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Journal articles on the topic 'Cinnamyl alcohol dehydrogenase'

Author: Grafiati

Published: 4 June 2021

Last updated: 31 January 2023

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1

Lobo-da-Cunha, Alexandre, Diogo Amaral-de-Carvalho, Gonçalo Calado, and Vítor Costa. "Oxidation of cinnamyl alcohol and ethanol by oxidases and dehydrogenases in the digestive gland of gastropods." Journal of Molluscan Studies 85, no. 4 (November 2019): 398–403. http://dx.doi.org/10.1093/mollus/eyz025.

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Abstract Alcohol oxidases and dehydrogenases are poorly studied in the Mollusca, the second largest phylum of metazoans. In order to obtain an overview of the distribution of aromatic alcohols and ethanol-oxidizing enzymes in the gastropod phylogenetic tree, we investigated the activity of these enzymes in the digestive gland of 26 gastropod species in the clades Patellogastropoda, Neritimorpha, Vetigastropoda, Caenogastropoda and Heterobranchia. Marine, freshwater and terrestrial species, as well as herbivores and carnivores, were sampled so that gastropods varying widely in habitat and diet were included in the study. An aromatic alcohol oxidase, which was previously reported in herbivorous terrestrial gastropods, was detected in 25 of the studied species. The activity of a cinnamyl alcohol dehydrogenase was detected for the first time in gastropods and this enzyme was found to be present in all the species that were studied. Our study, thus, demonstrates that alcohol oxidases and dehydrogenases are ubiquitous enzymes among gastropods; these enzymes are found across the gastropod phylogenetic tree and across species varying widely in habitat and diet. The enzymes that catalyze the oxidation or dehydrogenation of cinnamyl alcohol must be involved in the metabolism of aromatic alcohols of very different dietary origins and conceivably have a detoxification function. Oxidase or dehydrogenase activities involving ethanol as a substrate were detected only in a few species, mostly those belonging to the Panpulmonata. This suggests that for many gastropods ethanol may not be metabolically relevant.

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2

Schubert, R., Christoph Sperisen, Gerhard Müller-Starck, Sabina La Scala, Dieter Ernst, Heinrich Sandermann Jr., and Klaus-Peter Häger. "The cinnamyl alcohol dehydrogenase gene structure in." Trees 12, no. 8 (1998): 453. http://dx.doi.org/10.1007/s004680050175.

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3

Mee, Blanaid, Dermot Kelleher, Jesus Frias, Renee Malone, Keith F. Tipton, Gary T. M. Henehan, and Henry J. Windle. "Characterization of cinnamyl alcohol dehydrogenase of Helicobacter pylori." FEBS Journal 272, no. 5 (February 17, 2005): 1255–64. http://dx.doi.org/10.1111/j.1742-4658.2005.04561.x.

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4

Richard Bowen, W., Nigel Lambert, Shirley Y. R. Pug, and Frank Taylor. "The yeast alcohol dehydrogenase catalysed conversion of cinnamaldehyde to cinnamyl alcohol." Journal of Chemical Technology & Biotechnology 36, no. 6 (April 24, 2007): 267–72. http://dx.doi.org/10.1002/jctb.280360605.

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5

McKie, James H., Rabih Jaouhari, Kenneth T. Douglas, Deborah Goffner, Catherine Feuillet, Jacqueline Grima-Pettenati, Alain M. Boudet, Michel Baltas, and Liliane Gorrichon. "A molecular model for cinnamyl alcohol dehydrogenase, a plant aromatic alcohol dehydrogenase involved in lignification." Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 1202, no. 1 (September 1993): 61–69. http://dx.doi.org/10.1016/0167-4838(93)90063-w.

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6

Lapierre, Catherine, Gilles Pilate, Brigitte Pollet, Isabelle Mila, Jean-Charles Leplé, Lise Jouanin, Hoon Kim, and John Ralph. "Signatures of cinnamyl alcohol dehydrogenase deficiency in poplar lignins." Phytochemistry 65, no. 3 (February 2004): 313–21. http://dx.doi.org/10.1016/j.phytochem.2003.11.007.

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7

Galliano, Hélène, Werner Heller, and Heinrich Sandermann. "Ozone induction and purification of spruce cinnamyl alcohol dehydrogenase." Phytochemistry 32, no. 3 (February 1993): 557–63. http://dx.doi.org/10.1016/s0031-9422(00)95136-7.

