메뉴 건너뛰기




Volumn 64, Issue 2, 2000, Pages 261-267

An Organic Solvent Resistant Tyrosinase from Streptomyces sp. REN-21: Purification and Characterization

Author keywords

Organic solvent resistance; Purification; Streptomyces; Tyrosinase

Indexed keywords

METAL; MONOPHENOL MONOOXYGENASE; ORGANIC COMPOUND; SOLVENT;

EID: 0034133890     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.64.261     Document Type: Article
Times cited : (33)

References (33)
  • 2
    • 0001064298 scopus 로고
    • Copper monooxygenases: Tyrosinase and dopamine βmonooxygenase
    • Edited by Sigel, H., Marcel Dekker, New York, pp
    • Lerch, K., Copper monooxygenases: tyrosinase and dopamine βmonooxygenase. In “Metal Ions in Biological Systems”, vol. 13, Edited by Sigel, H., Marcel Dekker, New York, pp. 143-184 (1981).
    • (1981) Metal Ions in Biological Systems , vol.13 , pp. 143-184
    • Lerch, K.1
  • 3
    • 0023629886 scopus 로고
    • Catalytic oxidation of 2-aminophenols and ortho hydroxylation of aromatic amines by tyrosinase
    • Toussaint, O. and Lerch, K., Catalytic oxidation of 2-aminophenols and ortho hydroxylation of aromatic amines by tyrosinase. Biochemistry, 26, 8567-8571 (1987).
    • (1987) Biochemistry , vol.26 , pp. 8567-8571
    • Toussaint, O.1    Lerch, K.2
  • 4
    • 0027164650 scopus 로고
    • Melanin production by Rhizo-bium meliloti GR4 is linked to nonsymbiotic plasmid pRmeGR4b: Cloning, sequencing, and expression of the tyrosinase gene mepA
    • Mercado-Bianco, J., Garcia, F., Fernandez-Lopez, M., and Olivares J., Melanin production by Rhizo-bium meliloti GR4 is linked to nonsymbiotic plasmid pRmeGR4b: cloning, sequencing, and expression of the tyrosinase gene mepA. J. Bacteriol., 175, 5403-5410 (1993).
    • (1993) J. Bacteriol. , vol.175 , pp. 5403-5410
    • Mercado-Bianco, J.1    Garcia, F.2    Fernandez-Lopez, M.3    Olivares, J.4
  • 5
    • 0022240091 scopus 로고
    • The nucleotide sequence of the tyrosinase gene from Streptomyces antibioticus and characterization of the gene product
    • Bernan, V., Filpula, D., Herber, W., Bibb, M., and Katz, E., The nucleotide sequence of the tyrosinase gene from Streptomyces antibioticus and characterization of the gene product. Gene, 37, 101-110(1985).
    • (1985) Gene , vol.37 , pp. 101-110
    • Bernan, V.1    Filpula, D.2    Herber, W.3    Bibb, M.4    Katz, E.5
  • 6
    • 0022397908 scopus 로고
    • Primary structure of tyrosinase from Streptomyces glau-cescens
    • Huber, M., Hintermann, G., and Lerch, K., Primary structure of tyrosinase from Streptomyces glau-cescens. Biochemistry, 24, 6038-6044 (1985).
    • (1985) Biochemistry , vol.24 , pp. 6038-6044
    • Huber, M.1    Hintermann, G.2    Lerch, K.3
  • 7
    • 0027718095 scopus 로고
    • Cloning, sequence and expression of the tyrosinase gene from Streptomyces lavendulae MA406 A-l
    • Kawamoto, S., Nakamura, M., and Yashima, S., Cloning, sequence and expression of the tyrosinase gene from Streptomyces lavendulae MA406 A-l. J. Ferment. Bioeng., 76, 345-355 (1993).
    • (1993) J. Ferment. Bioeng. , vol.76 , pp. 345-355
    • Kawamoto, S.1    Nakamura, M.2    Yashima, S.3
  • 8
    • 0029994563 scopus 로고    scopus 로고
    • Cloning and sequence analysis of the highly expressed melanin-synthesizing gene operon from Streptomyces castaneoglobisporus
    • Ikeda, K., Masujima, T., Suzuki, K., and Sugiyama, M., Cloning and sequence analysis of the highly expressed melanin-synthesizing gene operon from Streptomyces castaneoglobisporus. Appl. Microbiol. Biotechnol., 45, 80-85 (1996).
