The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
Chemical Compound Review

Laccase     (2S)-1-[(2S,3S)-2-[[(2S)-4- aminocarbonyl-2...

Synonyms: AC1MHXGX, Hericium erinaceum laccase
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of Laccase

  • The CotA laccase from the endospore coat of Bacillus subtilis has been crystallized in the presence of the non-catalytic co-oxidant 2,2'-azinobis-(3-ethylbenzothiazoline-6-sulfonate) (ABTS), and the structure was determined using synchrotron radiation [1].
  • The fungus Cryptococcus neoformans is an opportunistic human pathogen that causes a life-threatening meningoencephalitis by expression of virulence factors such as melanin, a black pigment produced by the cell wall-associated enzyme laccase [2].
  • 16-O- Acetylvindoline (1a) was oxidatively transformed into an iminium derivative (2a) by copper oxidases (laccase and human ceruloplasmin), an unknown enzyme system(s) of Streptomyces griseus, and the chemical oxidizing agent 2,3-dichloro-5,6- dicyano -1,4-benzoquinone ( DDQ ) [3].
  • Cryptococcus neoformans is an important opportunistic pathogen in immunocompromised patients, including those with human immunodeficiency virus, and expresses a virulence-associated laccase which is believed to oxidize brain catecholamines and iron as a defense against host immune cells [4].
  • While laccase of Cryptococcus neoformans is implicated in the virulence of the organism, our recent studies showing absence of melanin in the infected mouse brain has led us to a search for alternative roles for laccase in cryptococcosis [5].

Psychiatry related information on Laccase

  • In the enzymatic prebleaching the enzyme laccase was used at two conditions of pH and temperature, whereas the reaction time was fixed at 1 h in all pretreatments [6].

High impact information on Laccase


Chemical compound and disease context of Laccase


Biological context of Laccase

  • Based on amino acid sequence comparison between these proteins, putative copper ligands of N. crassa laccase are proposed [13].
  • Low-temperature magnetic circular dichroism studies of native laccase: spectroscopic evidence for exogenous ligand bridging at a trinuclear copper active site [14].
  • The laccase (benzenediol:oxygen oxidoreductase, EC gene from Neurospora crassa was cloned and part of its nucleotide sequence corresponding to the carboxyl-terminal region of the protein has been determined [13].
  • The analyzed carboxyl-terminal region of laccase exhibits a striking sequence homology to the carboxyl-terminal part of the third homology unit of the multicopper oxidase ceruloplasmin and to a smaller extent, to the low molecular weight blue copper proteins plastocyanin and azurin [13].
  • Laccase is implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism in fungi and plants [15].

Anatomical context of Laccase

  • Finally, we show that these biological effects observed in the C1 deletion mutant are mediated by alteration of cell wall integrity and displacement of laccase from the cell wall [2].
  • Laccase protects Cryptococcus neoformans from antifungal activity of alveolar macrophages [5].
  • Infection with laccase-positive (melanotic) C. neoformans cells also elicited higher MCP-1 levels and more infiltrating leukocytes than did infection with laccase-negative cells [16].
  • The genes were verified as encoding active laccases by heterologous expression in tobacco cells and demonstration of laccase activity in extracts from transformed tobacco cell lines [17].
  • Liver melanosome extracts display a very strong laccase (dimethoxyphenoloxidase) activity but spleen extracts do not [18].

Associations of Laccase with other chemical compounds

  • The SKU5 gene belongs to a 19-member gene family designated SKS (SKU5 Similar) that is related structurally to the multiple-copper oxidases ascorbate oxidase and laccase [19].
  • Spectroscopic and kinetic studies on the oxygen-centered radical formed during the four-electron reduction process of dioxygen by Rhus vernicifera laccase [20].
  • The 14N ENDOR, and, therefore, the structure, of this site corresponds extremely closely to that of the laccase type 3 (Cu(II) [21].
  • Under the catalysis of laccase, the apparent oxidation rates (kcat and kcat/Km) of two nonphenolic substrates, potassium ferrocyanide and 2,2'-azinobis-(3-ethylbenzthiazoline-6-sulfonic acid), decreased monotonically as the pH increased [22].
  • This study investigates the possible role of a laccase and a FAD-dependent aryl alcohol oxidase (veratryl alcohol oxidase, VAO) excreted by the basidiomycete Pleurotus ostreatus [23].
  • From a detailed analysis of the catalytic reduction of dioxygen by laccase in the presence of a one-electron redox mediator it can be concluded that the immobilized enzyme remains as active as in homogeneous solution [24].

