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Volumn 62, Issue 7, 2010, Pages 539-547

Suicide inactivation of the diphenolase and monophenolase activities of Tyrosinase

Author keywords

Inactivation; Mechanism based inhibitors; O diphenols; Poly phenol oxidase; Suicide

Indexed keywords

COPPER; HYDROGEN PEROXIDE; HYDROXYL GROUP; MONOPHENOL MONOOXYGENASE; NUCLEOPHILE; PEROXIDE; QUINONE DERIVATIVE; SUICIDE SUBSTRATE; OXIDOREDUCTASE; PHENOL DERIVATIVE;

EID: 77955914529     PISSN: 15216543     EISSN: 15216551     Source Type: Journal    
DOI: 10.1002/iub.348     Document Type: Review
Times cited : (60)

References (37)
  • 1
    • 0002281576 scopus 로고    scopus 로고
    • The chemistry of melanins and related metabolites
    • (Nordlund, J. J.,Boissy, R. E.,Hearing, V. J.,King, R. A., and Ortonne, J. P., eds.) , Oxford University Press, Oxford
    • Prota, G., d'Ischia, M., and Napolitano, A. (1998) The chemistry of melanins and related metabolites. In The Pigmentary System, Physiology and Pathology. (Nordlund, J. J.,Boissy, R. E.,Hearing, V. J.,King, R. A., and Ortonne, J. P., eds.). pp. 307-332, Oxford University Press, Oxford.
    • (1998) The Pigmentary System, Physiology and Pathology , pp. 307-332
    • Prota, G.1    D'Ischia, M.2    Napolitano, A.3
  • 2
    • 67649216556 scopus 로고    scopus 로고
    • Physiological factors that regulate skin pigmentation
    • Yamaguchi, Y. and Hearing, V. J. (2009) Physiological factors that regulate skin pigmentation. Biofactors 35, 193-199.
    • (2009) Biofactors , vol.35 , pp. 193-199
    • Yamaguchi, Y.1    Hearing, V.J.2
  • 4
    • 0001639883 scopus 로고
    • Reaction inactivation of tyrosinase
    • (King, T. E.,Mason, H. S., and Morrison, M., eds.) , Pergamon Press, New York
    • Dietler, C. and Lerch, K. (1982) Reaction inactivation of tyrosinase. In Oxidases and Related Redox Systems. (King, T. E.,Mason, H. S., and Morrison, M., eds.). pp. 305-317, Pergamon Press, New York.
    • (1982) Oxidases and Related Redox Systems , pp. 305-317
    • Dietler, C.1    Lerch, K.2
  • 10
    • 0018184565 scopus 로고
    • Nature of tyrosinase inactivation in melanosomes
    • Seiji, M., Sasaki, M., and Tomita, Y. (1978) Nature of tyrosinase inactivation in melanosomes. Tohoku J. Exp. Med. 125, 233-245.
    • (1978) Tohoku J. Exp. Med. , vol.125 , pp. 233-245
    • Seiji, M.1    Sasaki, M.2    Tomita, Y.3
  • 11
    • 0000703969 scopus 로고
    • Properties of o-diphenol:O2 oxidoreductase from Musa cavendishii
    • Padron, M. P., Lozano, J. A., and Gonzalez, A. G. (1975) Properties of o-diphenol:O2 oxidoreductase from Musa cavendishii. Phytochemistry 14, 1959-1963.
    • (1975) Phytochemistry , vol.14 , pp. 1959-1963
    • Padron, M.P.1    Lozano, J.A.2    Gonzalez, A.G.3
  • 14
    • 0028930481 scopus 로고
    • Mechanism-based enzyme inactivators
    • Silverman, R. B. (1995) Mechanism-based enzyme inactivators. Methods Enzymol. 249, 240-283.
    • (1995) Methods Enzymol. , vol.249 , pp. 240-283
    • Silverman, R.B.1
  • 17
    • 33645980647 scopus 로고    scopus 로고
    • A critical evaluation of the experimental design of studies of mechanism based enzyme inhibition with implications for in vitro-in vivo extrapolation
    • Ghanbari, F., Rowland-Yeo, K., Bloomer, J. C., Clarke, S. E., Lennard, M. S., Tucker, G. T., and Rostami-Hodjegan, A. (2006) A critical evaluation of the experimental design of studies of mechanism based enzyme inhibition with implications for in vitro-in vivo extrapolation. Curr. Drug Metab. 7, 315-334.
    • (2006) Curr. Drug Metab. , vol.7 , pp. 315-334
