The mechanism of suicide-inactivation of tyrosinase: A substrate structure investigation

Tohoku Journal of Experimental Medicine

Volumn 212, Issue 4, 2007, Pages 341-348

  Land, Edward J ^a   Ramsden, Christopher A ^a   Riley, Patrick A ^b  

^a KEELE UNIVERSITY   (United Kingdom)

^b Totteridge Institute for Advanced Studies   (United Kingdom)

Author keywords

oxidation; Catecholase; Cresolase; Deprotonation; Suicide inactivation; Tyrosinase

Indexed keywords

CATECHOL; COPPER ION; MONOPHENOL MONOOXYGENASE; PHENOL; RESORCINOL; SUICIDE SUBSTRATE; CATECHOL DERIVATIVE; PHENOL DERIVATIVE;

ARTICLE; CATALYSIS; CHEMICAL PROCEDURES; CONTROLLED STUDY; CRYSTALLOGRAPHY; DEPROTONATION; ENZYME INACTIVATION; ENZYME INHIBITION; ENZYME KINETICS; ENZYME MECHANISM; ENZYME METABOLISM; ENZYME STRUCTURE; ENZYME SUBSTRATE; HYDROXYLATION; MUSHROOM; NONHUMAN; OXIDATION; BINDING SITE; CHEMICAL STRUCTURE; CHEMISTRY; DRUG ANTAGONISM; METABOLISM; OXIDATION REDUCTION REACTION; PROTEIN TERTIARY STRUCTURE; STRUCTURE ACTIVITY RELATION;

BINDING SITES; CATECHOLS; MOLECULAR STRUCTURE; MONOPHENOL MONOOXYGENASE; OXIDATION-REDUCTION; PHENOL; PHENOLS; PROTEIN STRUCTURE, TERTIARY; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 38449116139     PISSN: 00408727     EISSN: 13493329     Source Type: Journal    
DOI: 10.1620/tjem.212.341     Document Type: Article

References (31)

