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Volumn 1814, Issue 12, 2011, Pages 1974-1983

Catalytic oxidation of o-aminophenols and aromatic amines by mushroom tyrosinase

Author keywords

Aromatic amine; Aromatic o diamines; Catalytic constant; Michaelis constant; o aminophenols; Tyrosinase

Indexed keywords

2 AMINOPHENOL; 2 DIAMINE; AROMATIC AMINE; MONOPHENOL MONOOXYGENASE; UNCLASSIFIED DRUG;

EID: 81755184325     PISSN: 15709639     EISSN: 18781454     Source Type: Journal    
DOI: 10.1016/j.bbapap.2011.07.015     Document Type: Article
Times cited : (13)

References (37)
  • 5
    • 0034595323 scopus 로고    scopus 로고
    • How does tyrosinase work? Recent insights from model chemistry and structural biology
    • DOI 10.1002/(SICI)1521-3773(20000502)39:9<1591::AID-ANIE1591>3.0. CO;2-H
    • H. Decker, R. Dillinger, and F. Tuczek How does tyrosinase work? Recent insights from model chemistry and structural biology Angew. Chem. Int. Ed. 39 2000 1591 1595 (Pubitemid 30304081)
    • (2000) Angewandte Chemie - International Edition , vol.39 , Issue.9 , pp. 1591-1595
    • Decker, H.1    Dillinger, R.2    Tuczek, F.3
  • 6
    • 0031760504 scopus 로고    scopus 로고
    • Crystal structure of a plant catechol oxidase containing a dicopper center
    • DOI 10.1038/4193
    • T. Klabunde, C. Eicken, J.C. Sacchettini, and B. Krebs Crystal structure of a plant catechol oxidase containing a dicopper center Nat. Struct. Biol. 5 1998 1084 1090 (Pubitemid 28546272)
    • (1998) Nature Structural Biology , vol.5 , Issue.12 , pp. 1084-1090
    • Klabunde, T.1    Eicken, C.2    Sacchettini, J.C.3    Krebs, B.4
  • 7
    • 33646827679 scopus 로고    scopus 로고
    • Crystallographic evidence that the dinuclear copper center of tyrosinase is flexible during catalysis
    • DOI 10.1074/jbc.M509785200
    • Y. Matoba, T. Kumagai, A. Yamamoto, H. Yoshitsu, and M. Sugiyama Crystallographic evidence that the dinuclear copper center of tyrosinase is flexible during catalysis J. Biol. Chem. 281 2006 8981 8990 (Pubitemid 43848005)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.13 , pp. 8981-8990
    • Matoba, Y.1    Kumagai, T.2    Yamamoto, A.3    Yoshitsu, H.4    Sugiyama, M.5
  • 10
    • 0023629886 scopus 로고
    • Catalytic oxidation of 2-aminophenols and ortho hydroxylation of aromatic amines by tyrosinase
    • O. Toussaint, and K. Lerch Catalytic oxidation of 2-aminophenols and ortho hydroxylation of aromatic amines by tyrosinase Biochemistry 26 1987 8567 8571 (Pubitemid 18040784)
    • (1987) Biochemistry , vol.26 , Issue.26 , pp. 8567-8571
    • Toussaint, O.1    Lerch, K.2
  • 13
    • 0024288948 scopus 로고
    • Inhibition of mushroom tyrosinase by 3-amino-l-tyrosine: Molecular probing of the active site of the enzyme
    • F. Maddaluno, and K.F. Faull Inhibition of mushroom tyrosinase by 3-amino-l-tyrosine: molecular probing of the active site of the enzyme Experientia 44 1988 885 887
    • (1988) Experientia , vol.44 , pp. 885-887
    • Maddaluno, F.1    Faull, K.F.2
  • 14
    • 3242811929 scopus 로고    scopus 로고
    • Interaction of mushroom tyrosinase with aromatic amines, o-diamines and o-aminophenols
    • DOI 10.1016/j.bbagen.2004.04.013, PII S0304416504001096
