An approximate analytical solution to the lag period of monophenolase activity of tyrosinase

International Journal of Biochemistry and Cell Biology

Volumn 39, Issue 1, 2007, Pages 238-252

  Molina, F García ^a   Munoz J L ^a   Varon R ^b   López, J N Rodríguez ^a   Cánovas, F García ^a   Tudela, J ^a  

^a UNIVERSITY OF MURCIA   (Spain)

^b UNIVERSITY OF CASTILLA LA MANCHA   (Spain)

Author keywords

Diphenolase; Kinetic; Lag period; Monophenolase; Transient phase; Tyrosinase

Indexed keywords

CATECHOL OXIDASE; MONOPHENOL MONOOXYGENASE;

ANALYTIC METHOD; ARTICLE; BINDING SITE; ENZYME ACTIVITY; KINETICS; MICHAELIS CONSTANT;

AGARICALES; KINETICS; LEVODOPA; MODELS, CHEMICAL; MONOPHENOL MONOOXYGENASE;

EID: 33749858219     PISSN: 13572725     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biocel.2006.08.007     Document Type: Article

References (41)

1. Bradford M.M. A rapid and sensitive method for the quantisation of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical Biochemistry 72 (1976) 248-254
2. Duckworth H.W., and Coleman J.E. Physicochemical and kinetic properties of mushroom tyrosinase. The Journal of Biological Chemistry 245 (1970) 1613-1625
3. Easterby J.S. Coupled enzyme assays: A general expression for the transient. Biochimica et Biophysica Acta 293 (1973) 552-558
4. Easterby J.S. The kinetics of consecutive enzyme reactions. Biochemical Journal 219 (1984) 843-847
5. Espín J.C., García-Ruiz P.A., Tudela J., and García-Cánovas F. Study of stereospecifity in mushroom tyrosinase. Biochemical Journal 331 (1998) 547-551
6. Espín J.C., García-Ruiz P.A., Tudela J., and García-Cánovas F. Study of stereospecificity in pear and strawberry polyphenol oxidases. The Journal of Agricultural and Food Chemistry 46 (1998) 2469-2473
7. Espín J.C., García-Ruiz P.A., Tudela J., Varón R., and García-Cánovas F. Monophenolase and diphenolase reaction mechanisms of apple and pear polyphenol oxidases. The Journal of Agricultural and Food Chemistry 46 (1998) 2968-2975
8. Fenoll L.G., Peñalver M.J., Rodríguez-López J.N., Varón R., García-Cánovas F., and Tudela J. Tyrosinase kinetics: Discrimination between two models to explain the oxidation mechanism of monophenol and diphenol substrates. The International Journal of Biochemistry and Cell Biology 2 (2004) 235-246
9. Fenoll L.G., Rodríguez-López J.N., García-Sevilla F., et al. Analysis and interpretation of the action mechanism of mushroom tyrosinase on monophenols and diphenols generating highly unstable o-quinones. Biochimica et Biophysica Acta 1548 (2001) 1-22
10. Frieden C. Analysis of kinetic data: Practical applications of computer simulation and fitting programs. Methods in Enzymology 240 (1994) 311-322
11. García-Carmona F., Cabanes J., and García-Cánovas F. Enzymatic oxidation by frog epidermis tyrosinase of 4-methylcatechol and p-cresol. Influence of l-serine. Biochimica et Biophysica Acta 914 (1987) 198-204
12. García-Carmona F., Cabanes J., and García-Cánovas F. Kinetic study of sinephrine oxidation by mushroom tyrosinase. Biochemistry International 6 (1987) 1003-1013
13. García-Carmona F., García-Cánovas F., Iborra J.L., and Lozano J.A. A kinetic study of the pathway of melanization between l-dopa and dopachrome. Biochimica et Biophysica Acta 717 (1982) 124-131
14. García-Carmona F., García-Cánovas F., and Lozano J.A. Optimizing enzyme assays with one or two coupling enzymes. Analytical Biochemistry 113 (1981) 286-291
15. García-Cánovas F., García-Carmona F., Vera-Sánchez J., Iborra J.L., and Lozano J.A. The role of pH in the melanin biosynthesis pathway. The Journal of Biological Chemistry 257 (1982) 8738-8744
16. Garcia-Molina F., Peñalver M.J., Fenoll L.G., et al. Kinetic study of monophenol and o-diphenol binding to oxytyrosinase. The Journal Molecular Catalysis B: Enzymatic 32 (2005) 185-192
17. García-Sevilla F., Garrido del Solo C., Duggleby R.G., García-Cánovas F., Peyró-García R., and Varón R. Use of a windows program for simulation of the progress curves of reactants and intermediates involved in enzyme-catalyzed reactions. Biosystems 54 (2000) 151-164
18. Gerald C.F. Applied numerical analysis (1978), Addison-Wesley, Reading
19. Kertesz D., Brunori M., Zito R., and Antonini E. Transient kinetic studies of DOPA oxidation by polyphenol oxidase. Biochimica et Biophysica Acta 250 (1971) 306-310
