Purification, characterization, and molecular cloning of tyrosinase from Pholiota nameko

Bioscience, Biotechnology and Biochemistry

Volumn 71, Issue 7, 2007, Pages 1752-1760

  Kawamura Konishi, Yasuko ^a,b   Tsuji, Mariko ^a   Hatana, Seiichi ^a   Asanuma, Masahiro ^a   Kakuta, Dai ^a   Kawano, Takeshi ^a   Mukouyama, Etsuko B ^a   Goto, Hideyuki ^b   Suzuki, Haruo ^a  

^a KITASATO UNIVERSITY   (Japan)

^b ISHIKAWA PREFECTURAL UNIVERSITY   (Japan)

Author keywords

Pholiota nameko; Post translational modification; Proenzyme; Purification; Tyrosinase

Indexed keywords

CHARACTERIZATION; CLONING; COPPER; DEGRADATION; FRUITS; MOLECULAR WEIGHT; PURIFICATION;

PHOLIOTA NAMEKO; POST-TRANSLATIONAL MODIFICATION; PROENZYMES; TYROSINASE;

ENZYMES;

MONOPHENOL MONOOXYGENASE;

AGARICALES; AGARICUS; AMINO ACID SEQUENCE; ARTICLE; CHEMISTRY; COMPARATIVE STUDY; ENZYMOLOGY; GENETICS; ISOLATION AND PURIFICATION; MOLECULAR CLONING; MOLECULAR GENETICS; NUCLEOTIDE SEQUENCE;

AGARICALES; AGARICUS; AMINO ACID SEQUENCE; BASE SEQUENCE; CLONING, MOLECULAR; MOLECULAR SEQUENCE DATA; MONOPHENOL MONOOXYGENASE;

PHOLIOTA NAMEKO;

EID: 34548460251     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.70171     Document Type: Article

References (50)