1. Agrup, G., Rorsman, H. & Rosengren, E. (1982) 5-OH-dopa, product of and substrate for tyrosinase. Acta Dermatovener. (Stockholm), 62, 371-376.
2. Asimov, I. & Dawson, C.R. (1950) On the reaction inactivation of tyrosinase during aerobic oxidation of catechol. J. Biol. Chem., 72, 820-828.
3. Bubacco, L., van Gastel, M., Groenen, E.J.J., Vijgenboom, E. & Canters, G.W. (2003) Spectroscopic characterization of the electronic changes in the active site of Streptomyces antibioticus tyrosinase upon binding of transition state analogue inhibitors. J. Biol. Chem., 278, 7381-7389.
4. Burzio, L.A. & Waite, J.H. (2002) The other topa: formation of 3,4,5-trihydroxyphenylalanine in peptides. Analyt. Biochem., 306, 108-114.
5. Carlberg, M., Jergil, B., Lindbladh, C. & Rosengren, E. (1984) Enzymatic 5-hydroxylation of L-dopa by a tyrosinase isolated from the sea anemone Metrium senile. Gen. Pharmacol., 15, 301-307.
6. Cooksey, C.J., Garratt, P.J., Land, E.J., Pavel, S., Ramsden, C.A., Riley, P.A. & Smit, N.P.M. (1997) Evidence of the indirect formation of the catecholic intermediate substrate responsible for the autoactivation kinetics of tyrosinase. J. Biol. Chem., 272, 26226-26135.
7. Corse, J. & Ingraham, L.L. (1951) The monofluorocatechols. J. Org. Chem., 16, 1345-1348.
8. Cram, D.J. & Cranz, F.W. (1950) Mold Metabolite. IV. The ultraviolet absorption spectra of certain aromatic hydroxyketones. J. Am. Chem. Soc., 72, 595-600.
9. Decker, H., Schweikardt, T. & Tuczek, F. (2006) The first crystal structure of tyrosinase: All questions answered? Angew. Chem. Int. Ed., 45, 4546-4550.
10. Dietler, C. & Lerch, K. (1982) Reaction inactivation of tyrosinase. In: Oxidases and Related Redox Systems, edited by T.E. King, H.S. Mason & M. Morrison, Pergamon Press, NY, pp. 305-317.
11. Garcia-Canovas, F., Tudela, J., Martinez-Madrid, C., Varon, R., Garcia-Carmona, F. & Lozano, J.A. (1987) Kinetic study on the suicide inactivation of tyrosinase induced by catechol. Biochim. Biophys. Acta, 912, 417-423.
12. Garcia-Molina, F., Hiner, A.N., Fenoll, L.G., Rodriguez-Lopez, J.N., Garcia-Ruiz, P.A., Garcia-Canovas, F. & Tudela, J. (2005) Mushroom tyrosinase: catalase activity, inhibition, and suicide inactivation. J. Agric. Food Chem., 53, 3702-3709.
13. Haghbeen, K., Saboury, A.A. & Karbassi, F. (2004) Substrate share in the suicide inactivation of mushroom tyrosinase. Biochim. Biophys. Acta, 1675, 139-146.
14. Hansson, C., Rorsman, H. & Rosengren, E. (1980) 5-Hydroxydopa, a new compound in the Raper-Mason scheme of melanogenesis. Acta Dermatovener. (Stockholm), 60, 281-186.
15. Hansson, C., Rorsman, H. & Rosengren, E. (1981) Pronounced formation of 5-OH-dopa at enzymatic oxidation of dopa in the presence of ascorbic acid. Acta Dermatovener. (Stockholm), 61, 147-148.
16. Ingraham, L.L., Corse, J. & Makower, B. (1952) Enzymatic browning of fruits. III. Kinetics of the reaction inactivation of polyphenoloxidase. J. Amer. Chem. Soc., 74, 2623-2626.
17. Lerch, K. (1983) Neurospora tyrosinase: structural, spectroscopic and catalytic properties. Mol. Cell. Biochem., 52, 125-138.
18. Mason, H.S. (1955) Comparative biochemistry of the phenolase complex. In: Advances in Enzymology, vol. 16, edited by F.F. Nord, Interscience Publishers Inc., New York, pp. 105-184.
19. Matoba, Y., Kumagai, T., Yamamoto, A., Yoshitsu, H. & Sugiyama, M. (2006) Crystallographic evidence that dinuclear copper center of tyrosinase is flexible during catalysis, J. Biol. Chem., 281, 8981-9003.
20. Miranda, M. & Botti, D. (1983) Harding-Passey mouse melanoma tyrosinase inactivation by reaction products and activation by L-epinephrine. Gen. Pharmacol., 14, 231-237.
21. Nelson, J.M. & Dawson, C.R. (1944) Tyrosinase. In: Advances in Enzymology, vol. 4, edited by F.F. Nord, C.H. Werkman, Interscience Publishers Inc., New York, pp. 99-152.
22. Salkowski, H. (1884) Ueber die isomeren oxyphenylessigsäuren. Chem. Ber., 17, 504-510.
23. Seiji, M., Sasaki, M. & Tomita, Y, (1979) Nature of tyrosinase inactivation in melanosomes. Tohoku J. Exp. Med., 125, 233-245.
24. Spritz, R.A., Ho, L., Furumara, M., & Hearing, V.J. (1997) Mutational analysis of copper binding by human tyrosinase. J. Invest. Dermatol., 109, 207-212.
25. Tomita, Y. & Seiji, M. (1977) Inactivation mechanism of tyrosinase in mouse melanoma. J. Dermatol., 4, 245-249.
26. Tomita, Y., Hariu, A., Mizuno, C. & Seiji, M. (1980) Inactivation of tyrosinase by dopa. J. Invest. Dermatol., 75, 379-382.
27. Tadela, J., Garcia-Canovas, F., Varon R. Jimenez, M., Garcia-Carmona, F. & Lozano, J.A. (1988) Kinetic study in the transient phase of the suicide inactivation of frog epidermis tyrosinase. Biophys. Chem., 30, 303-310.
28. Van Gastel, M., Bubacco, L., Groenen, E.J.J., Vijgenboom, E. & Canters, G.W. (2000) EPR study of the dinuclear active copper site of tyrosinase from Streptomyces antibioticus. FEBS Letters, 474, 228-232.
29. Waley, S.G. (1985) Kinetics of suicide substrates: Practical procedures for determining parameters. Biochem. J., 227, 843-849.
30. Walsh, C.T. (1984) Suicide substrates, mechanism-based enzyme inactivators: Recent developments. Ann. Rev. Biochem., 53, 493-535.
31. Wood, B.J.B. & Ingraham, L.L. (1965) Labelled tyrosinase from labelled substrate. Nature, 205, 291-292.