Absolute configuration of a chiral CHD group via neutron diffraction: confirmation of the absolute stereochemistry of the enzymatic formation of malic acid

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Abstract

Neutron diffraction has been used to monitor the absolute stereochemistry of an enzymatic reaction. (-)(2S)malic-3-d acid was prepared by the action of fumarase on fumaric acid in D/sub 2/O. After a large number of cations were screened, it was found that (+)(R)..cap alpha..-phenylethylamine forms the large crystals necessary for a neutron diffraction analysis. The subsequent structure determination showed that (+)(R)..cap alpha..-phenylethylammonium (-)(2S)malate-3-d has an absolute configuration of R at the CHD site. This result confirms the absolute stereochemistry of fumarate-to-malate transformation as catalyzed by the enzyme fumarase.

Authors:: Bau, R; Brewer, I; Chiang, M Y; Fujita, S; Hoffman, J; Watkins, M I; Koetzle, T F

Publication Date:: 1983-09-30

Research Org.:: Univ. of Southern California, Los Angeles

OSTI Identifier:: 5152030

Resource Type:: Journal Article

Journal Name:: Biochem. Biophys. Res. Commun.; (United States)

Additional Journal Information:: Journal Volume: 115:3

Country of Publication:: United States

Language:: English

Subject:: 59 BASIC BIOLOGICAL SCIENCES; HYDRO-LYASES; BIOCHEMICAL REACTION KINETICS; STEREOCHEMISTRY; MALIC ACID; CRYSTALLIZATION; DERIVATIZATION; NEUTRON DIFFRACTION; AMINES; FUMARIC ACID; HEAVY WATER; KREBS CYCLE; LABELLING; CARBON-OXYGEN LYASES; CARBOXYLIC ACIDS; CHEMICAL REACTIONS; COHERENT SCATTERING; DICARBOXYLIC ACIDS; DIFFRACTION; ENZYMES; HYDROGEN COMPOUNDS; HYDROXY ACIDS; KINETICS; LYASES; ORGANIC ACIDS; ORGANIC COMPOUNDS; OXYGEN COMPOUNDS; PHASE TRANSFORMATIONS; REACTION KINETICS; SCATTERING; WATER; 550200* - Biochemistry

Citation Formats


                    Bau, R, Brewer, I, Chiang, M Y, Fujita, S, Hoffman, J, Watkins, M I, and Koetzle, T F. Absolute configuration of a chiral CHD group via neutron diffraction: confirmation of the absolute stereochemistry of the enzymatic formation of malic acid.  United States: N. p., 1983. 
        Web.  doi:10.1016/S0006-291X(83)80041-2.

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                    Bau, R, Brewer, I, Chiang, M Y, Fujita, S, Hoffman, J, Watkins, M I, & Koetzle, T F. Absolute configuration of a chiral CHD group via neutron diffraction: confirmation of the absolute stereochemistry of the enzymatic formation of malic acid.  United States.  https://doi.org/10.1016/S0006-291X(83)80041-2

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                    Bau, R, Brewer, I, Chiang, M Y, Fujita, S, Hoffman, J, Watkins, M I, and Koetzle, T F. Fri .  
        "Absolute configuration of a chiral CHD group via neutron diffraction: confirmation of the absolute stereochemistry of the enzymatic formation of malic acid".  United States.  https://doi.org/10.1016/S0006-291X(83)80041-2.

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@article{osti_5152030,

  title        = {Absolute configuration of a chiral CHD group via neutron diffraction: confirmation of the absolute stereochemistry of the enzymatic formation of malic acid},

  author       = {Bau, R and Brewer, I and Chiang, M Y and Fujita, S and Hoffman, J and Watkins, M I and Koetzle, T F},

  abstractNote = {Neutron diffraction has been used to monitor the absolute stereochemistry of an enzymatic reaction. (-)(2S)malic-3-d acid was prepared by the action of fumarase on fumaric acid in D/sub 2/O. After a large number of cations were screened, it was found that (+)(R)..cap alpha..-phenylethylamine forms the large crystals necessary for a neutron diffraction analysis. The subsequent structure determination showed that (+)(R)..cap alpha..-phenylethylammonium (-)(2S)malate-3-d has an absolute configuration of R at the CHD site. This result confirms the absolute stereochemistry of fumarate-to-malate transformation as catalyzed by the enzyme fumarase.},

  doi          = {10.1016/S0006-291X(83)80041-2},

  url          = {https://www.osti.gov/biblio/5152030},
  journal      = {Biochem. Biophys. Res. Commun.; (United States)},
number       = ,

  volume       = 115:3,

  place        = {United States},

  year         = {1983},

  month        = {9}

}

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https://doi.org/10.1016/S0006-291X(83)80041-2

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