1. Halaouli, S., Asther, M., Sigoillot, J.-C., Hamdi, M., and Lomascolo, A., Fungal tyrosinases: new prospects in molecular characteristics, bioengineering and biotechnological applications. J. Appl. Microbiol., 100, 219-232 (2006).
2. Seo, S.-Y., Sharma, V. K., and Sharma, N., Mushroom tyrosinase:recent prospects. J. Agric. Food Chem., 51, 2837-2853 (2003).
3. Jolivet, S., Arpin, N., Wichers, H. J., and Pellon, G., Agaricus bisporus browning:a review. Mycol. Res., 102, 1459-1483 (1998).
4. Claus, H., and Decker, H., Bacterial tyrosinases. Syst. Appl. Microbiol., 29, 3-14 (2006).
5. Sugumaran, M., Comparative biochemistry of eumelanogenesis and the protective roles of phenoloxidase and melanin in insects. Pigment Cell Res., 15, 2-9 (2002).
6. Westerhof, W., The discovery of the human melanocyte. Pigment Cell Res., 19, 183-193 (2006).
7. Wang, N., and Hebert, D. N., Tyrosinase maturation through the mammalian secretory pathway:bringing color to life. Pigment Cell Res., 19, 3-18 (2006).
8. Lerch, K., Neurospora tyrosinase:molecular weight, copper content and spectral properties. FEBS Lett., 69, 157-160 (1976).
9. Halaouli, S., Asther, M., Kruus, K., Guo, L., Hamdi, M., Sigoillot, J.-C., Asther, M., and Lomascolo, A., Characterization of a new tyrosinase from Pycnoporus species with high potential for food technological applications. J. Appl. Microbiol., 98, 332-343 (2005).
10. Naraoka, T., Uchisawa, H., Mori, H., Matsue, H., Chiba, S., and Kimura, A., Purification, characterization and molecular cloning of tyrosinase from the cephalopod mollusk, Illex argentinus. Eur. J. Biochem., 270, 4026-4038 (2003).
11. Selinheimo, E., Saloheimo, M., Ahola, E., Westerholm-Parvinen, A., Kalkkinen, N., Buchert, J., and Kruus, K., Production and characterization of a secreted, C-terminal processed tyrosinase from the filamentous fungus Trichoderma reesei. FEBS J., 273, 4322-4335 (2006).
12. Ito, M., and Oda, K., An organic solvent resistant tyrosinase from Streptomyces sp. REN-21:purification and characterization. Biosci. Biotechnol. Biochem., 64, 261-267 (2000).
13. Jaenicke, E., and Decker, H., Functional changes in the family of type 3 copper proteins during evolution. ChemBioChem, 5, 163-169 (2004).
14. Gerdemann, C., Eicken, C., and Krebs, B., The crystal structure of catechol oxidase:new insight into the function of type-3 copper proteins. Acc. Chem. Res., 35, 183-191 (2002).
15. Volbeda, A., and Hol, W. G., Crystal structure of hexameric haemocyanin from Panulirus interruptus refined at 3.2A resolution. J. Mol. Biol., 209, 249-279 (1989).
16. Solomon, E. I., Sundaram, U. M., and Machonkin, T. E., Multicopper oxidases and oxygenases. Chem. Rev., 96, 2563-2605 (1996).
17. Ros-Martínez, J. R., Rodríguez-López, J. N., Castellanos, R. V., and García-Cánovas, F., Discrimination between two kinetic mechanisms for the monophenolase activity of tyrosinase. Biochem. J., 294, 621-623 (1993).
18. Ros, J. R., Rodríguez-López, J. N., and García-Cánovas, F., Tyrosinase:kinetic analysis of the transient phase and the steady state. Biochim. Biophys. Acta, 1204, 33-42 (1994).
19. Decker, H., Dillinger, R., and Tuczek, F., How does tyrosinase work? Recent insights from model chemistry and structural biology. Angew. Chem. Int. Ed., 39, 1591-1595 (2000).
20. Peňalver, M. J., Hiner, A. N. P., 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. Biochim. Biophys. Acta, 1597, 140-148 (2002).
21. Matoba, Y., Kumagai, T., Yamamoto, A., Yoshitsu, H., and Sugiyama, M., Crystallographic evidence that the dinuclear copper center of tyrosinase is flexible during catalysis. J. Biol. Chem., 281, 8981-8990 (2006).
22. Ikehata, K., and Nicell, J. A., Color and toxicity removal following tyrosinase-catalyzed oxidation of phenols. Biotechnol. Prog., 16, 533-540 (2000).
23. Montiel, A. M., Fernández, F. J., Marcial, J., Soriano, J., Barrios-González, J., and Tomasini, A., A fungal phenoloxidase (tyrosinase) involved in pentachlorophenol degradation. Biotechnol. Lett., 26, 1353-1357 (2004).
24. Ensuncho, L., Alvarez-Cuenca, M., and Legge, R. L., Removal of aqueous phenol using immobilized enzymes in a bench scale and pilot scale three-phase fluidized bed reactor. Bioprocess Biosyst. Eng., 27, 185-191 (2005).
25. Haq, I., Ali, S., Qadeer, M. A., and Iqbal, J., Inductive effect of cresoquinone on microbiological transformation of L-tyrosine to 3,4 dihydroxy phenyl L-alanine by Aspergillus oryzae NG-11(P1). Appl. Microbiol. Biotechnol., 60, 696-699 (2003).
26. Chen, T., Embree, H. D., Wu, L.-Q., and Payne, G. F., In vitro protein-polysaccharide conjugation:Tyrosinase-catalyzed conjugation of gelation and chitosan. Biopolymers, 64, 292-302 (2002).
27. Thalmann, C. R., and Lötzbeyer, Enzymatic cross-linking of proteins with tyrosinase. Eur. Food Res. Technol., 214, 276-281 (2002).
