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Alcohol Dehydrogenase

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Liliane Gorrichon – One of the best experts on this subject based on the ideXlab platform.

  • A molecular model for cinnamyl Alcohol Dehydrogenase, a plant aromatic Alcohol Dehydrogenase involved in lignification
    Biochimica et Biophysica Acta, 1993
    Co-Authors: James H. Mckie, Rabih Jaouhari, Kenneth T. Douglas, Deborah Goffner, Catherine Feuillet, Jacqueline Grima-pettenati, Alain M. Boudet, Michel Baltas, Liliane Gorrichon

    Abstract:

    Abstract The plant aromatic Alcohol Dehydrogenase, cinnamyl Alcohol Dehydrogenase (CAD2 from Eucalyptus ) was found by sequence analysis of its cloned gene to be homolgous to a range of Dehydrogenases including Alcohol Dehydrogenases, l -threonine-3-Dehydrogenase, d -xylose reductase and sorbitol Dehydrogenase. A homology model of CAD2 was built using the X-ray crystallographic coordinates of horse-liver Alcohol dhydrogenase to provide the template, with additional input from other analogous regions of structure from similar enzymes where necessary. The structural model thus produced rationalised the Zn-binding properties of CAD2, indicated the possession of a Rossmann fold (GXGXXG motif), and explained the class A stereospecificity (pro-R hydrogen removal from substrate Alcohol) and aromatic substrate specificity of the enzyme. A range of potential ligands wasdesigned based on the homology model and tested as inhibitors of CAD2 and horse liver Alcohol Dehydrogenase.

  • A molecular model for cinnamyl Alcohol Dehydrogenase, a plant aromatic Alcohol Dehydrogenase involved in lignification
    Biochimica et biophysica acta, 1993
    Co-Authors: James H. Mckie, Rabih Jaouhari, Kenneth T. Douglas, Deborah Goffner, Catherine Feuillet, Jacqueline Grima-pettenati, Alain M. Boudet, Michel Baltas, Liliane Gorrichon

    Abstract:

    The plant aromatic Alcohol Dehydrogenase, cinnamyl Alcohol Dehydrogenase (CAD2 from Eucalyptus) was found by sequence analysis of its cloned gene to be homologous to a range of Dehydrogenases including Alcohol Dehydrogenases, L-threonine-3-Dehydrogenase, D-xylose reductase and sorbitol Dehydrogenase. A homology model of CAD2 was built using the X-ray crystallographic coordinates of horse-liver Alcohol Dehydrogenase to provide the template, with additional modelling input from other analogous regions of structure from similar enzymes where necessary. The structural model thus produced rationalised the Zn-binding properties of CAD2, indicated the possession of a Rossmann fold (GXGXXG motif), and explained the class A stereospecificity (pro-R hydrogen removal from substrate Alcohol) and aromatic substrate specificity of the enzyme. A range of potential ligands was designed based on the homology model and tested as inhibitors of CAD2 and horse liver Alcohol Dehydrogenase.

James H. Mckie – One of the best experts on this subject based on the ideXlab platform.

  • A molecular model for cinnamyl Alcohol Dehydrogenase, a plant aromatic Alcohol Dehydrogenase involved in lignification
    Biochimica et Biophysica Acta, 1993
    Co-Authors: James H. Mckie, Rabih Jaouhari, Kenneth T. Douglas, Deborah Goffner, Catherine Feuillet, Jacqueline Grima-pettenati, Alain M. Boudet, Michel Baltas, Liliane Gorrichon

    Abstract:

    Abstract The plant aromatic Alcohol Dehydrogenase, cinnamyl Alcohol Dehydrogenase (CAD2 from Eucalyptus ) was found by sequence analysis of its cloned gene to be homolgous to a range of Dehydrogenases including Alcohol Dehydrogenases, l -threonine-3-Dehydrogenase, d -xylose reductase and sorbitol Dehydrogenase. A homology model of CAD2 was built using the X-ray crystallographic coordinates of horse-liver Alcohol dhydrogenase to provide the template, with additional input from other analogous regions of structure from similar enzymes where necessary. The structural model thus produced rationalised the Zn-binding properties of CAD2, indicated the possession of a Rossmann fold (GXGXXG motif), and explained the class A stereospecificity (pro-R hydrogen removal from substrate Alcohol) and aromatic substrate specificity of the enzyme. A range of potential ligands wasdesigned based on the homology model and tested as inhibitors of CAD2 and horse liver Alcohol Dehydrogenase.

