Purification and properties of cinnamyl alcohol dehydrogenase from higher plants involved in lignin biosynthesis

Mansell, Richard L.; Gross, Georg G.; Stöckigt, Joachim; Franke, Heinz; Zenk, Meinhart H.

doi:10.1016/s0031-9422(00)86917-4

Cited by 144 publications

(63 citation statements)

References 24 publications

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“…Electrophoresis was performed as described by Laemmli (1970) but without SDS in the buffers. Activity staining was performed as described by Mansell et al (1974). The gels were incubated for 2 h at room temperature in darkness in 10 mL of a reaction mixture that contained 100 mM Tris-HCl (pH 8.8), 1.5 mg of nitroblue tetrazolium, 0.1 mg of phenazinemethosulfate, 2.5 mg of NADP, and 2.5 mg of coniferyl alcohol (or another cinnamyl alcohol) or 25 pL of ethanol.…”

Section: Nondenaturing Page and Activity Stainingmentioning

confidence: 99%

Changes in the Activity and mRNA of Cinnamyl Alcohol Dehydrogenase during Tracheary Element Differentiation in Zinnia

et al. 1997

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Section: Nondenaturing Page and Activity Stainingmentioning

confidence: 99%

Changes in the Activity and mRNA of Cinnamyl Alcohol Dehydrogenase during Tracheary Element Differentiation in Zinnia

et al. 1997

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“…Cinnamyl-alcohol dehydrogenase (CAD; EC 1.1. 1.195) is an enzyme in the lignin biosynthetic pathway that catalyzes the final reduction of the hydroxyl-cinnamaldehydes to the corresponding alcohols (Mansell et al 1974). The relative proportions of these cinnamyl alcohols are important factors that determine the structural and mechanical properties of lignin (Mellerowicz et al 2001;Sibout et al 2003).…”

Section: Introductionmentioning

confidence: 99%

FLEXIBLE CULM 1 encoding a cinnamyl-alcohol dehydrogenase controls culm mechanical strength in rice

et al. 2008

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Culm mechanical strength is an important agronomic trait in crop breeding. To understand the molecular mechanisms that control culm mechanical strength, we identified a flexible culm1 (fc1) mutant by screening a rice T-DNA insertion mutant library. This mutant exhibited an abnormal development phenotype, including late heading time, semi-dwarf habit, and flexible culm. In this study, we cloned the FLEXIBLE CULM1 (FC1) gene in rice using a T-DNA tagging approach. FC1 encodes a cinnamyl-alcohol dehydrogenase and is mainly expressed in the sclerenchyma cells of the secondary cell wall and vascular bundle region. In these types of cells, a deficiency of FC1 in the fc1 mutant caused a reduction in cell wall thickness, as well as a decrease in lignin. Extracts from the first internodes and panicles of the fc1 plants exhibited drastically reduced cinnamyl-alcohol dehydrogenase activity. Further histological and biochemical analyses revealed that the p-hydroxyphenyl and guaiacyl monomers in fc1 cell wall were reduced greatly. Our results indicated that FC1 plays an important role in the biosynthesis of lignin and the control of culm strength in rice.

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“…CAD leads to the conversion of hydroxy-cinnamaldehydes to the corresponding alcohols. The relative proportions of these cinnamyl alcohols is an important factor for lignin structural traits and mechanical properties (Baucher et al, 1998;Mellerowicz et al, 2001).CAD was one of the first enzymes studied in the lignin synthesis pathway (Mansell et al, 1974;Wyrambik and Grisebach, 1975). Since then, many CAD cDNAs have been isolated in different plant species (for review, see Dixon et al, 2001).…”

mentioning

confidence: 99%

“…CAD was one of the first enzymes studied in the lignin synthesis pathway (Mansell et al, 1974;Wyrambik and Grisebach, 1975). Since then, many CAD cDNAs have been isolated in different plant species (for review, see Dixon et al, 2001).…”

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confidence: 99%

Expression Pattern of Two Paralogs Encoding Cinnamyl Alcohol Dehydrogenases in Arabidopsis. Isolation and Characterization of the Corresponding Mutants

et al. 2003

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Studying Arabidopsis mutants of the phenylpropanoid pathway has unraveled several biosynthetic steps of monolignol synthesis. Most of the genes leading to monolignol synthesis have been characterized recently in this herbaceous plant, except those encoding cinnamyl alcohol dehydrogenase (CAD). We have used the complete sequencing of the Arabidopsis genome to highlight a new view of the complete CAD gene family. Among nine AtCAD genes, we have identified the two distinct paralogs AtCAD-C and AtCAD-D, which share 75% identity and are likely to be involved in lignin biosynthesis in other plants. Northern, semiquantitative restriction fragment-length polymorphism-reverse transcriptase-polymerase chain reaction and western analysis revealed that AtCAD-C and AtCAD-D mRNA and protein ratios were organ dependent. Promoter activities of both genes are high in fibers and in xylem bundles. However, AtCAD-C displayed a larger range of sites of expression than AtCAD-D. Arabidopsis null mutants (Atcad-D and Atcad-C) corresponding to both genes were isolated. CAD activities were drastically reduced in both mutants, with a higher impact on sinapyl alcohol dehydrogenase activity (6% and 38% of residual sinapyl alcohol dehydrogenase activities for Atcad-D and Atcad-C, respectively). Only Atcad-D showed a slight reduction in Klason lignin content and displayed modifications of lignin structure with a significant reduced proportion of conventional S lignin units in both stems and roots, together with the incorporation of sinapaldehyde structures ether linked at C␤. These results argue for a substantial role of AtCAD-D in lignification, and more specifically in the biosynthesis of sinapyl alcohol, the precursor of S lignin units.Lignin is a complex phenolic polymer whose structure is vital to functions such as imparting rigidity to plant organs and as a physical barrier to invading pests. Its presence in cell wall confers to vessels hydrophobic properties that facilitate conduction of water, photo-assimilates, and minerals to different parts of the plant. Lignin structure and composition differ widely at the interspecies level as well as cell types and at the subcellular cell wall level (Donaldson, 2001). Striking differences are mostly observable between gymnosperms and angiosperms. These taxa contain different qualitative and quantitative proportions of monolignols or cinnamyl alcohols representing the main lignin monomers. The formation of cinnamyl alcohols from the corresponding cinnamoylCoA esters requires two enzymatic modifications of the carbonate chain of the phenolic precursors. The first step is catalyzed by cinnamoyl CoA reductase, and the second step is catalyzed by cinnamyl alcohol dehydrogenase (CAD). CAD leads to the conversion of hydroxy-cinnamaldehydes to the corresponding alcohols. The relative proportions of these cinnamyl alcohols is an important factor for lignin structural traits and mechanical properties (Baucher et al., 1998;Mellerowicz et al., 2001).CAD was one of the first enzymes studied in the lignin syn...

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Purification and properties of cinnamyl alcohol dehydrogenase from higher plants involved in lignin biosynthesis

Cited by 144 publications

References 24 publications

Changes in the Activity and mRNA of Cinnamyl Alcohol Dehydrogenase during Tracheary Element Differentiation in Zinnia

Changes in the Activity and mRNA of Cinnamyl Alcohol Dehydrogenase during Tracheary Element Differentiation in Zinnia

FLEXIBLE CULM 1 encoding a cinnamyl-alcohol dehydrogenase controls culm mechanical strength in rice

Expression Pattern of Two Paralogs Encoding Cinnamyl Alcohol Dehydrogenases in Arabidopsis. Isolation and Characterization of the Corresponding Mutants

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