메뉴 건너뛰기




Volumn 34, Issue 12, 2002, Pages 1594-1607

Kinetic characterisation of the reaction mechanism of mushroom tyrosinase on tyramine/dopamine and L-tyrosine methyl esther/L-dopa methyl esther

Author keywords

Diphenols; Dopamine; Enzyme kinetics; L dopa methyl esther; L tyrosine methyl esther; Monophenols; Mushrooms; Nuclear magnetic resonance; Polyphenol oxidases; Quinones; Reaction mechanism; Tyramine; Tyrosinases

Indexed keywords

DOPAMINE; ESTER DERIVATIVE; MONOPHENOL MONOOXYGENASE; TYRAMINE; TYROSINE METHYL ESTER; DRUG DERIVATIVE; LEVODOPA; LEVODOPA METHYL ESTER; OXYGEN;

EID: 0036887577     PISSN: 13572725     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1357-2725(02)00076-6     Document Type: Article
Times cited : (33)

References (68)
  • 1
    • 77049203277 scopus 로고
    • Comparative biochemistry of the phenolase complex
    • Mason H.S. Comparative biochemistry of the phenolase complex. Adv. Enzymol. 16:1955;105-184.
    • (1955) Adv. Enzymol. , vol.16 , pp. 105-184
    • Mason, H.S.1
  • 2
    • 85053591293 scopus 로고
    • Tyrosinase
    • R. Lontie (Ed.), CRC Press, Boca Raton
    • D.A. Robb, Tyrosinase, in: R. Lontie (Ed.), Copper Proteins and Copper Enzymes, CRC Press, Boca Raton, 1984, pp. 207-241.
    • (1984) Copper Proteins and Copper Enzymes , pp. 207-241
    • Robb, D.A.1
  • 4
    • 0031213675 scopus 로고    scopus 로고
    • Sequence and structural features of plant and fungal tyrosinases
    • Van Gelder C.W.G., Flurkey W.H. Sequence and structural features of plant and fungal tyrosinases. Phytochemistry. 45:1997;1309-1323.
    • (1997) Phytochemistry , vol.45 , pp. 1309-1323
    • Van Gelder, C.W.G.1    Flurkey, W.H.2
  • 5
    • 0001888944 scopus 로고    scopus 로고
    • The enzymology of melanogenesis
    • J.J. Nordlund, R. Boissy, V. Hearing, R. King, J.P. Ortonne (Eds.), University Press, Oxford
    • J. Pawelek, A.K. Chakraborty, The enzymology of melanogenesis, in: J.J. Nordlund, R. Boissy, V. Hearing, R. King, J.P. Ortonne (Eds.), The Pigmentary System, University Press, Oxford, 1998, pp. 391-400.
    • (1998) The Pigmentary System , pp. 391-400
    • Pawelek, J.1    Chakraborty, A.K.2
  • 6
    • 0002281576 scopus 로고    scopus 로고
    • The chemistry of melanins and related metabolites
    • J.J. Nordlund, R. Boissy, V. Hearing, R. King, J.P. Ortonne (Eds.), University Press, Oxford
    • G. Prota, M. d'Ischia, A. Napolitano, The chemistry of melanins and related metabolites, in: J.J. Nordlund, R. Boissy, V. Hearing, R. King, J.P. Ortonne (Eds.), The Pigmentary System, University Press, Oxford, 1998, pp. 307-332.
    • (1998) The Pigmentary System , pp. 307-332
    • Prota, G.1    D'Ischia, M.2    Napolitano, A.3
  • 7
    • 0028849032 scopus 로고
    • The in vivo melanocytotoxicity and depigmenting potency of N-2,4-acetoxyphenyl thioethyl acetamide in the skin and hair
    • Jimbow M., Marusyk H., Jimbow K. The in vivo melanocytotoxicity and depigmenting potency of N-2,4-acetoxyphenyl thioethyl acetamide in the skin and hair. Br. J. Dermatol. 133:1995;526-536.
    • (1995) Br. J. Dermatol. , vol.133 , pp. 526-536
    • Jimbow, M.1    Marusyk, H.2    Jimbow, K.3
  • 8
    • 0030795081 scopus 로고    scopus 로고
    • Why tyrosinase for treatment of melanoma
    • Song Y.H. Why tyrosinase for treatment of melanoma. Lancet. 350:1997;82-83.
    • (1997) Lancet , vol.350 , pp. 82-83
    • Song, Y.H.1
  • 9
    • 0029082283 scopus 로고
    • Enhancement of the depigmenting effect of hydroquinone by cystamine and buthionine sulfoximine
    • Bolognia J.L., Sodi S.A., Osber M.P., Pawelek J.M. Enhancement of the depigmenting effect of hydroquinone by cystamine and buthionine sulfoximine. Br. J. Dermatol. 133:1995;349-357.