    • Ghanbari, F.1    Rowland-Yeo, K.2    Bloomer, J.C.3    Clarke, S.E.4    Lennard, M.S.5    Tucker, G.T.6    Rostami-Hodjegan, A.7
  • 19
    • 33646827679 scopus 로고    scopus 로고
    • Crystallographic evidence that the dinuclear copper center of tyrosinase is flexible during catalysis
    • Matoba, Y., Kumagai, T., Yamamoto, A., Yoshitsu, H., and Sugiyama, M. (2006) Crystallographic evidence that the dinuclear copper center of tyrosinase is flexible during catalysis. J. Biol. Chem. 281, 8981-8990.
    • (2006) J. Biol. Chem. , vol.281 , pp. 8981-8990
    • Matoba, Y.1    Kumagai, T.2    Yamamoto, A.3    Yoshitsu, H.4    Sugiyama, M.5
  • 21
    • 33751158263 scopus 로고
    • Coligand-dependent shifts in charge-distribution for copper-complexes containing 3,5-di-tert-butylcatecholate and 3,5-di-tert-butylsemiquinonate ligands
    • Speier, G., Tisza, S., Tyeklar, Z., Lange, C. W., and Pierpont, C. G. (1994) Coligand-dependent shifts in charge-distribution for copper-complexes containing 3,5-di-tert-butylcatecholate and 3,5-di-tert-butylsemiquinonate ligands. Inorg. Chem. 33, 2041-2045.
    • (1994) Inorg. Chem. , vol.33 , pp. 2041-2045
    • Speier, G.1    Tisza, S.2    Tyeklar, Z.3    Lange, C.W.4    Pierpont, C.G.5
  • 22
    • 38449116139 scopus 로고    scopus 로고
    • The mechanism of suicide-inactivation of tyrosinase: A substrate structure investigation
    • Land, E. J., Ramsden, C. A., and Riley, P. A. (2007) The mechanism of suicide-inactivation of tyrosinase: a substrate structure investigation. Tohoku J. Exp. Med. 212, 341-348.
    • (2007) Tohoku J. Exp. Med. , vol.212 , pp. 341-348
    • Land, E.J.1    Ramsden, C.A.2    Riley, P.A.3
  • 23
    • 33746291588 scopus 로고    scopus 로고
    • The first crystal structure of tyrosinase: All questions answered?
    • Decker, H., Schweikardt, T., and Tuczek, F. (2006) The first crystal structure of tyrosinase: all questions answered? Angew. Chem. Int. Ed. 45, 4546-4550.
    • (2006) Angew. Chem. Int. Ed. , vol.45 , pp. 4546-4550
    • Decker, H.1    Schweikardt, T.2    Tuczek, F.3
  • 24
    • 77949272214 scopus 로고    scopus 로고
    • Structural and mechanistic insights into the oxy form of tyrosinase from molecular dynamics simulations
    • Deeth, R. J. and Diedrich, C. (2010) Structural and mechanistic insights into the oxy form of tyrosinase from molecular dynamics simulations. J. Biol. Inorg. Chem. 15, 117-129.
    • (2010) J. Biol. Inorg. Chem. , vol.15 , pp. 117-129
    • Deeth, R.J.1    Diedrich, C.2
  • 25
    • 0000273832 scopus 로고
    • Enzymatic browning of fruits. III. Kinetics of the reaction inactivation of polyphenol oxidase
    • Ingraham, L. L., Corse, J., and Makower, B. (1952) Enzymatic browning of fruits. III. Kinetics of the reaction inactivation of polyphenol oxidase. J. Am. Chem. Soc. 74, 2623-2626.
    • (1952) J. Am. Chem. Soc. , vol.74 , pp. 2623-2626
    • Ingraham, L.L.1    Corse, J.2    Makower, B.3
  • 26
    • 70349290601 scopus 로고    scopus 로고
    • The influence of catechol structure on the suicide-inactivation of tyrosinase
    • Ramsden, C. A., Stratford, M. R. L., and Riley, P. A. (2009) The influence of catechol structure on the suicide-inactivation of tyrosinase. Org. Biomol. Chem. 7, 3388-3390.
    • (2009) Org. Biomol. Chem. , vol.7 , pp. 3388-3390
    • Ramsden, C.A.1    Stratford, M.R.L.2    Riley, P.A.3
  • 27
    • 59849124373 scopus 로고    scopus 로고
    • Evidence consistent with the requirement of cresolase activity for suicide inactivation of tyrosinase
    • Land, E. J., Ramsden, C. A., Riley, P. A., and Stratford, M. R. (2008) Evidence consistent with the requirement of cresolase activity for suicide inactivation of tyrosinase. Tohoku J. Exp. Med. 216, 231-238.