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8

PILLONEL, CHRISTIAN, PETER HUNZIKER, and ANDRES BINDER. "Multiple Forms of the Constitutive Wheat Cinnamyl Alcohol Dehydrogenase." Journal of Experimental Botany 43, no. 3 (1992): 299–305. http://dx.doi.org/10.1093/jxb/43.3.299.

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9

Park, Hye, Tae Kim, Seong Bhoo, Tae Lee, Sang-Won Lee, and Man-Ho Cho. "Biochemical Characterization of the Rice Cinnamyl Alcohol Dehydrogenase Gene Family." Molecules 23, no. 10 (October 16, 2018): 2659. http://dx.doi.org/10.3390/molecules23102659.

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Cinnamyl alcohol dehydrogenase (CAD) is involved in the final step of the phenylpropanod pathway, catalyzing the NADPH-dependent reduction of hydroxy-cinnamaldehydes into the corresponding alcohols. The rice genome contains twelve CAD and CAD-like genes, collectively called OsCADs. To elucidate the biochemical function of the OsCADs, OsCAD1, 2, 6, and 7, which are highly expressed in rice, were cloned from rice tissues. The cloned OsCADs were heterologously expressed in Escherichia coli as His-tag fusion proteins. The activity assay of the recombinant OsCADs showed that OsCAD2, 6, and 7 have CAD activity toward hydroxycinnamaldehydes, but OsCAD1 has no detectable catalytic activity. The kinetic parameters of the enzyme reactions demonstrated that OsCAD2 has the highest catalytic activity among the examined enzymes. This result agrees well with the finding that the Zn binding and NADPH binding motifs and the residues constituting the substrate binding pocket in bona fide plant CADs were fully conserved in OsCAD2. Although they have large variations in the residue for the substrate binding pocket, OsCAD6 and 7 catalyzed the reduction of hydroxycinnamaldehydes with a similar efficiency. Alignment of amino acid sequences showed that OsCAD1 lacks the GxxxxP motif for NADPH binding and has mismatches in residues important in the reduction process, which could be responsible for the loss of catalytic activity. OsCAD2 belongs to CAD Class I with bona fide CADs from other plant species and is constitutively expressed throughout the developmental stages of rice, with preferential expression in actively lignifying tissues such as the root, stem, and panicle, suggesting that it is mainly involved in developmental lignification in rice. The expression of OsCAD2 was also induced by biotic and abiotic stresses such as Xanthomonas oryzae pv. oryzae (Xoo) infection and UV-irradiation, suggesting that it plays a role in the defense response of rice, in addition to a bona fide role in developmental lignification. OsCAD6 and 7 belong in CAD Class II. Their expression is relatively lower than that of OsCAD2 and is confined to certain tissues, such as the leaf sheath, stem, and panicle. The expression of OsCAD6 was stimulated by Xoo infection and UV-irradiation. Thus OsCAD6 appears to be an inducible OsCAD that is likely involved in the defense response of rice against biotic and abiotic stresses.

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10

Halpin, Claire, Mary E. Knight, Geoffrey A. Foxon, Malcolm M. Campbell, Alain M. Boudet, Jaap J. Boon, Brigitte Chabbert, Marie-Therese Tollier, and Wolfgang Schuch. "Manipulation of lignin quality by downregulation of cinnamyl alcohol dehydrogenase." Plant Journal 6, no. 3 (September 1994): 339–50. http://dx.doi.org/10.1046/j.1365-313x.1994.06030339.x.

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11

Logemann, Elke, Susanne Reinold, Imre E. Somssich, and Klaus Hahlbrock. "A Novel Type of Pathogen Defense-Related Cinnamyl Alcohol Dehydrogenase." Biological Chemistry 378, no. 8 (1997): 909–14. http://dx.doi.org/10.1515/bchm.1997.378.8.909.

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12

Halpin, Claire, Mary E. Knight, Jacqueline Grima-Pettenati, Deborah Goffner, Alain Boudet, and Wolfgang Schuch. "Purification and Characterization of Cinnamyl Alcohol Dehydrogenase from Tobacco Stems." Plant Physiology 98, no. 1 (January 1, 1992): 12–16. http://dx.doi.org/10.1104/pp.98.1.12.

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13

Hibino, Takashi, Daisuke Shibata, Toshiaki Umezawa, and Takayoshi Higuchi. "Purification and partial sequences of Aralia cordata cinnamyl alcohol dehydrogenase." Phytochemistry 32, no. 3 (February 1993): 565–67. http://dx.doi.org/10.1016/s0031-9422(00)95137-9.