    • (1996) Appl. Microbiol. Biotechnol. , vol.45 , pp. 80-85
    • Ikeda, K.1    Masujima, T.2    Suzuki, K.3    Sugiyama, M.4
  • 9
    • 0028933613 scopus 로고
    • Molecular cloning and nucleotide sequence of the protyrosinase gene, melO, from Aspergillus oryzae and expression of the gene in yeast cells
    • Fujita, Y., Uraga, Y., and Ichisima, E., Molecular cloning and nucleotide sequence of the protyrosinase gene, melO, from Aspergillus oryzae and expression of the gene in yeast cells. Biochim. Biophys. Acta, 1261, 151-154 (1995).
    • (1995) Biochim. Biophys. Acta , vol.1261 , pp. 151-154
    • Fujita, Y.1    Uraga, Y.2    Ichisima, E.3
  • 10
    • 0024971467 scopus 로고
    • Isolation and characterization of the tyrosinase gene from Neurospora crassa
    • Kupper, U., Niedermann, D. M., Travaglini, G., and Lerch, K., Isolation and characterization of the tyrosinase gene from Neurospora crassa. J. Biol. Chem., 264, 17250-17258 (1989).
    • (1989) J. Biol. Chem. , vol.264 , pp. 17250-17258
    • Kupper, U.1    Niedermann, D.M.2    Travaglini, G.3    Lerch, K.4
  • 11
    • 0026446806 scopus 로고
    • Cloning and sequencing of the cDNA encoding tyrosinase of the Japanese pond frog, Rana nigromaculata
    • Takase, M., Miura, I., Nakata, A., Takeuchi, T., and Nishioka, M., Cloning and sequencing of the cDNA encoding tyrosinase of the Japanese pond frog, Rana nigromaculata. Gene, 121, 359-363 (1992).
    • (1992) Gene , vol.121 , pp. 359-363
    • Takase, M.1    Miura, I.2    Nakata, A.3    Takeuchi, T.4    Nishioka, M.5
  • 12
    • 0023783667 scopus 로고
    • Sequence analysis of mouse tyrosinase cDNA and the effect of melanotropin on its gene expression
    • Kwon, B. S., Wakulchik, M., Haq, A. K., Halaban, R., and Kestler, D., Sequence analysis of mouse tyrosinase cDNA and the effect of melanotropin on its gene expression. Biochem. Biophys. Res. Com-mun., 153, 1301-1309 (1988).
    • (1988) Biochem. Biophys. Res. Com-Mun. , vol.153 , pp. 1301-1309
    • Kwon, B.S.1    Wakulchik, M.2    Haq, A.K.3    Halaban, R.4    Kestler, D.5
  • 13
    • 0038523701 scopus 로고
    • Functional analysis of alternatively spliced tyrosinase gene transcripts
    • Muller, G., Ruppert, S., Schmid, E., and Schutz, G., Functional analysis of alternatively spliced tyrosinase gene transcripts. EMBO J., 7, 2723-2730 (1988).
    • (1988) EMBO J. , vol.7 , pp. 2723-2730
    • Muller, G.1    Ruppert, S.2    Schmid, E.3    Schutz, G.4
  • 14
    • 0013587129 scopus 로고
    • Isolation and sequence of a cDNA clone for human tyrosinase that maps at the mouse c-albino locus
    • Kwon, B. S., Haq, A. K., Pomerantz, S. H., and Halaban, R., Isolation and sequence of a cDNA clone for human tyrosinase that maps at the mouse c-albino locus. Proc. Natl. Acad. Sci. USA, 84, 7473-7477 (1987).
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 7473-7477
    • Kwon, B.S.1    Haq, A.K.2    Pomerantz, S.H.3    Halaban, R.4
  • 15
    • 0026070465 scopus 로고
    • Organization and nucleotide sequences of the human tyrosinase gene and a truncated tyrosinase-related segment
    • Giebel, L. B., Strunk, K. M., and Spritz, R. A., Organization and nucleotide sequences of the human tyrosinase gene and a truncated tyrosinase-related segment. Genomics, 9, 435-445 (1991).
    • (1991) Genomics , vol.9 , pp. 435-445
    • Giebel, L.B.1    Strunk, K.M.2    Spritz, R.A.3