    • (2008) Tohoku J. Exp. Med. , vol.216 , pp. 231-238
    • Land, E.J.1    Ramsden, C.A.2    Riley, P.A.3    Stratford, M.R.4
  • 28
    • 0020688520 scopus 로고
    • Neurospora tyrosinase: Structural, spectroscopic and catalytic properties
    • Lerch, K. (1983) Neurospora tyrosinase: structural, spectroscopic and catalytic properties. Mol. Cell. Biochem. 52, 125-138.
    • (1983) Mol. Cell. Biochem. , vol.52 , pp. 125-138
    • Lerch, K.1
  • 29
    • 0031760504 scopus 로고    scopus 로고
    • Crystal structure of a plant catechol oxidase containing a dicopper center
    • Klabunde, T., Eicken, C., Sachettini, J. C., and Krebs, B. (1998) Crystal structure of a plant catechol oxidase containing a dicopper center. Nat. Struct. Biol. 5, 1084-1090.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 1084-1090
    • Klabunde, T.1    Eicken, C.2    Sachettini, J.C.3    Krebs, B.4
  • 30
    • 0032941536 scopus 로고    scopus 로고
    • Purification and spectroscopic studies on catechol oxidase from Lycopus europaeus and Populus nigra: Evidence for a dinuclear copper center of type and spectroscopic similarities to tyrosinase and hemocyanin
    • Rompel, A., Fisher, H., Meiwes, D., Buldt-Karentzopoulos, K., Dillinger, R., Tuczek, F., Witzel, H., and Krebs, B. (1999) Purification and spectroscopic studies on catechol oxidase from Lycopus europaeus and Populus nigra: evidence for a dinuclear copper center of type and spectroscopic similarities to tyrosinase and hemocyanin. J. Biol. Inorg. Chem. 4, 56-63.
    • (1999) J. Biol. Inorg. Chem. , vol.4 , pp. 56-63
    • Rompel, A.1    Fisher, H.2    Meiwes, D.3    Buldt-Karentzopoulos, K.4    Dillinger, R.5    Tuczek, F.6    Witzel, H.7    Krebs, B.8
  • 31
    • 77149141385 scopus 로고    scopus 로고
    • Discovery of a new tyrosinase-like enzyme family lacking a C-terminally processed domain: Production and characterization of an Aspergillus oryzae catechol oxidase
    • Gasparetti, C., Faccio, G., Arvas, M., Buchert, J., Saloheimo, M., and Kruus, K. (2010) Discovery of a new tyrosinase-like enzyme family lacking a C-terminally processed domain: production and characterization of an Aspergillus oryzae catechol oxidase. Appl. Microbiol. Biotechnol. 86, 213-226.
    • (2010) Appl. Microbiol. Biotechnol. , vol.86 , pp. 213-226
    • Gasparetti, C.1    Faccio, G.2    Arvas, M.3    Buchert, J.4    Saloheimo, M.5    Kruus, K.6
  • 32
    • 0016311596 scopus 로고
    • O-diphenol: Oxygen-oxidoreductase from Musa cavendishii
    • Padron, M. P., Gonzalez, A. G., and Lozano, J. A. (1974) O-diphenol: oxygen-oxidoreductase from Musa cavendishii. Rev. Esp. Fisiol. 30, 167-176.
    • (1974) Rev. Esp. Fisiol. , vol.30 , pp. 167-176
    • Padron, M.P.1    Gonzalez, A.G.2    Lozano, J.A.3
  • 36
    • 33947600591 scopus 로고    scopus 로고
    • Two potent suicide substrates of mushroom tyrosinase
    • Chang, T. S. (2007) Two potent suicide substrates of mushroom tyrosinase. J. Agric. Food Chem. 55, 2010-2015.
    • (2007) J. Agric. Food Chem. , vol.55 , pp. 2010-2015
    • Chang, T.S.1
  • 37
    • 71749106972 scopus 로고    scopus 로고
    • Evaluation of depigmenting activity by 8-hydroxydaidzein in mouse B16 melanoma cells and human volunteers
    • Tai, S. S.-K., Lin, C.-G., Wu, M.-H., Chang, T. S. (2009) Evaluation of depigmenting activity by 8-hydroxydaidzein in mouse B16 melanoma cells and human volunteers. Int. J. Mol. Sci. 10, 4257-4266.
    • (2009) Int. J. Mol. Sci. , vol.10 , pp. 4257-4266
    • Tai, S.S.-K.1    Lin, C.-G.2    Wu, M.-H.3    Chang, T.S.4


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