The role of of laccase in lignification
Article first published online: 5 MAR 2002
The Plant Journal
Volume 4, Issue 5, pages 751–757, November 1993
How to Cite
O'Malley, D. M., Whetten, R., Bao, W., Chen, C.-L. and Sederoff, R. R. (1993), The role of of laccase in lignification. The Plant Journal, 4: 751–757. doi: 10.1046/j.1365-313X.1993.04050751.x
- Issue published online: 5 MAR 2002
- Article first published online: 5 MAR 2002
- Received 14 April 1993; revised 12 July 1993; accepted 16 July 1993.
- Cited By
The enzymatic mechanism of monolignol polymerization in lignin biosynthesis is not known, although it has been the subject of significant interest for more than 60 years. Peroxidase had been considered to be the exclusive plant enzyme involved in the oxidative polymerization of lignin precursors. Recently, laccase and laccase-like oxidase activities have been associated with lignification. Laccase is bound to lignifying plant cell walls and can polymerize lignin precursors in vitro. Strong circumstantial evidence from different species implicates this enzyme in the polymerization of lignin precursors. Lignin has a complex structure and it has been difficult to analyze the heterogeneity of lignin by chemical and physical techniques. If lignin precursors are polymerized by enzymes that differ in their catalytic properties, then lignin heterogeneity could be produced by differential expression of multiple enzymes during plant development. When laccase genes are correctly identified, these ideas can be tested in genetic experiments where gain or loss of function can be predicted by the presence or absence of the functional gene.