  • 16
    • 0021277975 scopus 로고
    • 3.2 A structure of the copper-containing, oxygen-carrying protein Panulius interruptus hae-mocyanin
    • Gaykema, W. P. J., Hoi, W. G. J., Vereijken, J. M., Soeter, N. M., Bak, H. J., and Beintema, J. J., 3.2 A structure of the copper-containing, oxygen-carrying protein Panulius interruptus hae-mocyanin. Nature, 309, 23-29 (1984).
    • (1984) Nature , vol.309 , pp. 23-29
    • Gaykema, W.P.J.1    Hoi, W.G.J.2    Vereijken, J.M.3    Soeter, N.M.4    Bak, H.J.5    Beintema, J.J.6
  • 17
    • 0023385298 scopus 로고
    • Polymerization of phenols catalyzed by peroxidase in nonaqueous media
    • Dordick, J. S., Marietta, M. A., and Klibanov, A. M., Polymerization of phenols catalyzed by peroxidase in nonaqueous media. Biotechnol. Bioeng., 30, 31-36 (1987).
    • (1987) Biotechnol. Bioeng. , vol.30 , pp. 31-36
    • Dordick, J.S.1    Marietta, M.A.2    Klibanov, A.M.3
  • 18
    • 0001650501 scopus 로고
    • Oxidation of aromatic compounds in organic solvents with laccase from Trametes versicolor
    • Milstein, O., Nicklas, B., and Hiittermann, A., Oxidation of aromatic compounds in organic solvents with laccase from Trametes versicolor. Appl. Microbiol. Biotechnol., 31, 70-74 (1989).
    • (1989) Appl. Microbiol. Biotechnol. , vol.31 , pp. 70-74
    • Milstein, O.1    Nicklas, B.2    Hiittermann, A.3
  • 19
    • 0000985708 scopus 로고
    • Synthesis of a new family of phenol resin by enzymatic oxidative polymerization
    • Uyama, H., Kurioka, H., Kaneko, I., and Kobayashi, S., Synthesis of a new family of phenol resin by enzymatic oxidative polymerization. Chem. Lett., 423-426 (1994).
    • (1994) Chem. Lett. , pp. 423-426
    • Uyama, H.1    Kurioka, H.2    Kaneko, I.3    Kobayashi, S.4
  • 21
    • 0000331319 scopus 로고
    • Peroxidase-catalyzed oxidative polymerization of cresols to a new family of polyphenols
    • Uyama, H., Kurioka, H., Sugihara, J., Komatsu, I., and Kobayashi, S., Peroxidase-catalyzed oxidative polymerization of cresols to a new family of polyphenols. Bull. Chem. Soc. Jpn., 68, 3209-3214 (1995).
    • (1995) Bull. Chem. Soc. Jpn. , vol.68 , pp. 3209-3214
    • Uyama, H.1    Kurioka, H.2    Sugihara, J.3    Komatsu, I.4    Kobayashi, S.5
  • 22
    • 0029344859 scopus 로고
    • Controlled free-radical polymerization of phenol derivatives by enzyme-catalyzed reactions in organic solvents
    • Ayyagari, M. S., Marx, K. A., Tripathy, S. K., Akkara, J. A., and Kaplan, D. L., Controlled free-radical polymerization of phenol derivatives by enzyme-catalyzed reactions in organic solvents. Macromolecules, 28, 5192-5197 (1995).
    • (1995) Macromolecules , vol.28 , pp. 5192-5197
    • Ayyagari, M.S.1    Marx, K.A.2    Tripathy, S.K.3    Akkara, J.A.4    Kaplan, D.L.5
  • 23
    • 0000501083 scopus 로고    scopus 로고
    • Enzymatic synthesis and thermal properties of a new class of polyphenol
    • Uyama, H., Kurioka, H., Sugihara, J., and Kobayashi, S., Enzymatic synthesis and thermal properties of a new class of polyphenol. Bull. Chem. Soc. Jpn., 69, 189-193 (1996).
    • (1996) Bull. Chem. Soc. Jpn. , vol.69 , pp. 189-193
    • Uyama, H.1    Kurioka, H.2    Sugihara, J.3    Kobayashi, S.4
  • 24
    • 0030574980 scopus 로고    scopus 로고
    • Novel synthetic pathway to a poly(Phenylene oxide). Lac-case-catalyzed oxidative polymerization of syringic acid