    • (1995) Br. J. Dermatol. , vol.133 , pp. 349-357
    • Bolognia, J.L.1    Sodi, S.A.2    Osber, M.P.3    Pawelek, J.M.4
  • 10
    • 0032503007 scopus 로고    scopus 로고
    • The oxidative metabolism of catecholamines in the brain: A review
    • Smythies J., Galzigna L. The oxidative metabolism of catecholamines in the brain: a review. Biochim. Biophys. Acta. 1380:1998;159-162.
    • (1998) Biochim. Biophys. Acta , vol.1380 , pp. 159-162
    • Smythies, J.1    Galzigna, L.2
  • 12
    • 0002810499 scopus 로고
    • Recent advances in chemistry of enzymatic browning: An overview
    • C.Y. Lee, J.R. Whitaker (Eds.), American Chemical Society, Washington
    • J.R. Whitaker, C.Y. Lee, Recent advances in chemistry of enzymatic browning: an overview, in: C.Y. Lee, J.R. Whitaker (Eds.), Enzymatic Browning and Its Prevention, American Chemical Society, Washington, 1995.
    • (1995) Enzymatic Browning and Its Prevention
    • Whitaker, J.R.1    Lee, C.Y.2
  • 13
    • 0002107288 scopus 로고
    • Enzymatic browning in fruits: Its biochemistry and control
    • C.Y. Lee, J.R. Whitaker (Eds.), American Chemical Society, Washington
    • J.R.L. Walker, Enzymatic browning in fruits: its biochemistry and control, in: C.Y. Lee, J.R. Whitaker (Eds.), Enzymatic Browning and Its Prevention, American Chemical Society, Washington, 1995.
    • (1995) Enzymatic Browning and Its Prevention
    • Walker, J.R.L.1
  • 14
    • 0003349223 scopus 로고
    • Prevention of enzymatic browning in fruits and vegetables: A review of principles and practice
    • C.Y. Lee, J.R. Whitaker (Eds.), American Chemical Society, Washington
    • L. Vámos-Vigyázó, Prevention of enzymatic browning in fruits and vegetables: a review of principles and practice, in: C.Y. Lee, J.R. Whitaker (Eds.), Enzymatic Browning and Its Prevention, American Chemical Society, Washington, 1995.
    • (1995) Enzymatic Browning and Its Prevention
    • Vámos-Vigyázó, L.1
  • 15
    • 0343081028 scopus 로고    scopus 로고
    • Inhibition of enzymatic browing and protection of sulfhydryl enzymes by thiol compounds
    • Negishi O., Ozawa T. Inhibition of enzymatic browing and protection of sulfhydryl enzymes by thiol compounds. Phytochemistry. 54:2000;481-487.
    • (2000) Phytochemistry , vol.54 , pp. 481-487
    • Negishi, O.1    Ozawa, T.2
  • 18
    • 0029835181 scopus 로고    scopus 로고
    • The dinuclear copper site structure of Agaricus bisporus tyrosinase in solution probet by X-ray absorption spectroscopy
    • Della Longa S., Ascone I., Bianconi A., Bonfigli A., Castellano A.C., Zarivi O., Miranda M. The dinuclear copper site structure of Agaricus bisporus tyrosinase in solution probet by X-ray absorption spectroscopy. J. Biol. Chem. 271:1996;21025-21030.
    • (1996) J. Biol. Chem. , vol.271 , pp. 21025-21030
    • Della Longa, S.1    Ascone, I.2    Bianconi, A.3    Bonfigli, A.4    Castellano, A.C.5    Zarivi, O.6    Miranda, M.7
  • 19
    • 0031760504 scopus 로고    scopus 로고
    • Crystal structure of a plant catechol oxidase containing a dicopper center
    • Klabunde T., Eicken C., Sacchettini J.C., Krebs B. Crystal structure of a plant catechol oxidase containing a dicopper center. Nat. Struct. Biol. 5:1998;1084-1090.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 1084-1090
    • Klabunde, T.1    Eicken, C.2    Sacchettini, J.C.3    Krebs, B.4
  • 32
    • 0031444758 scopus 로고    scopus 로고
    • Monophenolase activity of polyphenol oxidase from artichoke (Cynara scolymus L.) heads