    • B. Gasowska, P. Kafarski, and H. Wojtasek Interaction of mushroom tyrosinase with aromatic amines, o-diamines and o-aminophenols Biochim. Biophys. Acta 1673 2004 170 177 (Pubitemid 38981770)
    • (2004) Biochimica et Biophysica Acta - General Subjects , vol.1673 , Issue.3 , pp. 170-177
    • Gasowska, B.1    Kafarski, P.2    Wojtasek, H.3
  • 16
    • 0026645649 scopus 로고
    • Calibration of a Clark-type oxygen electrode by tyrosinase-catalyzed oxidation of a 4-tert-butylcatechol
    • J.N. Rodriguez-Lopez, J.R. Ros-Martinez, R. Varon, and F. Garcia-Canovas Calibration of a Clark-type oxygen electrode by tyrosinase-catalyzed oxidation of a 4-tert-butylcatechol Anal. Biochem. 202 1992 356 360
    • (1992) Anal. Biochem. , vol.202 , pp. 356-360
    • Rodriguez-Lopez, J.N.1    Ros-Martinez, J.R.2    Varon, R.3    Garcia-Canovas, F.4
  • 18
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of proteins utilising the principle of protein-dye binding
    • M.M. Bradford A rapid and sensitive method for the quantification of microgram quantities of proteins utilising the principle of protein-dye binding Anal. Biochem. 72 1976 248 254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 21
    • 81355165668 scopus 로고    scopus 로고
    • Jandel Scientific: Core Madera
    • Jandel Scientific. Sigma Plot 9.0 for Windows™ 2006 Jandel Scientific: Core Madera
    • (2006) Sigma Plot 9.0 for Windows™
  • 22
    • 77954456405 scopus 로고    scopus 로고
    • New features of the steady-state rate related with the initial concentration of substrate in the diphenolase and monophenolase activities of tyrosinase
    • J.L. Muñoz-Muñoz, F. Garcia-Molina, R. Varon, J. Tudela, F. Garcia-Canovas, and J.N. Rodriguez-Lopez New features of the steady-state rate related with the initial concentration of substrate in the diphenolase and monophenolase activities of tyrosinase J. Math. Chem. 48 2010 347 362
    • (2010) J. Math. Chem. , vol.48 , pp. 347-362
    • Muñoz-Muñoz, J.L.1    Garcia-Molina, F.2    Varon, R.3    Tudela, J.4    Garcia-Canovas, F.5    Rodriguez-Lopez, J.N.6
  • 24
    • 0000498085 scopus 로고    scopus 로고
    • Functional modelling of tyrosinase. Mechanism of phenol ortho hydroxylation by dinuclear copper complexes
    • L. Casella, E. Monzani, M. Gulloti, D. Cavagino, G. Cerina, L. Santagostini, and R. Ugo Functional modelling of tyrosinase. Mechanism of phenol ortho hydroxylation by dinuclear copper complexes Inorg. Chem. 35 1996 7516 7625
    • (1996) Inorg. Chem. , vol.35 , pp. 7516-7625
    • Casella, L.1    Monzani, E.2    Gulloti, M.3    Cavagino, D.4    Cerina, G.5    Santagostini, L.6    Ugo, R.7
  • 29
    • 0032524470 scopus 로고    scopus 로고
    • 4-hydroxyanisole: The most suitable monophenolic substrate for determining spectrophotometrically the monophenolase activity of polyphenol oxidase from fruits and vegetables
    • DOI 10.1006/abio.1998.2598
    • J.C. Espin, J. Tudela, and F. Garcia-Canovas 4-Hydroxyanisole: the most suitable monophenolic substrate for determining spectrophotometrically the monophenolase activity of polyphenol oxidase from fruits and vegetables Anal. Biochem. 259 1998 118 126 (Pubitemid 28247059)
    • (1998) Analytical Biochemistry , vol.259 , Issue.1 , pp. 118-126
    • Espin, J.C.1    Tudela, J.2    Garcia-Canovas, F.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.