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Volumn 2011, Issue , 2011, Pages

The Laccase Engineering Database: A classification and analysis system for laccases and related multicopper oxidases

Author keywords

[No Author keywords available]

Indexed keywords

COPPER; LACCASE;

EID: 80052342138     PISSN: 17580463     EISSN: None     Source Type: Journal    
DOI: 10.1093/database/bar006     Document Type: Article
Times cited : (110)

References (40)
  • 1
    • 7744236144 scopus 로고    scopus 로고
    • Multicopper oxidases and oxygenases
    • Solomon, E., Sundaram, U. and Machonkin, T. (1996) Multicopper oxidases and oxygenases. Chem. Rev., 96, 2563-2606.
    • (1996) Chem. Rev. , vol.96 , pp. 2563-2606
    • Solomon, E.1    Sundaram, U.2    Machonkin, T.3
  • 3
    • 0001290045 scopus 로고    scopus 로고
    • Prosite: A documented database using patterns and profiles as motif descriptors
    • Sigrist, C. J., Cerutti, L., Hulo, N. et al. (2002) PROSITE: a documented database using patterns and profiles as motif descriptors. Brief Bioinform., 3, 265-274.
    • (2002) Brief Bioinform. , vol.3 , pp. 265-274
    • Sigrist, C.J.1    Cerutti, L.2    Hulo, N.3
  • 4
    • 0025058305 scopus 로고
    • The blue oxidases, ascorbate oxidase, laccase and ceruloplasmin. Modelling and structural relationships
    • DOI 10.1111/j.1432-1033.1990.tb15311.x
    • Messerschmidt, A. and Huber, R. (1990) The blue oxidases, ascorbate oxidase, laccase and ceruloplasmin. Modelling and structural relationships. Eur. J. Biochem., 187, 341-352. (Pubitemid 20040393)
    • (1990) European Journal of Biochemistry , vol.187 , Issue.2 , pp. 341-352
    • Messerschmidt, A.1    Huber, R.2
  • 5
    • 0026060726 scopus 로고
    • A structure-derived sequence pattern for the detection of type i copper binding domains in distantly related proteins
    • Ouzounis, C. and Sander, C. (1991) A structure-derived sequence pattern for the detection of type I copper binding domains in distantly related proteins. FEBS Lett., 279, 73-78.
    • (1991) FEBS Lett. , vol.279 , pp. 73-78
    • Ouzounis, C.1    Sander, C.2
  • 6
    • 0038034712 scopus 로고    scopus 로고
    • Combined sequence and structure analysis of the fungal laccase family
    • DOI 10.1002/bit.10681
    • Kumar, S. V. S., Phale, P. S., Durani, S. et al. (2003) Combined sequence and structure analysis of the fungal laccase family. Biotechnol. Bioeng., 83, 386-394. (Pubitemid 36885658)
    • (2003) Biotechnology and Bioengineering , vol.83 , Issue.4 , pp. 386-394
    • Kumar, S.V.S.1    Phale, P.S.2    Durani, S.3    Wangikar, P.P.4
  • 7
    • 24744433115 scopus 로고    scopus 로고
    • Function and molecular evolution of multicopper blue proteins
    • DOI 10.1007/s00018-004-5076-x
    • Nakamura, K. and Go, N. (2005) Function and molecular evolution of multicopper blue proteins. Cell. Mol. Life Sci., 62, 2050-2066. (Pubitemid 41291662)
    • (2005) Cellular and Molecular Life Sciences , vol.62 , Issue.18 , pp. 2050-2066
    • Nakamura, K.1    Go, N.2
  • 8
    • 0030975668 scopus 로고    scopus 로고
    • Structural comparison of cupredoxin domains: Domain recycling to construct proteins with novel functions
    • Murphy, M. E., Lindley, P. F. and Adman, E. T. (1997) Structural comparison of cupredoxin domains: domain recycling to construct proteins with novel functions. Protein Sci., 6, 761-770. (Pubitemid 27154802)