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14

Patel, Parth, Neha Gupta, Sushama Gaikwad, Dinesh C. Agrawal, and Bashir M. Khan. "Leucaena sp. recombinant cinnamyl alcohol dehydrogenase: Purification and physicochemical characterization." International Journal of Biological Macromolecules 63 (February 2014): 254–60. http://dx.doi.org/10.1016/j.ijbiomac.2013.09.005.

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15

Chanquia, Santiago Nahuel, Lei Huang, Guadalupe García Liñares, Pablo Domínguez de María, and Selin Kara. "Deep Eutectic Solvents as Smart Cosubstrate in Alcohol Dehydrogenase-Catalyzed Reductions." Catalysts 10, no. 9 (September 3, 2020): 1013. http://dx.doi.org/10.3390/catal10091013.

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Alcohol dehydrogenase (ADH) catalyzed reductions in deep eutectic solvents (DESs) may become efficient and sustainable alternatives to afford alcohols. This paper successfully explores the ADH-catalyzed reduction of ketones and aldehydes in a DES composed of choline chloride and 1,4-butanediol, in combination with buffer (Tris-HCl, 20% v/v). 1,4-butanediol (a DES component), acts as a smart cosubstrate for the enzymatic cofactor regeneration, shifting the thermodynamic equilibrium to the product side. By means of the novel DES media, cyclohexanone reduction was optimized to yield maximum productivity with low enzyme amounts (in the range of 10 g L−1 d−1). Notably, with the herein developed reaction media, cinnamaldehyde was reduced to cinnamyl alcohol, an important compound for the fragrance industry, with promising high productivities of ~75 g L−1 d−1.

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16

Pan, H., R. Zhou, G. V. Louie, J. K. Muhlemann, E. K. Bomati, M. E. Bowman, N. Dudareva, R. A. Dixon, J. P. Noel, and X. Wang. "Structural Studies of Cinnamoyl-CoA Reductase and Cinnamyl-Alcohol Dehydrogenase, Key Enzymes of Monolignol Biosynthesis." Plant Cell 26, no. 9 (September 1, 2014): 3709–27. http://dx.doi.org/10.1105/tpc.114.127399.

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17

Ramos, Rose Lucia Braz, Francisco Javier Tovar, Ricardo Magrani Junqueira, Fabiane Borges Lino, and Gilberto Sachetto-Martins. "Sugarcane expressed sequences tags (ESTs) encoding enzymes involved in lignin biosynthesis pathways." Genetics and Molecular Biology 24, no. 1-4 (December 2001): 235–41. http://dx.doi.org/10.1590/s1415-47572001000100031.

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Lignins are phenolic polymers found in the secondary wall of plant conductive systems where they play an important role by reducing the permeability of the cell wall to water. Lignins are also responsible for the rigidity of the cell wall and are involved in mechanisms of resistance to pathogens. The metabolic routes and enzymes involved in synthesis of lignins have been largely characterized and representative genes that encode enzymes involved in these processes have been cloned from several plant species. The synthesis of lignins is liked to the general metabolism of the phenylpropanoids in plants, having enzymes (e.g. phenylalanine ammonia-lyase (PAL), cinnamate 4-hydroxylase (C4H) and caffeic acid O-methyltransferase (COMT)) common to other processes as well as specific enzymes such as cinnamoyl-CoA reductase (CCR) and cinnamyl alcohol dehydrogenase (CAD). Some maize and sorghum mutants, shown to have defective in CAD and/or COMT activity, are easier to digest because they have a reduced lignin content, something which has motivated different research groups to alter the lignin content and composition of model plants by genetic engineering try to improve, for example, the efficiency of paper pulping and digestibility. In the work reported in this paper, we have made an inventory of the sugarcane expressed sequence tag (EST) coding for enzymes involved in lignin metabolism which are present in the sugarcane EST genome project (SUCEST) database. Our analysis focused on the key enzymes ferulate-5-hydroxylase (F5H), caffeic acid O-methyltransferase (COMT), caffeoyl CoA O-methyltransferase (CCoAOMT), hydroxycinnamate CoA ligase (4CL), cinnamoyl-CoA reductase (CCR) and cinnamyl alcohol dehydrogenase (CAD). The comparative analysis of these genes with those described in other species could be used as molecular markers for breeding as well as for the manipulation of lignin metabolism in sugarcane.

