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Volumn 22, Issue 4, 2007, Pages 383-394

Effect of tetrahydropteridines on the monophenolase and diphenolase activities of tyrosinase

Author keywords

Activation; Coenzymes, tyrosinase; Inhibition; Melanogenesis; Monophenol; O diphenol

Indexed keywords

6 ,7 DIMETHYLTETRAHYDROBIOPTERIN; 6 TETRAHYDROBIOPTERIN; ASCORBIC ACID; MONOPHENOL MONOOXYGENASE; REDUCING AGENT; TETRAHYDROPTERIDINE DERIVATIVE; UNCLASSIFIED DRUG;

EID: 34547777548     PISSN: 14756366     EISSN: 14756374     Source Type: Journal    
DOI: 10.1080/14756360701189776     Document Type: Article
Times cited : (6)

References (28)
  • 1
    • 0018401599 scopus 로고
    • Slow transitions and hysteretic behavior in enzymes
    • Frieden, C. (1979) Slow transitions and hysteretic behavior in enzymes. Annu Rev Biochem, 48, pp. 471-489.
    • (1979) Annu Rev Biochem , vol.48 , pp. 471-489
    • Frieden, C.1
  • 6
    • 0942289902 scopus 로고    scopus 로고
    • Indirect oxidation of 6-tetrahydrobiopterin by tyrosinase
    • Jung, HJ, Choi, SW and Han, S. (2004) Indirect oxidation of 6-tetrahydrobiopterin by tyrosinase. Biochem Biophys Res Commun, 314, pp. 937-942.
    • (2004) Biochem Biophys Res Commun , vol.314 , pp. 937-942
    • Jung, H.J.1    Choi, S.W.2    Han, S.3
  • 8
    • 14844295412 scopus 로고    scopus 로고
    • Regulation of tyrosinase by tetrahydropterines- What is real? A comment on the work published by Wood et al
    • Wojtasek, H. (2005) Regulation of tyrosinase by tetrahydropterines- what is real? A comment on the work published by Wood et al. on December 24, 2004. Biochem Biophys Res Commun, 329, pp. 801-803.
    • (2005) Biochem Biophys Res Commun , vol.329 , pp. 801-803
    • Wojtasek, H.1
  • 9
    • 18844435942 scopus 로고    scopus 로고
    • Regulation of tyrosinase by tetrahydropterines - What is real? A critical reanalysis of H Wojtasek's view
    • Wood, JM, Chavan, B., Hafeez, I. and Schallreuter, KU (2005) Regulation of tyrosinase by tetrahydropterines - What is real? A critical reanalysis of H. Wojtasek's view. Biochem Biophys Res Commun, 331, pp. 891-893.
    • (2005) Biochem Biophys Res Commun , vol.331 , pp. 891-893
    • Wood, J.M.1    Chavan, B.2    Hafeez, I.3    Schallreuter, K.U.4
  • 10
    • 0025807858 scopus 로고
    • Studies on the reactions between human tyrosinase, superoxide anion, hydrogen peroxide and thiols
    • Wood, JM and Schallreuter, KU (1991) Studies on the reactions between human tyrosinase, superoxide anion, hydrogen peroxide and thiols. Biochim Biophys Acta, 1074, pp. 378-385.
    • (1991) Biochim Biophys Acta , vol.1074 , pp. 378-385
    • Wood, J.M.1    Schallreuter, K.U.2
  • 11
    • 0014010123 scopus 로고
    • The tyrosine hydroxylase activity of mammalian tyrosinase
    • Pomerantz, SH (1966) The tyrosine hydroxylase activity of mammalian tyrosinase. J Biol Chem, 241, pp. 161-168.
    • (1966) J Biol Chem , vol.241 , pp. 161-168
    • Pomerantz, S.H.1
  • 12
    • 28044455441 scopus 로고    scopus 로고
    • A novel mechanism in control of human pigmentation by β-melanocyte-stimulating hormone and 7-tetrahydrobiopterin
    • Spencer, JD, Chavan, B., Marles, LK, Kaueser, S., Rokos, H. and Schallreuter, KU (2005) A novel mechanism in control of human pigmentation by β-melanocyte-stimulating hormone and 7-tetrahydrobiopterin. J Endocrinol, 187, pp. 293-302.
    • (2005) J Endocrinol , vol.187 , pp. 293-302
    • Spencer, J.D.1    Chavan, B.2    Marles, L.K.3    Kaueser, S.4    Rokos, H.5    Schallreuter, K.U.6
  • 13
    • 0014939358 scopus 로고
    • Physicochemical and kinetic properties of mushroom tyrosinase
    • Duckworth, HW and Coleman, JE (1970) Physicochemical and kinetic properties of mushroom tyrosinase. J Biol Chem, 245, pp. 1613-1625.
    • (1970) J Biol Chem , vol.245 , pp. 1613-1625
    • Duckworth, H.W.1    Coleman, J.E.2
  • 14