Gene context of Laccase

  • In this study, cDNA and genomic clones encoding a homologue of the yeast gene anti-oxidant 1 (ATX1) from the white-rot fungus Trametes versicolor, a basidiomycete known to produce several laccase isoenzymes involved in lignin degradation, were identified [25].
  • A number of genes have been implicated in the regulation of laccase and melanization, including IPC1, GPA1, MET3, and STE12 [26].
  • The protein encoded by the RSp1530 locus is a multicopper protein with laccase activity [27].
  • Serotype D yeasts were transformed with a plasmid containing the CNA1 cDNA in an antisense orientation under the control of the inducible GAL7 promoter, and serotype A yeasts were transformed with a plasmid containing the LAC1 cDNA in an antisense orientation under the control of the constitutive actin promoter [28].
  • Overexpression of ire1 in a T. reesei strain that expresses a foreign protein (laccase 1 from Phlebia radiata), results in up-regulation of the UPR pathway, as indicated by the increased expression levels of the known UPR target genes bip1 and pdi1 [29].

Analytical, diagnostic and therapeutic context of Laccase


  1. Substrate and dioxygen binding to the endospore coat laccase from Bacillus subtilis. Enguita, F.J., Marçal, D., Martins, L.O., Grenha, R., Henriques, A.O., Lindley, P.F., Carrondo, M.A. J. Biol. Chem. (2004) [Pubmed]
  2. The role and mechanism of diacylglycerol-protein kinase C1 signaling in melanogenesis by Cryptococcus neoformans. Heung, L.J., Kaiser, A.E., Luberto, C., Del Poeta, M. J. Biol. Chem. (2005) [Pubmed]
  3. Formation of a reactive iminium derivative by enzymatic and chemical oxidations of 16-O-acetylvindoline. Sariaslani, F.S., Eckenrode, F.M., Beale, J.M., Rosazza, J.P. J. Med. Chem. (1984) [Pubmed]
  4. Laccase of Cryptococcus neoformans is a cell wall-associated virulence factor. Zhu, X., Gibbons, J., Garcia-Rivera, J., Casadevall, A., Williamson, P.R. Infect. Immun. (2001) [Pubmed]
  5. Laccase protects Cryptococcus neoformans from antifungal activity of alveolar macrophages. Liu, L., Tewari, R.P., Williamson, P.R. Infect. Immun. (1999) [Pubmed]
  6. Laccase from Trametes versicolor: stability at temperature and alkaline conditions and its effect on biobleaching of hardwood kraft pulp. de Carvalho, M.E., Monteiro, M.C., Sant'Anna, G.L. Appl. Biochem. Biotechnol. (1999) [Pubmed]
  7. Effect of the laccase gene CNLAC1, on virulence of Cryptococcus neoformans. Salas, S.D., Bennett, J.E., Kwon-Chung, K.J., Perfect, J.R., Williamson, P.R. J. Exp. Med. (1996) [Pubmed]
  8. The DEAD-box RNA helicase Vad1 regulates multiple virulence-associated genes in Cryptococcus neoformans. Panepinto, J., Liu, L., Ramos, J., Zhu, X., Valyi-Nagy, T., Eksi, S., Fu, J., Jaffe, H.A., Wickes, B., Williamson, P.R. J. Clin. Invest. (2005) [Pubmed]
  9. TRANSPARENT TESTA10 encodes a laccase-like enzyme involved in oxidative polymerization of flavonoids in Arabidopsis seed coat. Pourcel, L., Routaboul, J.M., Kerhoas, L., Caboche, M., Lepiniec, L., Debeaujon, I. Plant Cell (2005) [Pubmed]
  10. Loss of cytochrome c oxidase activity and acquisition of resistance to quinone analogs in a laccase-positive variant of Azospirillum lipoferum. Alexandre, G., Bally, R., Taylor, B.L., Zhulin, I.B. J. Bacteriol. (1999) [Pubmed]
  11. Enzymological characterization of EpoA, a laccase-like phenol oxidase produced by Streptomyces griseus. Endo, K., Hayashi, Y., Hibi, T., Hosono, K., Beppu, T., Ueda, K. J. Biochem. (2003) [Pubmed]
  12. Dimethoxyphenol oxidase activity of different microbial blue multicopper proteins. Solano, F., Lucas-Elío, P., López-Serrano, D., Fernández, E., Sanchez-Amat, A. FEMS Microbiol. Lett. (2001) [Pubmed]
  13. Isolation and partial nucleotide sequence of the laccase gene from Neurospora crassa: amino acid sequence homology of the protein to human ceruloplasmin. Germann, U.A., Lerch, K. Proc. Natl. Acad. Sci. U.S.A. (1986) [Pubmed]
  14. Low-temperature magnetic circular dichroism studies of native laccase: spectroscopic evidence for exogenous ligand bridging at a trinuclear copper active site. Allendorf, M.D., Spira, D.J., Solomon, E.I. Proc. Natl. Acad. Sci. U.S.A. (1985) [Pubmed]