    • Espín J.C., Tudela J., Garcia-Canovas F. Monophenolase activity of polyphenol oxidase from artichoke (Cynara scolymus L.) heads. Lebbensm. Wiss. Technol. 30:1997;819-825.
    • (1997) Lebbensm. Wiss. Technol. , vol.30 , pp. 819-825
    • Espín, J.C.1    Tudela, J.2    Garcia-Canovas, F.3
  • 33
    • 0027244227 scopus 로고
    • Characterisation of the Michaelis constants for oxygen in tyrosinase catalyzed oxidation of monophenols and o-diphenols
    • Rodríguez-López J.N., Ros J.R., Varón R., García-Cánovas F. Characterisation of the Michaelis constants for oxygen in tyrosinase catalyzed oxidation of monophenols and o-diphenols. Biochem. J. 293:1993;859-866.
    • (1993) Biochem. J. , vol.293 , pp. 859-866
    • Rodríguez-López, J.N.1    Ros, J.R.2    Varón, R.3    García-Cánovas, F.4
  • 44
    • 0030722720 scopus 로고    scopus 로고
    • Evidence of the indirect formation of the catecholic intermediate substrate responsible for the autoactivation kinetics of tyrosinase
    • Cooksey C.J., Garratt P.J., Land E.J., Pavel S., Ramsden C.A., Riley P.A., Smit P.M. Evidence of the indirect formation of the catecholic intermediate substrate responsible for the autoactivation kinetics of tyrosinase. J. Biol. Chem. 272:1997;26226-26235.
    • (1997) J. Biol. Chem. , vol.272 , pp. 26226-26235
    • Cooksey, C.J.1    Garratt, P.J.2    Land, E.J.3    Pavel, S.4    Ramsden, C.A.5    Riley, P.A.6    Smit, P.M.7
  • 45
    • 0032142793 scopus 로고    scopus 로고
    • Tyrosinase kinetics: Failure of the auto-activation mechanism of monohydric phenol oxidation by rapid formation of a quinomethane intermediate
    • Cooksey C.J., Garratt P.J., Land E.J., Ramsden C.A., Riley P.A. Tyrosinase kinetics: failure of the auto-activation mechanism of monohydric phenol oxidation by rapid formation of a quinomethane intermediate. Biochem. J. 333:1998;685-691.
    • (1998) Biochem. J. , vol.333 , pp. 685-691
    • Cooksey, C.J.1    Garratt, P.J.2    Land, E.J.3    Ramsden, C.A.4    Riley, P.A.5
  • 46
    • 0032041019 scopus 로고    scopus 로고
    • Tyrosinase kinetics: Failure of acceleration in oxidation of ring-blocked monohydric phenol substrate
    • Naish-Byfield S., Riley P.A. Tyrosinase kinetics: failure of acceleration in oxidation of ring-blocked monohydric phenol substrate. Pigment Cell Res. 11:1998;94-97.
    • (1998) Pigment Cell Res. , vol.11 , pp. 94-97
    • Naish-Byfield, S.1    Riley, P.A.2
  • 47
    • 0032087905 scopus 로고    scopus 로고
    • Tyrosinase autoactivation and the problem of the lag period
    • Naish-Byfield S., Riley P.A. Tyrosinase autoactivation and the problem of the lag period. Pigment Cell Res. 11:1998;127-133.
    • (1998) Pigment Cell Res. , vol.11 , pp. 127-133
    • Naish-Byfield, S.1    Riley, P.A.2
  • 48
    • 0034615509 scopus 로고    scopus 로고
    • Tyrosinase kinetics: A semiquantitative model of the mechanism of oxidation monohydric and dihydric phenolic substrates
    • Riley P.A. Tyrosinase kinetics: a semiquantitative model of the mechanism of oxidation monohydric and dihydric phenolic substrates. J. Theor. Biol. 203:2000;1-12.
    • (2000) J. Theor. Biol. , vol.203 , pp. 1-12
    • Riley, P.A.1
  • 49
    • 0014939358 scopus 로고
    • Physicochemical and kinetic properties of mushroom tyrosinase
    • Duckworth H.W., Coleman J.E. Physicochemical and kinetic properties of mushroom tyrosinase. J. Biol. Chem. 245:1970;1613-1625.
    • (1970) J. Biol. Chem. , vol.245 , pp. 1613-1625
    • Duckworth, H.W.1    Coleman, J.E.2
  • 50
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of proteins utilising the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantification of microgram quantities of proteins utilising the principle of protein-dye binding. Anal. Biochem. 72:1976;248-256.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-256