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantization of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, MM (1976) A rapid and sensitive method for the quantization of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem, 72, pp. 248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 15
    • 0037140963 scopus 로고    scopus 로고
    • Mechanistic implications of variable stoichiometries of oxygen consumption during tyrosinase catalyzed oxidation of monophenols and o-diphenols
    • Peñalver, MJ, Hiner, AN, Rodríguez-López, JN, García-Cánovas, F. and Tudela, J. (2002) Mechanistic implications of variable stoichiometries of oxygen consumption during tyrosinase catalyzed oxidation of monophenols and o-diphenols. Biochim Biophys Acta, 1597, pp. 140-148.
    • (2002) Biochim Biophys Acta , vol.1597 , pp. 140-148
    • Peñalver, M.J.1    Hiner, A.N.2    Rodríguez-López, J.N.3    García-Cánovas, F.4    Tudela, J.5
  • 17
    • 0033983446 scopus 로고    scopus 로고
    • Use of a windows program for simulation of the progress curves of reactants and intermediates involved in enzyme-catalyzed reactions
    • García-Sevilla, F., Solo, C Garrido-del, Duggleby, RG, García-Cánovas, F., Peyro, R. and Varón, R. (2000) Use of a windows program for simulation of the progress curves of reactants and intermediates involved in enzyme-catalyzed reactions. BioSystems, 54, pp. 151-164.
    • (2000) BioSystems , vol.54 , pp. 151-164
    • García-Sevilla, F.1    Garrido-del Solo, C.2    Duggleby, R.G.3    García-Cánovas, F.4    Peyro, R.5    Varón, R.6
  • 18
    • 0027954660 scopus 로고
    • Tyrosinase: Kinetic analysis of the transient phase and the steady-state
    • Ros, JR, Rodríguez-López, JN and García-Cánovas, F. (1994) Tyrosinase: Kinetic analysis of the transient phase and the steady-state. Biochim Biophys Acta, 1204, pp. 33-42.
    • (1994) Biochim Biophys Acta , vol.1204 , pp. 33-42
    • Ros, J.R.1    Rodríguez-López, J.N.2    García-Cánovas, F.3
  • 19
  • 22
    • 0344845292 scopus 로고    scopus 로고
    • Tyrosinase kinetics: Discrimination between two models to explain the oxidation mechanism of monophenol and o-diphenol substrates
    • Fenoll, LG, Peñalver, MJ, Rodríguez-López, JN, Varón, R., García-Cánovas, F. and Tudela, J. (2004) Tyrosinase kinetics: Discrimination between two models to explain the oxidation mechanism of monophenol and o-diphenol substrates. Int J Biochem Cell Biol, 36, pp. 235-246.
    • (2004) Int J Biochem Cell Biol , vol.36 , pp. 235-246
    • Fenoll, L.G.1    Peñalver, M.J.2    Rodríguez-López, J.N.3    Varón, R.4    García-Cánovas, F.5    Tudela, J.6
  • 23
    • 0027453615 scopus 로고
    • Effect of L-ascorbic acid on the monophenolase activity of tyrosinase
    • Ros, JR, Rodríguez-López, JN and García-Cánovas, F. (1993) Effect of L-ascorbic acid on the monophenolase activity of tyrosinase. Biochem J, 295, pp. 309-312.
    • (1993) Biochem J , vol.295 , pp. 309-312
    • Ros, J.R.1    Rodríguez-López, J.N.2    García-Cánovas, F.3
  • 24
    • 34547795449 scopus 로고    scopus 로고
    • Use of a windows program for simulation of the progress curves of reactants and intermediates involved in enzyme-catalyzed reactions
    • García-Sevilla, F., Soto, C Garrido-del, Duggleby, RG, García-Cánovas, F., Peyró P. and Varón, R. (2000) Use of a windows program for simulation of the progress curves of reactants and intermediates involved in enzyme-catalyzed reactions. BioSystems, 541, pp. 51-164.
    • (2000) BioSystems , vol.541 , pp. 51-164
    • García-Sevilla, F.1    Soto, C.2    del Garrido3    Duggleby, R.G.4    García-Cánovas, F.5    Peyró, P.6    Varón, R.7
  • 28
    • 0014010123 scopus 로고
    • The tyrosine hydroxylase activity of mammalian tyrosinase
    • Pomerantz, SH (1966) The tyrosine hydroxylase activity of mammalian tyrosinase. J Biol Chem, 241, pp. 161-168.
    • (1966) J Biol Chem , vol.241 , pp. 161-168
    • Pomerantz, S.H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.