  15. Crystal structure of the type-2 Cu depleted laccase from Coprinus cinereus at 2.2 A resolution. Ducros, V., Brzozowski, A.M., Wilson, K.S., Brown, S.H., Ostergaard, P., Schneider, P., Yaver, D.S., Pedersen, A.H., Davies, G.J. Nat. Struct. Biol. (1998) [Pubmed]
  16. Melanization of Cryptococcus neoformans affects lung inflammatory responses during cryptococcal infection. Mednick, A.J., Nosanchuk, J.D., Casadevall, A. Infect. Immun. (2005) [Pubmed]
  17. Characterization and heterologous expression of laccase cDNAs from xylem tissues of yellow-poplar (Liriodendron tulipifera). LaFayette, P.R., Eriksson, K.E., Dean, J.F. Plant Mol. Biol. (1999) [Pubmed]
  18. Spleen and liver pigmented macrophages of Rana esculenta L. A new melanogenic system? Gallone, A., Guida, G., Maida, I., Cicero, R. Pigment Cell Res. (2002) [Pubmed]
  19. The Arabidopsis SKU5 gene encodes an extracellular glycosyl phosphatidylinositol-anchored glycoprotein involved in directional root growth. Sedbrook, J.C., Carroll, K.L., Hung, K.F., Masson, P.H., Somerville, C.R. Plant Cell (2002) [Pubmed]
  20. Spectroscopic and kinetic studies on the oxygen-centered radical formed during the four-electron reduction process of dioxygen by Rhus vernicifera laccase. Huang, H., Zoppellaro, G., Sakurai, T. J. Biol. Chem. (1999) [Pubmed]
  21. Coordination environment for the type 3 copper center of tree laccase and CuB of cytochrome c oxidase as determined by electron nuclear double resonance. Cline, J., Reinhammar, B., Jensen, P., Venters, R., Hoffman, B.M. J. Biol. Chem. (1983) [Pubmed]
  22. Effects of redox potential and hydroxide inhibition on the pH activity profile of fungal laccases. Xu, F. J. Biol. Chem. (1997) [Pubmed]
  23. Veratryl alcohol oxidase from Pleurotus ostreatus participates in lignin biodegradation and prevents polymerization of laccase-oxidized substrates. Marzullo, L., Cannio, R., Giardina, P., Santini, M.T., Sannia, G. J. Biol. Chem. (1995) [Pubmed]
  24. Oriented immobilization of a fully active monolayer of histidine-tagged recombinant laccase on modified gold electrodes. Balland, V., Hureau, C., Cusano, A.M., Liu, Y., Tron, T., Limoges, B. Chemistry (2008) [Pubmed]
  25. Identification and functional expression of tahA, a filamentous fungal gene involved in copper trafficking to the secretory pathway in Trametes versicolor. Uldschmid, A., Engel, M., Dombi, R., Marbach, K. Microbiology (Reading, Engl.) (2002) [Pubmed]
  26. CNLAC1 is required for extrapulmonary dissemination of Cryptococcus neoformans but not pulmonary persistence. Noverr, M.C., Williamson, P.R., Fajardo, R.S., Huffnagle, G.B. Infect. Immun. (2004) [Pubmed]
  27. Polyphenol oxidase activity expression in Ralstonia solanacearum. Hernández-Romero, D., Solano, F., Sanchez-Amat, A. Appl. Environ. Microbiol. (2005) [Pubmed]
  28. Antisense repression in Cryptococcus neoformans as a laboratory tool and potential antifungal strategy. Gorlach, J.M., McDade, H.C., Perfect, J.R., Cox, G.M. Microbiology (Reading, Engl.) (2002) [Pubmed]
  29. The ire1 and ptc2 genes involved in the unfolded protein response pathway in the filamentous fungus Trichoderma reesei. Valkonen, M., Penttilä, M., Saloheimo, M. Mol. Genet. Genomics (2004) [Pubmed]
  30. Copper-mediated reversal of defective laccase in a Deltavph1 avirulent mutant of Cryptococcus neoformans. Zhu, X., Gibbons, J., Zhang, S., Williamson, P.R. Mol. Microbiol. (2003) [Pubmed]
  31. The structure of Rigidoporus lignosus Laccase containing a full complement of copper ions, reveals an asymmetrical arrangement for the T3 copper pair. Garavaglia, S., Cambria, M.T., Miglio, M., Ragusa, S., Iacobazzi, V., Palmieri, F., D'Ambrosio, C., Scaloni, A., Rizzi, M. J. Mol. Biol. (2004) [Pubmed]
  32. Electrochemical characterization of purified Rhus vernicifera laccase: voltammetric evidence for a sequential four-electron transfer. Johnson, D.L., Thompson, J.L., Brinkmann, S.M., Schuller, K.A., Martin, L.L. Biochemistry (2003) [Pubmed]
WikiGenes - Universities