    • (1997) Protein Science , vol.6 , Issue.4 , pp. 761-770
    • Murphy, M.E.P.1    Lindley, P.F.2    Adman, E.T.3
  • 10
    • 0035983821 scopus 로고    scopus 로고
    • Laccase: New functions for an old enzyme
    • DOI 10.1016/S0031-9422(02)00171-1, PII S0031942202001711
    • Mayer, A. M. and Staples, R. C. (2002) Laccase: new functions for an old enzyme. Phytochemistry, 60, 551-565. (Pubitemid 34832184)
    • (2002) Phytochemistry , vol.60 , Issue.6 , pp. 551-565
    • Mayer, A.M.1    Staples, R.C.2
  • 11
    • 0033974765 scopus 로고    scopus 로고
    • Laccases are widespread in bacteria
    • Alexandre, G. and Zhulin, I. B. (2000) Laccases are widespread in bacteria. Trends Biotechnol., 18, 41-42.
    • (2000) Trends Biotechnol. , vol.18 , pp. 41-42
    • Alexandre, G.1    Zhulin, I.B.2
  • 12
    • 0742305629 scopus 로고    scopus 로고
    • Characterization of cDNAs encoding putative laccase-like multicopper oxidases and developmental expression in the tobacco hornworm, Manduca sexta, and the malaria mosquito, Anopheles gambiae
    • DOI 10.1016/j.ibmb.2003.08.003
    • Dittmer, N. T., Suderman, R. J., Jiang, H. et al. (2004) Characterization of cDNAs encoding putative laccase-like multicopper oxidases and developmental expression in the tobacco hornworm, Manduca sexta, and the malaria mosquito, Anopheles gambiae. Insect. Biochem. Mol. Biol., 34, 29-41. (Pubitemid 38157610)
    • (2004) Insect Biochemistry and Molecular Biology , vol.34 , Issue.1 , pp. 29-41
    • Dittmer, N.T.1    Suderman, R.J.2    Jiang, H.3    Zhu, Y.-C.4    Gorman, M.J.5    Kramer, K.J.6    Kanost, M.R.7
  • 13
    • 0025315157 scopus 로고
    • Oxidation of non-phenolic substrates. An expended role for laccase in lignin biodegradation
    • DOI 10.1016/0014-5793(90)80298-W
    • Bourbonnais, R. and Paice, M. G. (1990) Oxidation of non-phenolic substrates. An expanded role for laccase in lignin biodegradation. FEBS Lett., 267, 99-102. (Pubitemid 20211711)
    • (1990) FEBS Letters , vol.267 , Issue.1 , pp. 99-102
    • Bourbonnais, R.1    Paice, M.G.2
  • 14
    • 0015341932 scopus 로고
    • Absence of laccase from yellow-spored mutants of aspergillus nidulans
    • Clutterbuck, A. J. (1972) Absence of laccase from yellow-spored mutants of Aspergillus nidulans. J. Gen. Microbiol., 70, 423-435.
    • (1972) J. Gen. Microbiol. , vol.70 , pp. 423-435
    • Clutterbuck, A.J.1
  • 15
    • 85005358973 scopus 로고
    • Root-rot diseases of hevea brasiliensis. 1. Physiological and biochemical aspects of host aggression
    • Geiger, J.P, Nicole, M., Nandris, D. and Rio, B. (1986) Root-rot diseases of Hevea brasiliensis. 1. Physiological and biochemical aspects of host aggression. Eur. J. Forest Pathol., 16, 22-37.
    • (1986) Eur. J. Forest Pathol. , vol.16 , pp. 22-37
    • Geiger J.P Nicole, M.1    Nandris, D.2    Rio, B.3
  • 16
    • 0027139074 scopus 로고
    • The role of of laccase in lignification
    • O'Malley, D. M., Whetten, R., Bao, W. et al. (1993) The role of of laccase in lignification. Plant J., 4, 751-757.
    • (1993) Plant J. , vol.4 , pp. 751-757
    • O'Malley, D.M.1    Whetten, R.2    Bao, W.3
  • 18
    • 33746142419 scopus 로고    scopus 로고
    • Industrial and biotechnological applications of laccases: A review
    • DOI 10.1016/j.biotechadv.2006.04.003, PII S0734975006000619