    • Bradford, M.M.1
  • 52
    • 77956756062 scopus 로고
    • Charge density-NMR chemical shift correlations in organic ions
    • V.D. Gold (Ed.), Academic Press, New York
    • D.G. Farnun, Charge density-NMR chemical shift correlations in organic ions, in: V.D. Gold (Ed.), Advances in Physical Organic Chemistry, Academic Press, New York, 1975, pp. 123-173.
    • (1975) Advances in Physical Organic Chemistry , pp. 123-173
    • Farnun, D.G.1
  • 57
    • 33845471694 scopus 로고
    • N2 reactions of nitranions with benzyl chlorides
    • N2 reactions of nitranions with benzyl chlorides. J. Am. Chem. Soc. 106:1984;3234-3240.
    • (1984) J. Am. Chem. Soc. , vol.106 , pp. 3234-3240
    • Bordell, F.G.1    Hughes, D.L.2
  • 58
    • 85046046003 scopus 로고
    • Factors influencing the antioxidant activities of phenols by an ab initio study
    • Tomiyama S., Sakai S., Nihiyama T., Yasmada F. Factors influencing the antioxidant activities of phenols by an ab initio study. Bull. Chem. Soc. Jpn. 66:1993;205-211.
    • (1993) Bull. Chem. Soc. Jpn. , vol.66 , pp. 205-211
    • Tomiyama, S.1    Sakai, S.2    Nihiyama, T.3    Yasmada, F.4
  • 59
    • 0025708340 scopus 로고
    • Computer program for the expression of the kinetic equations of enzyme reactions as functions of the rate constants and the initial concentrations
    • Varón R., Havsteen B.H., García-Moreno M., García-Cánovas F., Tudela J. Computer program for the expression of the kinetic equations of enzyme reactions as functions of the rate constants and the initial concentrations. Biochem. J. 270:1990;825-828.
    • (1990) Biochem. J. , vol.270 , pp. 825-828
    • Varón, R.1    Havsteen, B.H.2    García-Moreno, M.3    García-Cánovas, F.4    Tudela, J.5
  • 60
    • 0025744841 scopus 로고
    • Computer program for the kinetic equations of enzyme reactions: The case in which more than one enzyme species is present at the onset of the reactions
    • Varón R., Havsteen B.H., García-Moreno M., García-Cánovas F., Tudela J. Computer program for the kinetic equations of enzyme reactions: the case in which more than one enzyme species is present at the onset of the reactions. Biochem. J. 278:1991;91-97.
    • (1991) Biochem. J. , vol.278 , pp. 91-97
    • Varón, R.1    Havsteen, B.H.2    García-Moreno, M.3    García-Cánovas, F.4    Tudela, J.5
  • 61
    • 0019874460 scopus 로고
    • Transient phase kinetics of enzyme reactions
    • Gálvez J., Varón R. Transient phase kinetics of enzyme reactions. J. Theor. Biol. 89:1981;1-17.
    • (1981) J. Theor. Biol. , vol.89 , pp. 1-17
    • Gálvez, J.1    Varón, R.2
  • 62
    • 0000169232 scopus 로고
    • An algorithm for least-squares estimation of non-linear parameters
    • Marquardt D.W. An algorithm for least-squares estimation of non-linear parameters. J. Soc. Ind. Appl. Math. 11:1963;431-441.
    • (1963) J. Soc. Ind. Appl. Math. , vol.11 , pp. 431-441
    • Marquardt, D.W.1
  • 65
    • 0005499841 scopus 로고
    • Statistical estimations in enzyme kinetics
    • Wilkinson G.N. Statistical estimations in enzyme kinetics. Biochem. J. 80:1961;324-332.
    • (1961) Biochem. J. , vol.80 , pp. 324-332
    • Wilkinson, G.N.1
  • 66
    • 0014163158 scopus 로고
    • The statistical analysis of enzyme kinetic data
    • Cleland W.W. The statistical analysis of enzyme kinetic data. Adv. Enzymol. 29:1967;1-32.
    • (1967) Adv. Enzymol. , vol.29 , pp. 1-32
    • Cleland, W.W.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.