  • A molecular model for cinnamyl Alcohol Dehydrogenase, a plant aromatic Alcohol Dehydrogenase involved in lignification
    Biochimica et biophysica acta, 1993
    Co-Authors: James H. Mckie, Rabih Jaouhari, Kenneth T. Douglas, Deborah Goffner, Catherine Feuillet, Jacqueline Grima-pettenati, Alain M. Boudet, Michel Baltas, Liliane Gorrichon

    Abstract:

    The plant aromatic Alcohol Dehydrogenase, cinnamyl Alcohol Dehydrogenase (CAD2 from Eucalyptus) was found by sequence analysis of its cloned gene to be homologous to a range of Dehydrogenases including Alcohol Dehydrogenases, L-threonine-3-Dehydrogenase, D-xylose reductase and sorbitol Dehydrogenase. A homology model of CAD2 was built using the X-ray crystallographic coordinates of horse-liver Alcohol Dehydrogenase to provide the template, with additional modelling input from other analogous regions of structure from similar enzymes where necessary. The structural model thus produced rationalised the Zn-binding properties of CAD2, indicated the possession of a Rossmann fold (GXGXXG motif), and explained the class A stereospecificity (pro-R hydrogen removal from substrate Alcohol) and aromatic substrate specificity of the enzyme. A range of potential ligands was designed based on the homology model and tested as inhibitors of CAD2 and horse liver Alcohol Dehydrogenase.

Deborah Goffner – One of the best experts on this subject based on the ideXlab platform.

  • A molecular model for cinnamyl Alcohol Dehydrogenase, a plant aromatic Alcohol Dehydrogenase involved in lignification
    Biochimica et Biophysica Acta, 1993
    Co-Authors: James H. Mckie, Rabih Jaouhari, Kenneth T. Douglas, Deborah Goffner, Catherine Feuillet, Jacqueline Grima-pettenati, Alain M. Boudet, Michel Baltas, Liliane Gorrichon

    Abstract:

    Abstract The plant aromatic Alcohol Dehydrogenase, cinnamyl Alcohol Dehydrogenase (CAD2 from Eucalyptus ) was found by sequence analysis of its cloned gene to be homolgous to a range of Dehydrogenases including Alcohol Dehydrogenases, l -threonine-3-Dehydrogenase, d -xylose reductase and sorbitol Dehydrogenase. A homology model of CAD2 was built using the X-ray crystallographic coordinates of horse-liver Alcohol dhydrogenase to provide the template, with additional input from other analogous regions of structure from similar enzymes where necessary. The structural model thus produced rationalised the Zn-binding properties of CAD2, indicated the possession of a Rossmann fold (GXGXXG motif), and explained the class A stereospecificity (pro-R hydrogen removal from substrate Alcohol) and aromatic substrate specificity of the enzyme. A range of potential ligands wasdesigned based on the homology model and tested as inhibitors of CAD2 and horse liver Alcohol Dehydrogenase.

  • A molecular model for cinnamyl Alcohol Dehydrogenase, a plant aromatic Alcohol Dehydrogenase involved in lignification
    Biochimica et biophysica acta, 1993
    Co-Authors: James H. Mckie, Rabih Jaouhari, Kenneth T. Douglas, Deborah Goffner, Catherine Feuillet, Jacqueline Grima-pettenati, Alain M. Boudet, Michel Baltas, Liliane Gorrichon

    Abstract:

    The plant aromatic Alcohol Dehydrogenase, cinnamyl Alcohol Dehydrogenase (CAD2 from Eucalyptus) was found by sequence analysis of its cloned gene to be homologous to a range of Dehydrogenases including Alcohol Dehydrogenases, L-threonine-3-Dehydrogenase, D-xylose reductase and sorbitol Dehydrogenase. A homology model of CAD2 was built using the X-ray crystallographic coordinates of horse-liver Alcohol Dehydrogenase to provide the template, with additional modelling input from other analogous regions of structure from similar enzymes where necessary. The structural model thus produced rationalised the Zn-binding properties of CAD2, indicated the possession of a Rossmann fold (GXGXXG motif), and explained the class A stereospecificity (pro-R hydrogen removal from substrate Alcohol) and aromatic substrate specificity of the enzyme. A range of potential ligands was designed based on the homology model and tested as inhibitors of CAD2 and horse liver Alcohol Dehydrogenase.