A molecular model for cinnamyl alcohol dehydrogenase, a plant aromatic alcohol dehydrogenase involved in lignification

James H. McKie; Rabih Jaouhari; Kenneth T. Douglas; Deborah Goffner; Catherine Feuillet; Jacqueline Grima-Pettenati; Alain M. Boudet; Michel Baltas; Liliane Gorrichon

doi:10.1016/0167-4838(93)90063-W

A molecular model for cinnamyl alcohol dehydrogenase, a plant aromatic alcohol dehydrogenase involved in lignification

James H. McKie, Rabih Jaouhari, Kenneth T. Douglas^*, Deborah Goffner, Catherine Feuillet, Jacqueline Grima-Pettenati, Alain M. Boudet, Michel Baltas, Liliane Gorrichon

^*Corresponding author for this work

Pharmacy

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

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.

Original language	English
Pages (from-to)	61-69
Number of pages	9
Journal	Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular
Volume	1202
Issue number	1
DOIs	https://doi.org/10.1016/0167-4838(93)90063-W
Publication status	Published - 3 Sept 1993

Keywords

alcohol dehydrogenase
dehydrogenase
lignification
molecular modeling
sequence homology
structural model

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10.1016/0167-4838(93)90063-W

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McKie, J. H., Jaouhari, R., Douglas, K. T., Goffner, D., Feuillet, C., Grima-Pettenati, J., Boudet, A. M., Baltas, M., & Gorrichon, L. (1993). A molecular model for cinnamyl alcohol dehydrogenase, a plant aromatic alcohol dehydrogenase involved in lignification. Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular, 1202(1), 61-69. https://doi.org/10.1016/0167-4838(93)90063-W

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title = "A molecular model for cinnamyl alcohol dehydrogenase, a plant aromatic alcohol dehydrogenase involved in lignification",

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.",

keywords = "alcohol dehydrogenase, dehydrogenase, lignification, molecular modeling, sequence homology, structural model",

author = "McKie, {James H.} and Rabih Jaouhari and Douglas, {Kenneth T.} and Deborah Goffner and Catherine Feuillet and Jacqueline Grima-Pettenati and Boudet, {Alain M.} and Michel Baltas and Liliane Gorrichon",

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doi = "10.1016/0167-4838(93)90063-W",

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McKie, JH, Jaouhari, R, Douglas, KT, Goffner, D, Feuillet, C, Grima-Pettenati, J, Boudet, AM, Baltas, M & Gorrichon, L 1993, 'A molecular model for cinnamyl alcohol dehydrogenase, a plant aromatic alcohol dehydrogenase involved in lignification', Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular, vol. 1202, no. 1, pp. 61-69. https://doi.org/10.1016/0167-4838(93)90063-W

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AU - McKie, James H.

AU - Jaouhari, Rabih

AU - Douglas, Kenneth T.

AU - Goffner, Deborah

AU - Feuillet, Catherine

AU - Grima-Pettenati, Jacqueline

AU - Boudet, Alain M.

AU - Baltas, Michel

AU - Gorrichon, Liliane

PY - 1993/9/3

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N2 - 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.

AB - 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.

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KW - sequence homology

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JF - Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular

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A molecular model for cinnamyl alcohol dehydrogenase, a plant aromatic alcohol dehydrogenase involved in lignification

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