28. Hurrell, R. F., and Finot, P. A., Protein-polyphenol reactions. 1. Nutritional metabolic consequences of the reaction between oxidized caffeic acid and the lysine residues of casein. Br. J. Nutr., 47, 191-211 (1982).
29. Rodriguez-López, J. N., Ros-Martínez, J. R., Varón, R., and García-Cánovas, F., Calibration of a Clark-type oxygen electrode by tyrosinase-catalyzed oxidation of 4-tert-butylcatechol. Anal. Biochem., 202, 356-360 (1992).
30. Sanjust, E., Cecchini, G., Sollai, F., Curreli, N., and Rescigno, A., 3-Hydroxykynurenine as a substrate/activator for mushroom tyrosinase. Arch. Biochem. Biophys., 412, 272-278 (2003).
31. Carlson, B. W., and Miller, L. L., Mechanism of the oxidation of NADH by quinones:energetics of one-electron and hydride routes. J. Am. Chem. Soc., 107, 479-485 (1985).
32. Espín, J. C., Varón, R., Fenoll, L. G., Gilabert, M. A., García-Ruíz, P. A., Tudela, J., and García-Cánovas, F., Kinetic characterization of the substrate specificity and mechanism of mushroom tyrosinase. Eur. J. Biochem., 267, 1270-1279 (2000).
33. Abrams, J. J., and Webster, D. A., Purification, partial characterization, and possible role of catalase in the bacterium Vitreoscilla. Arch. Biochem. Biophys., 279, 54-59 (1990).
34. Laemmli, U. K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680-685 (1970).
35. Solomon, E. I., Binuclear copper active site: hemocyanin, tyrosinase and type 3 copper oxidases. In "Copper Proteins" Vol. 3, ed. Spiro, T. G., Wiley-Interscience, New York, pp. 41-108 (1981).
36. Eickman, N. C., Himmelwright, R. S., and Solomon, E. I., Geometric and electronic structure of oxyhemocyanin: spectral and chemical correlations to met apo, half met, met, and dimer active sites. Proc. Natl. Acad. Sci. USA, 76, 2094-2098 (1979).
37. Jolley, R. L. Jr., Evans, L. H., Makino, N., and Mason, H. S., Oxytyrosinase. J. Biol. Chem., 249, 335-345 (1974).
38. Eicken, C., Zippel, F., Büldt-Karentzopoulos, K., and Krebs, B., Biochemical and spectroscopic characterization of catechol oxidase from sweet potatoes (Ipomoea batatas) containing a type-3 dicopper center. FEBS Lett., 436, 293-299 (1998).
39. Rompel, A., Fischer, H., Meiwes, D., Büldt-Karentzopoulos, K., Dillinger, R., Tuczek, F., Witzel, H., and Krebs, B., Purification and spectroscopic studies on catechol oxidases from Lycopus europaeus and Populus nigra:evidence for a dinuclear copper center of type 3 and spectroscopic similarities to tyrosinase and hemocyanin. J. Biol. Inorg. Chem., 4, 56-63 (1999).
40. Espín, J. C., García-Ruiz, P. A., Tudela, J., and García-Cánovas, F., Study of stereospecificity in mushroom tyrosinase. Biochem. J., 331, 547-551 (1998).
41. Wichers, H. J., Recourt, K., Hendriks, M., Ebbelaar, C. E. M., Biancone, G., Hoeberichts, F. A., Mooibroek, H., and Soler-Rivas, C., Cloning, expression and characterization of two tyrosinase cDNAs from Agaricus bisporus. Appl. Microbiol. Bioechnol., 61, 336-341 (2003).
42. Van Gelder, C. W. G., Flurkey, W. H., and Wichers, H. J., Sequence and structural features of plant and fungal tyrosinases. Phytochemistry, 45, 1309-1323 (1997).
43. Garcia-Borron, J. C., and Solano, F., Molecular anatomy of tyrosinase and its related proteins:beyond the histidine-bound metal catalytic center. Pigment Cell Res., 15, 162-173 (2002).
44. Lerch, K., Primary structure of tyrosinase from Neurospora crassa. II. Complete amino acid sequence and chemical structure of a tripeptide containing an unusual thioether. J. Biol. Chem., 257, 6414-6419 (1982).
45. Nakamura, M., Nakajima, T., Ohba, Y., Yamauchi, S., Lee, B. R., and Ichikawa, E., Identification of copper ligands in Aspergillus oryzae tyrosinase by site-directed mutagenesis. Biochem. J., 350, 537-545 (2000).
46. Nau, H., Lerch, K., and Witte, L., Amino acid sequence determination of the blocked N-terminal tryptic peptide of Neurospora tyrosinase by mass spectrometry. FEBS Lett., 79, 203-206 (1977).
47. Kupper, U., Niedermann, D. M., Travaglini, G., and Lerch, K., Isolation and characterization of the tyrosinase gene from Neurospora crassa. J. Biol. Chem., 264, 17250-17258 (1989).
48. Halaouli, S., Record, E., Casalot, L., Hamdi, M., Sigoillot, J.-C., Asther, M., and Lomascolo, A., Cloning and characterization of a tyrosinase gene from the white-rot fungus Pycnoporus sanguineus, and overproduction of the recombinant protein in Aspergillus niger. Appl. Microbiol. Biotechnol., 70, 580-589 (2006).
49. Espín, J. C., and Wichers, H. J., Kinetics of activation of latent mushroom (Agaricus bisporus) tyrosinase by benzyl alcohol. J. Agric. Food Chem., 47, 3503-3508 (1999).
50. Espín, J. C., van Leeuwen, J., and Wichers, H. J., Kinetic study of the activation process of a latent mushroom (Agaricus bisporus) tyrosinase by serine proteases. J. Agric. Food Chem., 47, 3509-3517 (1999).