Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:1.10.3.2 (laccase)
4,656 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The single-celled cotton fibers, produced from seed coat epidermal cells are the largest natural source of textile fibers. The economic value of cotton fiber lies in its length and quality. The multifunctional laccase enzymes play important roles in cell elongation, lignification and pigmentation in plants and could play crucial role in cotton fiber quality. Genome-wide analysis of cultivated allotetraploid (G. hirsutum) and its progenitor diploid (G. arboreum and G. raimondii) cotton species identified 84, 44 and 46 laccase genes, respectively. Analysis of chromosomal location, phylogeny, conserved domain and physical properties showed highly conserved nature of laccases across three cotton species. Gene expression, enzymatic activity and biochemical analysis of developing cotton fibers was performed using G. arboreum species. Of the total 44, 40 laccases showed expression during different stages of fiber development. The higher enzymatic activity of laccases correlated with higher lignin content at 25 DPA (Days Post Anthesis). Further, analysis of cotton fiber phenolic compounds showed an overall decrease at 25 DPA indicating possible incorporation of these substrates into lignin polymer during secondary cell wall biosynthesis. Overall data indicate significant roles of laccases in cotton fiber development, and presents an excellent opportunity for manipulation of fiber development and quality.
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PMID:Genome-wide identification of multifunctional laccase gene family in cotton (Gossypium spp.); expression and biochemical analysis during fiber development. 2767 39

To gain better understanding on laccase in apples and reveal its role in browning color formation during storage, laccases in apples were investigated. The full-length complementary DNAs encoding laccase genes were obtained from different tissues of apple including flowers, calyx, leaves and fruit peel of 'Red Delicious' and 'Cortland'. The apple laccases were compared to those in other plant species and found to have up to 99% homology to Arabidopsis and litchi. qRT-PCR analysis revealed changes in transcript abundance of LAC genes (2, 7, 9, 12, 14, 15 and 16) during storage and in response to DPA and 1-MCP treatments. Enzyme activity of laccase protein in apple peel increased with storage in control fruit, while decreased significantly with DPA or 1-MCP. Changes in phenolic compounds in pericarp tissues decreased generally during storage, but no significant effect of DPA and 1-MCP treatments on the phenolic compounds was found.
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PMID:Characterization of laccase from apple fruit during postharvest storage and its response to diphenylamine and 1-methylcyclopropene treatments. 2950 38