    • Ikeda, R., Uyama, H., and Kobayashi, S., Novel synthetic pathway to a poly(phenylene oxide). Lac-case-catalyzed oxidative polymerization of syringic acid. Macromolecules, 29, 3053-3054 (1996).
    • (1996) Macromolecules , vol.29 , pp. 3053-3054
    • Ikeda, R.1    Uyama, H.2    Kobayashi, S.3
  • 25
    • 0030379974 scopus 로고    scopus 로고
    • Enzymatic oxidative polymerization of 2,6-dimethylphenol
    • Ikeda, R., Sugihara, J., Uyama, H., and Kobayashi, S., Enzymatic oxidative polymerization of 2,6-dimethylphenol. Macromolecules, 29, 8702-8705 (1996).
    • (1996) Macromolecules , vol.29 , pp. 8702-8705
    • Ikeda, R.1    Sugihara, J.2    Uyama, H.3    Kobayashi, S.4
  • 26
    • 0031646273 scopus 로고    scopus 로고
    • Chemoselective polymerization of a phenol derivative having a methacryl group by peroxidase catalyst
    • Uyama, H., Lohavisavapanich, C., Ikeda, R., and Kobayashi, S., Chemoselective polymerization of a phenol derivative having a methacryl group by peroxidase catalyst. Macromolecules, 31, 554-556 (1998).
    • (1998) Macromolecules , vol.31 , pp. 554-556
    • Uyama, H.1    Lohavisavapanich, C.2    Ikeda, R.3    Kobayashi, S.4
  • 27
    • 0042647535 scopus 로고    scopus 로고
    • Synthesis of a new class of polyphenols by peroxidase-catalyzed polymerization
    • Kobayashi, S. and Uyama, EL, Synthesis of a new class of polyphenols by peroxidase-catalyzed polymerization. Bio Industry (in Japanese), 15, 44-51 (1998).
    • (1998) Bio Industry (In Japanese) , vol.15 , pp. 44-51
    • Kobayashi, S.1    Uyama, E.L.2
  • 28
    • 0015239523 scopus 로고
    • The tyrosinases of mouse melanoma. Isolation and molecular properties
    • Burnett, J. B., The tyrosinases of mouse melanoma. Isolation and molecular properties. J. Biol. Chem., 246, 3079-3091 (1971).
    • (1971) J. Biol. Chem. , vol.246 , pp. 3079-3091
    • Burnett, J.B.1
  • 29
    • 0023664635 scopus 로고
    • Sequence from picomole quantities of proteins electroblotted on to polyvinylidene difluoride membranes
    • Matsudaira, P., Sequence from picomole quantities of proteins electroblotted on to polyvinylidene difluoride membranes. J. Biol. Chem., 262, 10035-10038 (1987).
    • (1987) J. Biol. Chem. , vol.262 , pp. 10035-10038
    • Matsudaira, P.1
  • 31
    • 0015515423 scopus 로고
    • Purification and characterization of a tyrosinase from Streptomyces glau-cescens
    • Lerch, K. and Ettlinger, L., Purification and characterization of a tyrosinase from Streptomyces glau-cescens. Eur. J. Biochem., 31, 427-437 (1972).
    • (1972) Eur. J. Biochem. , vol.31 , pp. 427-437
    • Lerch, K.1    Ettlinger, L.2
  • 32
    • 0021867510 scopus 로고
    • Extracellular tyrosinase from Streptomyces sp. KY-453: Purification and some enzymatic properties
    • Yoshimoto, T., Ymamoto, K., and Tsuru, D., Extracellular tyrosinase from Streptomyces sp. KY-453: Purification and some enzymatic properties. J. Biochem., 91, 1747-1754 (1985).
    • (1985) J. Biochem. , vol.91 , pp. 1747-1754
    • Yoshimoto, T.1    Ymamoto, K.2    Tsuru, D.3
  • 33
    • 0000411077 scopus 로고
    • The multiple forms of mushroom tyrosinase: Purification and molecular properties of the enzymes
    • Bouchilloux, S., McMahill, P., and Mason, H. S., The multiple forms of mushroom tyrosinase: Purification and molecular properties of the enzymes. J. Biol. Chem., 238, 1699-1707 (1963).
    • (1963) J. Biol. Chem. , vol.238 , pp. 1699-1707
    • Bouchilloux, S.1    Mc Mahill, P.2    Mason, H.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.