    • Rodriguez Couto, S. and Toca Herrera, J. L. (2006) Industrial and biotechnological applications of laccases: a review. Biotechnol. Adv., 24, 500-513. (Pubitemid 44082015)
    • (2006) Biotechnology Advances , vol.24 , Issue.5 , pp. 500-513
    • Rodriguez Couto, S.1    Toca Herrera, J.L.2
  • 19
    • 33646154205 scopus 로고    scopus 로고
    • Laccases: Blue enzymes for green chemistry
    • Riva, S. (2006) Laccases: blue enzymes for green chemistry. Trends Biotechnol., 24, 219-226.
    • (2006) Trends Biotechnol. , vol.24 , pp. 219-226
    • Riva, S.1
  • 20
    • 0242559061 scopus 로고    scopus 로고
    • Oxidizing enzymes as biocatalysts
    • DOI 10.1016/j.tibtech.2003.10.006
    • Burton, S. G. (2003) Oxidizing enzymes as biocatalysts. Trends Biotechnol., 21, 543-549. (Pubitemid 37415006)
    • (2003) Trends in Biotechnology , vol.21 , Issue.12 , pp. 543-549
    • Burton, S.G.1
  • 21
    • 58149381901 scopus 로고    scopus 로고
    • Engineering and applications of fungal laccases for organic synthesis
    • Kunamneni, A., Camarero, S., Garcia-Burgos, C. et al. (2008) Engineering and Applications of fungal laccases for organic synthesis. Microb. Cell Fact., 7, 32.
    • (2008) Microb. Cell Fact. , vol.7 , pp. 32
    • Kunamneni, A.1    Camarero, S.2    Garcia-Burgos, C.3
  • 22
    • 33751255103 scopus 로고    scopus 로고
    • Dwarf-A data warehouse system for analyzing protein families
    • Fischer, M., Thai, Q. K., Grieb, M. et al. (2006) DWARF-A data warehouse system for analyzing protein families. BMC Bioinformatics, 7, 495.
    • (2006) BMC Bioinformatics , vol.7 , pp. 495
    • Fischer, M.1    Thai, Q.K.2    Grieb, M.3
  • 23
    • 33646268426 scopus 로고    scopus 로고
    • Phylogenetic comparison and classification of laccase and related multicopper oxidase protein sequences
    • Hoegger, P. J., Kilaru, S., James, T. Y. et al. (2006) Phylogenetic comparison and classification of laccase and related multicopper oxidase protein sequences. FEBS J., 273, 2308-2326.
    • (2006) FEBS J. , vol.273 , pp. 2308-2326
    • Hoegger, P.J.1    Kilaru, S.2    James, T.Y.3
  • 24
    • 4344699077 scopus 로고    scopus 로고
    • Characterization of SLAC: A small laccase from Streptomyces coelicolor with unprecedented activity
    • DOI 10.1110/ps.04759104
    • Machczynski, M. C., Vijgenboom, E., Samyn, B. et al. (2004) Characterization of SLAC: a small laccase from Streptomyces coelicolor with unprecedented activity. Protein Sci., 13, 2388-2397. (Pubitemid 39128859)
    • (2004) Protein Science , vol.13 , Issue.9 , pp. 2388-2397
    • Machczynski, M.C.1    Vijgenboom, E.2    Samyn, B.3    Canters, G.W.4
  • 28
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J. D., Higgins, D. G. and Gibson, T. J. (1994) CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res., 22, 4673-4680. (Pubitemid 24354800)
    • (1994) Nucleic Acids Research , vol.22 , Issue.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 30
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch, W. and Sander, C. (1983) Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers, 22, 2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 31
    • 0034201441 scopus 로고    scopus 로고
    • Emboss: The european molecular biology open software suite
    • Rice, P., Longden, I. and Bleasby, A. (2000) EMBOSS: the European Molecular Biology Open Software Suite. Trends Genet., 16, 276-277.
