Role of Plant Laccases in Lignin Polymerization
作者： Lise Jouanin , Lise Jouanin , Isabelle Debeaujon , Isabelle Debeaujon , Nathalie Demont-Caulet
DOI: 10.1016/B8978-0-12-416023-1.00005-7
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摘要: Abstract Laccases are ubiquitous oxidases present in animals, plants, bacteria, and fungi. In plant species, they occur as large multigenic families. The involvement of peroxidases lignification is supported by a wealth literature data. contrast, the role laccases this major process less firmly established. number laccases, which argues for variety functions development, makes identification lignin-specific challenge. However, past decade, development new genetic technologies tools has played central towards resolving issue. addition, model, Arabidopsis thaliana, recently provided novel insights about occurrence involved stem lignification. Information lignin-related also available from other such poplar, or organs tissues, seed coats. This review brings short cutting edge survey
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sci-hub.st 参考文章(96)
M. Koornneef, Mutations affecting the testa colour in Arabidopsis. Arabidopsis Information Service. ,vol. 27, pp. 1- 4 ,(1990)
W. Kiszczak, D. Rybaczek, K. Gorecka, U Kowalska, D. Krzyzanowska, Cytological assessment of carrot plants obtained in anther culture Acta Biologica Cracoviensia Series Botanica. ,vol. 50, pp. 7- 11 ,(2008)
, Analysis of the genome sequence of the flowering plant Arabidopsis thaliana. Nature. ,vol. 408, pp. 796- 815 ,(2000) , 10.1038/35048692
Alexander I. Saeed, Nirmal K. Bhagabati, John C. Braisted, Wei Liang, Vasily Sharov, Eleanor A. Howe, Jianwei Li, Mathangi Thiagarajan, Joseph A. White, John Quackenbush, TM4 microarray software suite Methods in Enzymology. ,vol. 411, pp. 134- 193 ,(2006) , 10.1016/S0076-6879(06)11009-5
Silvia Fornalé, Xinhui Shi, Chenglin Chai, Antonio Encina, Sami Irar, Montserrat Capellades, Elisabet Fuguet, Josep-Lluís Torres, Pere Rovira, Pere Puigdomènech, Joan Rigau, Erich Grotewold, John Gray, David Caparrós-Ruiz, ZmMYB31 directly represses maize lignin genes and redirects the phenylpropanoid metabolic flux. Plant Journal. ,vol. 64, pp. 633- 644 ,(2010) , 10.1111/J.1365-313X.2010.04363.X
C. W. Dence, The Determination of Lignin Springer, Berlin, Heidelberg. pp. 33- 61 ,(1992) , 10.1007/978-3-642-74065-7_3
Karl Freudenberg, Arthur Charles Neish, Constitution and Biosynthesis of Lignin ,(1968)
Christiane Galhaup, Sabine Goller, Clemens K. Peterbauer, Josef Strauss, Dietmar Haltrich, Characterization of the major laccase isoenzyme from Trametes pubescens and regulation of its synthesis by metal ions. Microbiology. ,vol. 148, pp. 2159- 2169 ,(2002) , 10.1099/00221287-148-7-2159
WATARU NAKAMURA, Studies on the biosynthesis of lignin. I. Disproof against the catalytic activity of laccase in the oxidation of coniferyl alcohol. Journal of Biochemistry. ,vol. 62, pp. 54- 61 ,(1967) , 10.1093/OXFORDJOURNALS.JBCHEM.A128635