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18

Uthoff, Stefan, and Alexander Steinbüchel. "Purification and Characterization of an NAD+-Dependent XylB-Like Aryl Alcohol Dehydrogenase Identified in Acinetobacter baylyi ADP1." Applied and Environmental Microbiology 78, no. 24 (October 5, 2012): 8743–52. http://dx.doi.org/10.1128/aem.02224-12.

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ABSTRACTThe genexylBADP1fromAcinetobacter baylyiADP1 (gene annotation number ACIAD1578), coding for a putative aryl alcohol dehydrogenase, was heterologously expressed inEscherichia coliBL21(DE3). The respective aryl alcohol dehydrogenase was purified by fast protein liquid chromatography to apparent electrophoretic homogeneity. The predicted molecular weight of 39,500 per subunit was confirmed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. According to the nativeMwas determined by gel filtration, the enzyme forms dimers and therefore seems to be XylB related. The enzyme showed the highest activity at 40°C. For both the reduction and the oxidation reactions, the pH for optimum activity was 6.5. The enzyme was NADH dependent and able to reduce medium- to long-chainn-alkylaldehydes, methyl-branched aldehydes, and aromatic aldehydes, with benzaldehyde yielding the highest activity. The oxidation reaction with the corresponding alcohols showed only 2.2% of the reduction activity, with coniferyl alcohol yielding the highest activity. Maximum activities for the reduction and the oxidation reaction were 104.5 and 2.3 U mg−1of protein, respectively. The enzyme activity was affected by low concentrations of Ag+and Hg2+and high concentrations of Cu2+, Zn2+, and Fe2+. The genexylBADP1seems to be expressed constitutively and an involvement in coniferyl alcohol degradation is suggested. However, the enzyme is most probably not involved in the degradation of benzyl alcohol, anisalcohol, salicyl alcohol, vanillyl alcohol, cinnamyl alcohol, or aliphatic and isoprenoid alcohols.

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19

KURT, Fırat, and Ertuğrul FİLİZ. "Analysis of cinnamyl alcohol dehydrogenase (CAD) proteins from higher plant species." Bitlis Eren Üniversitesi Fen Bilimleri Dergisi 8, no. 1 (March 12, 2019): 26–38. http://dx.doi.org/10.17798/bitlisfen.462778.

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20

Somers, D. A., J. P. Nourse, J. M. Manners, S. Abrahams, and J. M. Watson. "A Gene Encoding a Cinnamyl Alcohol Dehydrogenase Homolog in Arabidopsis thaliana." Plant Physiology 108, no. 3 (July 1, 1995): 1309–10. http://dx.doi.org/10.1104/pp.108.3.1309.

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21

Lapierre, Catherine, Brigitte Pollet, John J. MacKay, and Ronald R. Sederoff. "Lignin Structure in a Mutant Pine Deficient in Cinnamyl Alcohol Dehydrogenase." Journal of Agricultural and Food Chemistry 48, no. 6 (June 2000): 2326–31. http://dx.doi.org/10.1021/jf991398p.

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22

Möller, Ralf, Diane Steward, Lorelle Phillips, Heather Flint, and Armin Wagner. "Gene silencing of cinnamyl alcohol dehydrogenase in Pinus radiata callus cultures." Plant Physiology and Biochemistry 43, no. 12 (December 2005): 1061–66. http://dx.doi.org/10.1016/j.plaphy.2005.11.001.

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23

Grima-Pettenati, Jacqueline, Christian Campargue, Annie Boudet, and Alain M. Boudet. "Purification and characterization of cinnamyl alcohol dehydrogenase isoforms from Phaseolus vulgaris." Phytochemistry 37, no. 4 (November 1994): 941–47. http://dx.doi.org/10.1016/s0031-9422(00)89508-4.

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24

Goffner, D., I. Joffroy, J. Grima-Pettenati, C. Halpin, M. E. Knight, W. Schuch, and A. M. Boudet. "Purification and characterization of isoforms of cinnamyl alcohol dehydrogenase fromEucalyptus xylem." Planta 188, no. 1 (1992): 48–53. http://dx.doi.org/10.1007/bf01160711.

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25

Feuillet, C., A. M. Boudet, and J. Grima-Pettenati. "Nucleotide Sequence of a cDNA Encoding Cinnamyl Alcohol Dehydrogenase from Eucalyptus." Plant Physiology 103, no. 4 (December 1, 1993): 1447. http://dx.doi.org/10.1104/pp.103.4.1447.

