This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Sterjiades, R. Articles by Eriksson, K.-E. L. Search for Related Content PubMed PubMed Citation Articles by Sterjiades, R. Articles by Eriksson, K.-E. L. Agricola Articles by Sterjiades, R. Articles by Eriksson, K.-E. L.

Metabolism and Enzymology

Laccase from Sycamore Maple (Acer pseudoplatanus) Polymerizes Monolignols

Department of Biochemistry, Center for Biological Resource Recovery, University of Georgia, Athens, Georgia 30602

Current understanding of the final oxidative steps leading to lignin deposition in trees and other higher plants is limited with respect to what enzymes are involved, where they are localized, how they are transported, and what factors regulate them. With the use of cell suspension cultures of sycamore maple (Acer pseudoplatanus), an in-depth study of laccase, one of the oxidative enzymes possibly responsible for catalyzing the dehydrogenative polymerization of monolignols in the extracellular matrix, was undertaken. The time course for secretion of laccase into suspension culture medium was determined with respect to age and mass of the cells. Laccase was completely separated from peroxidase activity by hydrophobic interaction column chromatography, and its purity was assessed with different types of gel electrophoresis (isoelectric focusing-, native-, and sodium dodecyl sulfate-polyacrylamide gel electrophoresis). Amino acid and glycosyl analyses of the purified enzyme were compared with those reported from previous studies of plant and fungal laccases. The specific activity of laccase toward several common substrates, including monolignols, was determined. Unlike a laccase purified from the Japanese lacquer tree (Rhus vernicifera), laccase from sycamore maple oxidized sinapyl, coniferyl, and p-coumaryl alcohols to form water-insoluble polymers (dehydrogenation polymers).

This article has been cited by other articles:

				A. Zamboni, L. Minoia, A. Ferrarini, G. B. Tornielli, E. Zago, M. Delledonne, and M. Pezzotti Molecular analysis of post-harvest withering in grape by AFLP transcriptional profiling J. Exp. Bot., November 13, 2008; (2008) ern256v1. [Abstract] [Full Text] [PDF]

				S. E. Abdel-Ghany and M. Pilon MicroRNA-mediated Systemic Down-regulation of Copper Protein Expression in Response to Low Copper Availability in Arabidopsis J. Biol. Chem., June 6, 2008; 283(23): 15932 - 15945. [Abstract] [Full Text] [PDF]

				G. J. Dick, J. W. Torpey, T. J. Beveridge, and B. M. Tebo Direct Identification of a Bacterial Manganese(II) Oxidase, the Multicopper Oxidase MnxG, from Spores of Several Different Marine Bacillus Species Appl. Envir. Microbiol., March 1, 2008; 74(5): 1527 - 1534. [Abstract] [Full Text] [PDF]

				X. Cai, E. J. Davis, J. Ballif, M. Liang, E. Bushman, V. Haroldsen, J. Torabinejad, and Y. Wu Mutant identification and characterization of the laccase gene family in Arabidopsis J. Exp. Bot., August 1, 2006; 57(11): 2563 - 2569. [Abstract] [Full Text] [PDF]

				L. Pourcel, J.-M. Routaboul, L. Kerhoas, M. Caboche, L. Lepiniec, and I. Debeaujon TRANSPARENT TESTA10 Encodes a Laccase-Like Enzyme Involved in Oxidative Polymerization of Flavonoids in Arabidopsis Seed Coat PLANT CELL, November 1, 2005; 17(11): 2966 - 2980. [Abstract] [Full Text] [PDF]

				P. Ranocha, M. Chabannes, S. Chamayou, S. Danoun, A. Jauneau, A.-M. Boudet, and D. Goffner Laccase Down-Regulation Causes Alterations in Phenolic Metabolism and Cell Wall Structure in Poplar Plant Physiology, May 1, 2002; 129(1): 145 - 155. [Abstract] [Full Text] [PDF]

				G. J. McDougall A comparison of proteins from the developing xylem of compression and non-compression wood of branches of Sitka spruce (Picea sitchensis) reveals a differentially expressed laccase J. Exp. Bot., August 1, 2000; 51(349): 1395 - 1401. [Abstract] [Full Text] [PDF]

				A.-C. Fitchette, M. Cabanes-Macheteau, L. Marvin, B. Martin, B. Satiat-Jeunemaitre, V. Gomord, K. Crooks, P. Lerouge, L. Faye, and C. Hawes Biosynthesis and Immunolocalization of Lewis a-Containing N-Glycans in the Plant Cell Plant Physiology, October 1, 1999; 121(2): 333 - 344. [Abstract] [Full Text]

				W. Bao, D. M. O'Malley, R. Whetten, and R. R. Sederoff A Laccase Associated with Lignification in Loblolly Pine Xylem Science, April 30, 1993; 260(5108): 672 - 674. [Abstract] [PDF]