372
Views
4
CrossRef citations to date
0
Altmetric
Research Article

Effect of tetrahydropteridines on the monophenolase and diphenolase activities of tyrosinase

, , , , &
Pages 383-394 | Received 20 Jul 2006, Accepted 30 Nov 2006, Published online: 04 Oct 2008

References

  • Frieden C. Slow transitions and hysteretic behavior in enzymes. Annu Rev Biochem 1979; 48: 471–489
  • Prota G, Ischia M, Napolitano A. The chemistry of melanins and related metabolites. Oxford University Press, New York 1998
  • Solomon EI, Sundaram UM, Machonkin TE. Multicopper oxidases and oxygenases. Chem Rev 1996; 96: 2563–2605
  • Rodríguez-López JN, Tudela J, Varón R, García-Carmona F, García-Cánovas F. Analysis of a kinetic model for melanin biosynthesis pathway. J Biol Chem 1992; 267: 3801–3810
  • Wood JM, Schallreuter-Wood KU, Lindsey NJ, Callaghan S, Gardner ML. A specific tetrahydrobiopterin binding domain on tyrosinase controls melanogenesis. Biochem Biophys Res Commun 1995; 206: 480–485
  • Jung HJ, Choi SW, Han S. Indirect oxidation of 6-tetrahydrobiopterin by tyrosinase. Biochem Biophys Res Commun 2004; 314: 937–942
  • Wood JM, Chavan B, Hafeez I, Schallreuter KU. Regulation of tyrosinase by tetrahydropteridines and H2O2. Biochem Biophys Res Commun 2004; 325: 1412–1417
  • Wojtasek H. 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 2005; 329: 801–803
  • Wood JM, Chavan B, Hafeez I, Schallreuter KU. Regulation of tyrosinase by tetrahydropterines – What is real? A critical reanalysis of H. Wojtasek's view. Biochem Biophys Res Commun 2005; 331: 891–893
  • Wood JM, Schallreuter KU. Studies on the reactions between human tyrosinase, superoxide anion, hydrogen peroxide and thiols. Biochim Biophys Acta 1991; 1074: 378–385
  • Pomerantz SH. The tyrosine hydroxylase activity of mammalian tyrosinase. J Biol Chem 1966; 241: 161–168
  • Spencer JD, Chavan B, Marles LK, Kaueser S, Rokos H, Schallreuter KU. A novel mechanism in control of human pigmentation by β-melanocyte-stimulating hormone and 7-tetrahydrobiopterin. J Endocrinol 2005; 187: 293–302
  • Duckworth HW, Coleman JE. Physicochemical and kinetic properties of mushroom tyrosinase. J Biol Chem 1970; 245: 1613–1625
  • Bradford MM. A rapid and sensitive method for the quantization of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 1976; 72: 248–254
  • Peñalver MJ, Hiner AN, Rodríguez-López JN, García-Cánovas F, Tudela J. Mechanistic implications of variable stoichiometries of oxygen consumption during tyrosinase catalyzed oxidation of monophenols and o-diphenols. Biochim Biophys Acta 2002; 1597: 140–148
  • Gerald CF. Applied Numerical Analysis. Addison-Wesley, Reading 1978
  • García-Sevilla F, Garrido-del Solo C, Duggleby RG, García-Cánovas F, Peyro R, Varón R. Use of a windows program for simulation of the progress curves of reactants and intermediates involved in enzyme-catalyzed reactions. BioSystems 2000; 54: 151–164
  • Ros JR, Rodríguez-López JN, García-Cánovas F. Tyrosinase: Kinetic analysis of the transient phase and the steady-state. Biochim Biophys Acta 1994; 1204: 33–42
  • Espín JC, García-Ruiz PA, Tudela J, Varón R, García-Cánovas F. Monophenolase and diphenolase reaction mechanisms of apple and pear polyphenol oxidases. J Agric Food Chem 1998; 46: 2968–2975
  • Espín JC, Morales M, Varón R, Tudela J, García-Cánovas F. Monophenolase activity of polyphenol oxidase from blanquilla pear. Phytochemistry 1997; 44: 17–22
  • Sánchez-Ferrer A, Rodríguez-López JN, García-Cánovas F, García-Carmona F. Tyrosinase: A comprehensive review of its mechanism. Biochim Biophys Acta 1995; 1247: 1–11
  • Fenoll LG, Peñalver MJ, Rodríguez-López JN, Varón R, García-Cánovas F, Tudela J. Tyrosinase kinetics: Discrimination between two models to explain the oxidation mechanism of monophenol and o-diphenol substrates. Int J Biochem Cell Biol 2004; 36: 235–246
  • Ros JR, Rodríguez-López JN, García-Cánovas F. Effect of L-ascorbic acid on the monophenolase activity of tyrosinase. Biochem J 1993; 295: 309–312

References

  • García-Sevilla F, Garrido-del Soto C, Duggleby RG, García-Cánovas F, Peyró P, Varón R. Use of a windows program for simulation of the progress curves of reactants and intermediates involved in enzyme-catalyzed reactions. BioSystems 2000; 541: 51–164
  • Hiromi K. Kinetics of fast enzymes reactions. Halsted Press, New York, U.S.A. 1979
  • Rodriguez-Lopez JN, Fenoll LG, García-Ruiz PA, Varón R, Tudela J, Thorneley RN, García-Cánovas F. Stopped-flow and steady-state study of the diphenolase activity of mushroom tyrosinase. Biochemistry 2000; 39: 10497–10506
  • Espín JC, Varon R, Fenoll LG, Gilabert MA, García-Ruiz PA, Tudela J, García Cánovas F. Kinetic characterization of the substrate specificity and mechanism of mushroom tyrosinase. Eur J Biochemistry 2000; 267: 1270–1279
  • Pomerantz SH. The tyrosine hydroxylase activity of mammalian tyrosinase. J Biol Chem 1966; 241: 161–168

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.