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26

Hibino, T., J. Q. Chen, D. Shibata, and T. Higuchi. "Nucleotide Sequence of a Eucalyptus botryoides Gene Encoding Cinnamyl Alcohol Dehydrogenase." Plant Physiology 104, no. 1 (January 1, 1994): 305–6. http://dx.doi.org/10.1104/pp.104.1.305.

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27

Baudracco, S., J. Grima-Pettanati, A. M. Boudet, and P. B. Gahan. "Quantitative cytochemical localization of cinnamyl alcohol dehydrogenase activity in plant tissues." Phytochemical Analysis 4, no. 5 (September 1993): 205–9. http://dx.doi.org/10.1002/pca.2800040503.

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28

Larroy, Carol, Xavier Parés, and Josep A. Biosca. "Characterization of a Saccharomyces cerevisiae NADP(H)-dependent alcohol dehydrogenase (ADHVII), a member of the cinnamyl alcohol dehydrogenase family." European Journal of Biochemistry 269, no. 22 (October 30, 2002): 5738–45. http://dx.doi.org/10.1046/j.1432-1033.2002.03296.x.

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29

Galeano, Esteban, Tarcísio Sales Vasconcelos, and Helaine Carrer. "Characterization of Cinnamyl Alcohol Dehydrogenase gene family in lignifying tissues of Tectona grandis L.f." Silvae Genetica 67, no. 1 (March 7, 2018): 1–11. http://dx.doi.org/10.2478/sg-2018-0001.

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Abstract The cinnamyl alcohol dehydrogenase (CAD) enzyme catalyzes the last step of monolignols synthesis in the lignin pathway. Tectona grandis (teak) is a tropical tree with high valuable timber. As there is few genetic information about lignin formation in teak, the purpose of this study is to characterize members of CAD family in this species. As methodology, PCR amplification using cDNA samples, vector cloning, sequencing, bioinformatics analyses and gene expression studies using real time RT-qPCR were performed. As results, four members (TgCAD1- TgCAD4) were obtained. Comparative analyses showed that all of them have conserved residues for catalytic zinc action, structural zinc ligation, NADPH binding and substrate specificity, consistent with the mechanism of alcohol dehydrogenases. Phylogenetic analysis showed that TgCADs are present in three main classes and seven groups. Expression analyses revealed that TgCAD1 was highly expressed in leaves and could be related with pathogen defense. TgCAD2 was more expressed in branches and roots. Differently, TgCAD3 and TgCAD4 were highly expressed in juvenile and mature sapwood, suggesting a crucial role in wood development and lignin biosynthesis, with tissue-specialized expression profiles. Furthermore, TgCAD4 could be related with teak maturation for being more expressed in sapwood of mature teak trees. As conclusion, this work is the first to characterize genes of CAD family in Tectona grandis. These genes could be interesting to develop transgenic plants for basic research and field applications.

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30

GE, Qian, Jing KUANG, Yu-Cui WU, Yuan ZHANG, Ya-Ping XIAO, and Zhe-Zhi WANG. "Cloning and Expression Analysis of Cinnamyl Alcohol Dehydrogenase (SmCAD) Gene inSalvia miltiorrhizaBunge." Plant Science Journal 31, no. 3 (2013): 261. http://dx.doi.org/10.3724/sp.j.1142.2013.30261.

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31

Kim, Kwang Ho, Jae-Young Kim, Chang Soo Kim, and Joon Weon Choi. "Pyrolysis of Lignin Obtained from Cinnamyl Alcohol Dehydrogenase (CAD) Downregulated Arabidopsis Thaliana." Journal of the Korean Wood Science and Technology 47, no. 4 (July 2019): 442–50. http://dx.doi.org/10.5658/wood.2019.47.4.442.

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32

Halpin, Claire, Karen Holt, Jan Chojecki, Duncan Oliver, Brigitte Chabbert, Bernard Monties, Keith Edwards, Abdellah Barakate, and Geoffrey A. Foxon. "Brown-midrib maize (bm1) - a mutation affecting the cinnamyl alcohol dehydrogenase gene." Plant Journal 14, no. 5 (June 1998): 545–53. http://dx.doi.org/10.1046/j.1365-313x.1998.00153.x.