20. Lerch K. Copper monooxygenases: Tyrosinase and dopamine beta-hydroxylase. In: Sigel H. (Ed). Metal ions in biological systems (1981), Marcel Dekker Inc., New York 143-186
21. Lerch K., and Ettlinger L. Purification and characterization of a tyrosinase from Streptomyces glaucescens. The European Journal of Biochemistry 31 (1972) 427-437
22. Makino N., and Mason H.S. Reactivity of oxytyrosinase toward substrates. The Journal of Biological Chemistry 248 (1973) 5731-5735
23. Orenes-Piñero E., García-Carmona F., and Sanchez-Ferrer A. A kinetic study of p-cresol oxidation by quince fruit polyphenol oxidase. The Journal of Agricultural and Food Chemistry 53 (2005) 1196-1200
24. Peñalver M.J., Fenoll L.G., Rodríguez-López J.N., et al. Reaction mechanism to explain the high kinetic autoactivation of tyrosinase. The Journal Molecular Catalysis B: Enzymatic 33 (2005) 35-42
25. Peñalver M.J., Hiner A.N., Rodríguez-López J.N., García-Cánovas F., and Tudela J. Mechanistic implications of variable stoichiometries of oxygen consumption during tyrosinase catalyzed oxidation of monophenols and o-diphenols. Biochimica et Biophysica Acta 1597 (2002) 140-148
26. Peñalver M.J., Rodríguez-López J.N., García-Ruiz P.A., García-Cánovas F., and Tudela J. Solvent deuterium isotope effect on the oxidation of o-diphenols by tyrosinase. Biochimica et Biophysica Acta 1650 (2003) 128-135
27. Perez-Gilabert M., Morte A., Honrubia M., and García-Carmona F. Monophenolase activity of latent Terfezia claveryi tyrosinase: Characterization and histochemical localization. Physiologia Plantarum 113 (2001) 203-209
28. Pomerantz S.H. The tyrosine hydroxylase activity of mammalian tyrosinase. The Journal of Biological Chemistry 241 (1966) 161-168
29. Pomerantz S.H., and Warner M.C. 3, 4-Dihydroxy-1-phenilalanine as the tyrosinase cofactor. The Journal of Biological Chemistry 242 (1967) 5308-5314
30. Prota G., d'Ischia M., and Napolitano A. The chemistry of melanins and related metabolites. In: Nordlund J.J., Boissy R.E., Hearing V.J., King R.A., and Ortonne J.P. (Eds). The pigmentary system, physiology and phatology (1998), Oxford University Press, Oxford 307-332
31. Rodríguez-López J.N., Escribano J., and García-Cánovas F. A continuous spectrophotometric method for the determination of monophenolase activity of tyrosinase using 3-methyl-benzothiazolinone hydrazone. Analytical Biochemistry 216 (1994) 205-212
32. Rodríguez-López J.N., Fenoll L.G., García-Ruíz P.A., et al. Stopped-flow and steady-state study of the diphenolase activity of mushroom tyrosinase. Biochemistry 39 (2000) 10497-10506
33. Rodríguez-López J.N., Fenoll L.G., Peñalver M.J., et al. Tyrosinase action on monophenols: Evidence for direct enzymatic release of o-diphenol. Biochimica et Biophysica Acta 1548 (2001) 238-256
34. Rodríguez-López J.N., Tudela J., Varón R., and García-Cánovas F. Kinetic study on the effect of pH on the melanin biosynthesis pathway. Biochimica et Biophysica Acta 1076 (1991) 379-386
35. Rodríguez-López J.N., Tudela J., Varón R., García-Carmona F., and García-Cánovas F. Analysis of a kinetic model for melanin biosynthesis pathway. The Journal of Biological Chemistry 267 (1992) 3801-3810
36. Ros J.R., Rodríguez-López J.N., and García-Cánovas F. Tyrosinase: Kinetic analysis of the transient phase and the steady-state. Biochimica et Biophysica Acta 1204 (1994) 33-42
37. Ros J.R., Rodríguez-López J.N., and García-Cánovas F. Kinetics study of the oxidation of 4-tert-butylphenol by tyrosinase. The European Journal of Biochemistry 222 (1994) 449-452
38. Sánchez-Ferrer A., Rodríguez-López J.N., García-Cánovas F., and García-Carmona F. Tyrosinase: A comprehensive review of its mechanism. Biochimica et Biophysica Acta 1247 (1995) 1-11
39. Solomon E.I., Sundaram U.M., and Machonkin T.E. Multicopper oxidases and oxygenases. Chemical Review 96 (1996) 2563-2605
40. Varón R., Ruiz-Galea M.M., Garrido-del Solo C., et al. Transient phase of enzymes reactions. Time course equations of the strict and rapid equilibrium conditions and their computerized derivation. Biosystems 50 (1999) 99-126
41. Xie L.P., Chen Q.X., Huang H., Lui X.D., Chen H.T., and Zhang R.Q. Inhibitory effects of cupferron on the monophenolase and diphenolase activity of mushroom tyrosinase. The International Journal of Biochemistry and Cell Biology 35 (2003) 1658-1666