    • (2000) Trends Genet. , vol.16 , pp. 276-277
    • Rice, P.1    Longden, I.2    Bleasby, A.3
  • 33
    • 0000120520 scopus 로고    scopus 로고
    • Prodom: Automated clustering of homologous domains
    • Servant, F., Bru, C., Carrere, S. et al. (2002) ProDom: automated clustering of homologous domains. Brief Bioinform., 3, 246-251.
    • (2002) Brief Bioinform. , vol.3 , pp. 246-251
    • Servant, F.1    Bru, C.2    Carrere, S.3
  • 34
    • 0037246592 scopus 로고    scopus 로고
    • The Lipase Engineering Database: A navigation and analysis tool for protein families
    • DOI 10.1093/nar/gkg015
    • Fischer, M. and Pleiss, J. (2003) The Lipase Engineering Database: a navigation and analysis tool for protein families. Nucleic Acids Res., 31, 319-321. (Pubitemid 36150394)
    • (2003) Nucleic Acids Research , vol.31 , Issue.1 , pp. 319-321
    • Fischer, M.1    Pleiss, J.2
  • 35
    • 64549129098 scopus 로고    scopus 로고
    • The pha depolymerase engineering database: A systematic analysis tool for the diverse family of polyhydroxyalkanoate (pha) depolymerases
    • Knoll, M., Hamm, T. M., Wagner, F., Martinez, V. and Pleiss, J. (2009) The PHA Depolymerase Engineering Database: a systematic analysis tool for the diverse family of polyhydroxyalkanoate (PHA) depolymerases. BMC Bioinformatics, 10, 89.
    • (2009) BMC Bioinformatics , vol.10 , pp. 89
    • Knoll, M.1    Hamm, T.M.2    Wagner, F.3    Martinez, V.4    Pleiss, J.5
  • 36
    • 73449127232 scopus 로고    scopus 로고
    • The cytochrome p450 engineering database: Integration of biochemical properties
    • Sirim, D., Wagner, F., Lisitsa, A. and Pleiss, J. (2009) The Cytochrome P450 Engineering Database: integration of biochemical properties. BMC Biochem., 10, 27.
    • (2009) BMC Biochem. , vol.10 , pp. 27
    • Sirim, D.1    Wagner, F.2    Lisitsa, A.3    Pleiss, J.4
  • 37
    • 61449134084 scopus 로고    scopus 로고
    • Identification of selectivitydetermining residues in cytochrome p450 monooxygenases: A systematic analysis of the substrate recognition site 5
    • Seifert, A. and Pleiss, J. (2009) Identification of selectivitydetermining residues in cytochrome P450 monooxygenases: a systematic analysis of the substrate recognition site 5. Proteins, 74, 1028-1035.
    • (2009) Proteins , vol.74 , pp. 1028-1035
    • Seifert, A.1    Pleiss, J.2
  • 38
    • 65549113338 scopus 로고    scopus 로고
    • Rational design of a minimal and highly enriched cyp102a1 mutant library with improved regio-, stereo-And chemoselectivity
    • Seifert, A., Vomund, S., Grohmann, K. et al. (2009) Rational design of a minimal and highly enriched CYP102A1 mutant library with improved regio-, stereo-And chemoselectivity. Chembiochem, 10, 853-861.
    • (2009) Chembiochem , vol.10 , pp. 853-861
    • Seifert, A.1    Vomund, S.2    Grohmann, K.3
  • 39
    • 0037020063 scopus 로고    scopus 로고
    • Crystal structure of a laccase from the fungus trametes versicolor at 1.90-A resolution containing a full complement of coppers
    • Piontek, K., Antorini, M. and Choinowski, T. (2002) Crystal structure of a laccase from the fungus Trametes versicolor at 1.90-A resolution containing a full complement of coppers. J. Biol. Chem., 277, 37663-37669.
    • (2002) J. Biol. Chem. , vol.277 , pp. 37663-37669
    • Piontek, K.1    Antorini, M.2    Choinowski, T.3


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