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33

Barakat, Abdelali, Agnieszka Bagniewska-Zadworna, Alex Choi, Urmila Plakkat, Denis S. DiLoreto, Priyadarshini Yellanki, and John E. Carlson. "The cinnamyl alcohol dehydrogenase gene family in Populus: phylogeny, organization, and expression." BMC Plant Biology 9, no. 1 (2009): 26. http://dx.doi.org/10.1186/1471-2229-9-26.

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34

Kim, S. J., M. R. Kim, D. L. Bedgar, S. G. A. Moinuddin, C. L. Cardenas, L. B. Davin, C. Kang, and N. G. Lewis. "Functional reclassification of the putative cinnamyl alcohol dehydrogenase multigene family in Arabidopsis." Proceedings of the National Academy of Sciences 101, no. 6 (January 26, 2004): 1455–60. http://dx.doi.org/10.1073/pnas.0307987100.

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35

Li, Xing, Dongming Ma, Jianlin Chen, Gaobin Pu, Yunpeng Ji, Caiyan Lei, Zhigao Du, Benye Liu, Hechun Ye, and Hong Wang. "Biochemical characterization and identification of a cinnamyl alcohol dehydrogenase from Artemisia annua." Plant Science 193-194 (September 2012): 85–95. http://dx.doi.org/10.1016/j.plantsci.2012.05.011.

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36

Lee, Choonseok, Diana L. Bedgar, Laurence B. Davin, and Norman G. Lewis. "Assessment of a putative proton relay in Arabidopsis cinnamyl alcohol dehydrogenase catalysis." Organic & Biomolecular Chemistry 11, no. 7 (2013): 1127. http://dx.doi.org/10.1039/c2ob27189c.

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37

Knight, M. E., C. Halpin, and W. Schuch. "Identification and characterisation of cDNA clones encoding cinnamyl alcohol dehydrogenase from tobacco." Plant Molecular Biology 19, no. 5 (August 1992): 793–801. http://dx.doi.org/10.1007/bf00027075.

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38

Bukh, Christian, Pia Haugaard Nord-Larsen, and Søren K. Rasmussen. "Phylogeny and structure of the cinnamyl alcohol dehydrogenase gene family in Brachypodium distachyon." Journal of Experimental Botany 63, no. 17 (October 2012): 6223–36. http://dx.doi.org/10.1093/jxb/ers275.

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39

Preisner, Marta, Anna Kulma, Jacek Zebrowski, Lucyna Dymińska, Jerzy Hanuza, Malgorzata Arendt, Michal Starzycki, and Jan Szopa. "Manipulating cinnamyl alcohol dehydrogenase (CAD) expression in flax affects fibre composition and properties." BMC Plant Biology 14, no. 1 (2014): 50. http://dx.doi.org/10.1186/1471-2229-14-50.

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40

Ma, Q. H. "Functional analysis of a cinnamyl alcohol dehydrogenase involved in lignin biosynthesis in wheat." Journal of Experimental Botany 61, no. 10 (April 16, 2010): 2735–44. http://dx.doi.org/10.1093/jxb/erq107.

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41

Hawkins, S., J. Samaj, V. Lauvergeat, A. Boudet, and J. Grima-Pettenati. "Cinnamyl Alcohol Dehydrogenase: Identification of New Sites of Promoter Activity in Transgenic Poplar." Plant Physiology 113, no. 2 (February 1, 1997): 321–25. http://dx.doi.org/10.1104/pp.113.2.321.

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42

Marque, Nabila Yahiaoui, Christiane, Hélène Corbière, and Alain Michel Boudet. "Comparative efficiency of different constructs for down regulation of tobacco cinnamyl alcohol dehydrogenase." Phytochemistry 49, no. 2 (September 1998): 295–306. http://dx.doi.org/10.1016/s0031-9422(98)00269-6.

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43

Stasolla, Claudio, Jay Scott, Ulrika Egertsdotter, John Kadla, David O’ Malley, Ronald Sederoff, and Leonel van Zyl. "Analysis of lignin produced by cinnamyl alcohol dehydrogenase-deficient Pinus taeda cultured cells." Plant Physiology and Biochemistry 41, no. 5 (May 2003): 439–45. http://dx.doi.org/10.1016/s0981-9428(03)00051-2.

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44

Fu, Chunxiang, Xirong Xiao, Yajun Xi, Yaxin Ge, Fang Chen, Joseph Bouton, Richard A. Dixon, and Zeng-Yu Wang. "Downregulation of Cinnamyl Alcohol Dehydrogenase (CAD) Leads to Improved Saccharification Efficiency in Switchgrass." BioEnergy Research 4, no. 3 (January 7, 2011): 153–64. http://dx.doi.org/10.1007/s12155-010-9109-z.

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45

Mitchell, H. J., J. L. Hall, and M. S. Barber. "Elicitor-Induced Cinnamyl Alcohol Dehydrogenase Activity in Lignifying Wheat (Triticum aestivum L.) Leaves." Plant Physiology 104, no. 2 (February 1, 1994): 551–56. http://dx.doi.org/10.1104/pp.104.2.551.

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46

Zhang, Kewei, Qian Qian, Zejun Huang, Yiqin Wang, Ming Li, Lilan Hong, Dali Zeng, Minghong Gu, Chengcai Chu, and Zhukuan Cheng. "GOLD HULL AND INTERNODE2 Encodes a Primarily Multifunctional Cinnamyl-Alcohol Dehydrogenase in Rice." Plant Physiology 140, no. 3 (January 27, 2006): 972–83. http://dx.doi.org/10.1104/pp.105.073007.

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47

Baucher, M., J. Van Doorsselaere, J. Gielen, M. Van Montagu, D. Inze, and W. Boerjan. "Genomic Nucleotide Sequence of an Arabidopsis thaliana Gene Encoding a Cinnamyl Alcohol Dehydrogenase." Plant Physiology 107, no. 1 (January 1, 1995): 285–86. http://dx.doi.org/10.1104/pp.107.1.285.

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48

Russell, Wendy R., Gordon J. Provan, Mark J. Burkitt, and Andrew Chesson. "Extent of incorporation of hydroxycinnamaldehydes into lignin in cinnamyl alcohol dehydrogenase-downregulated plants." Journal of Biotechnology 79, no. 1 (April 2000): 73–85. http://dx.doi.org/10.1016/s0168-1656(00)00212-1.

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Marroni, Fabio, Sara Pinosio, Giusi Zaina, Federico Fogolari, Nicoletta Felice, Federica Cattonaro, and Michele Morgante. "Nucleotide diversity and linkage disequilibrium in Populus nigra cinnamyl alcohol dehydrogenase (CAD4) gene." Tree Genetics & Genomes 7, no. 5 (April 15, 2011): 1011–23. http://dx.doi.org/10.1007/s11295-011-0391-5.

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Bucciarelli, B., H. G. Jung, M. E. Ostry, N. A. Anderson, and C. P. Vance. "Wound response characteristics as related to phenylpropanoid enzyme activity and lignin deposition in resistant and susceptible Populus tremuloides inoculated with Entoleuca mammata (Hypoxylon mammatum)." Canadian Journal of Botany 76, no. 7 (July 1, 1998): 1282–89. http://dx.doi.org/10.1139/b98-121.

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Abstract:

Green internodal stem tissues of glasshouse grown Populus tremuloides were either wounded or wound-inoculated with Entoleuca mammata (Hypoxylon mammatum) and assayed for phenylalanine ammonia-lyase (PAL), caffeic acid - o-methyltransferase (CA-OMT), and cinnamyl - alcohol dehydrogenase (CAD) activity over a 96-h period. Lignin deposited in response to the treatments was analyzed by the Klason and the pyrolysis - gas chromatographic (GC) - mass spectroscopy (MS) methodologies. The wound-inoculated treatment resulted in a wound morphology congruent with a typical resistant and susceptible response to E. mammata. Wounding alone resulted in no morphological differences between the two genotypes. In wound-inoculated stem tissue PAL and CAD activities were substantially higher in the resistant relative to the susceptible genotype. Total Klason lignin was similar for both genotypes; however, pyrolysis-GC-MS analysis revealed a difference in the lignin monomeric composition between the two genotypes, with the susceptible genotype accumulating higher levels of hydroxyphenyl units relative to the resistant genotype. It is concluded that differences in PAL and CAD activity and the synthesis of distinct phenylpropanoid monomers distinguish the resistant from the susceptible aspen genotype. Alterations in boundary zone formation due to the differential synthesis of phenylpropanoid monomers and its effect on compartmentalization of the pathogen are discussed.Key words: aspen, Hypoxylon canker, phenylalanine ammonia-lyase, cinnamyl - alcohol dehydrogenase, caffeic acid - o-methyltransferase, disease resistance.

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