Switch between tyrosinase and catecholoxidase activity of scorpion hemocyanin by allosteric effectors

FEBS Letters

Volumn 582, Issue 5, 2008, Pages 749-754

  Nillius, Dorothea ^a   Jaenicke, Elmar ^a   Decker, Heinz ^a  

^a JOHANNES GUTENBERG UNIVERSITY   (Germany)

Author keywords

Activated hemocyanin; Catecholoxidase; Scorpion Pandinus imperator; Type 3 copper protein; Tyrosinase

Indexed keywords

CATECHOLOXIDASE; HEMOCYANIN; MAGNESIUM; MONOPHENOL MONOOXYGENASE; OXIDOREDUCTASE; PHENOLOXIDASE DERIVATIVE; UNCLASSIFIED DRUG;

ALLOSTERISM; ARTICLE; CATALYSIS; CONTROLLED STUDY; ENZYME ACTIVITY; MELANOGENESIS; NONHUMAN; PRIORITY JOURNAL; SCORPION;

ALLOSTERIC REGULATION; ANIMALS; CATALYSIS; CATECHOL OXIDASE; DOPAMINE; ENZYME ACTIVATION; HEMOCYANIN; HEMOLYMPH; MAGNESIUM CHLORIDE; MONOPHENOL MONOOXYGENASE; SCORPIONS; SPECTRUM ANALYSIS; SUBSTRATE SPECIFICITY; TYRAMINE;

PANDINUS IMPERATOR; SCORPIONES;

EID: 39649113539     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2008.01.056     Document Type: Article

References (44)

1. van Holde K.E., and Miller K.I. Hemocyanins. Adv. Protein Chem. 47 (1995) 1-81
2. Solomon E.I., Sundaram U.M., and Machonkin T.E. Multicopper oxidases and oxygenases. Chem. Rev. 96 (1996) 2563-2606
3. Sánchez-Ferrer A., Rodrígues-López J., García-Cánovas F., and García-Carmona F. Tyrosinase: a comprehensive review of its mechanism. Biochim. Biophys. Acta 1247 (1995) 1-11
4. Riley P. Melanin. Int. J. Biochem. Cell Biol. 29 (1997) 1235-1239
5. Hoffmann J., Reichhart J., and Hetru C. Innate immunity in higher insects. Curr. Opin. Immunol. 8 (1996) 8-13
6. Jaenicke E., and Decker H. Tyrosinases from crustaceans form hexamers. Biochem. J. 371 (2003) 515-523
7. van Gelder C.W., Flurkey W.H., and Wichers H.J. Sequence and structural features of plant and fungal tyrosinases. Phytochemistry 45 (1997) 1309-1323
8. Oetting W.S., Fryer J.P., Shriram S., and King R.A. Oculocutaneous albinism Type 1: the last 100 years. Pigment Cell Res. 16 (2003) 307-311
9. Moore B., and Flurkey W. Sodium dodecyl sulfate activation of a plant polyphenoloxidase. Effect of sodium dodecyl sulfate on enzymatic and physical characteristics of purified broad bean polyphenoloxidase. J. Biol. Chem. 265 (1990) 4982-4988
10. Kanade S.R., Paul B., Appu Rao A.G., and Gowda L.R. The conformational state of polyphenol oxidase from field bean (Dolichos lablab) upon sodium dodecyl sulphate and acid-pH activation. Biochem. J. 395 (2006) 551-562
11. Kenten R.H. Latent phenolase in extracts of broad-bean. Biochem. J. 68 (1958) 244-251
12. Marques L., Fleuriet A., and Macheix J. Characterization of multiple forms of polyphenoloxidase of apple fruit. Plant Physiol. Biochem. 33 (1995) 193-200
13. Decker H., and Tuczek F. Tyrosinase/catecholoxidase activity of hemocyanins: structural basis and molecular mechanism. TIBS Rev. 25 (2000) 392-397
14. Matoba Y., Kumagai T., Yamamoto A., Yoshitsu H., and Sugiyama M. Crystallographic evidence that dinuclear copper center of tyrosinase is flexible during catalysis. J. Biol. Chem. 281 (2006) 8981-8990
15. Klabunde T., Eicken C., Sacchettini J., and Krebs B. Crystal structure of a plant catechol oxidase containing a dicopper center. Nature Struct. Biol. 5 (1998) 1084-1090
16. Decker H., Dillinger R., and Tuczek F. How does tyrosinase work? Recent insights from model chemistry and structural biology. Angew. Chem. Int. Ed. 39 (2000) 1591-1595
17. Tepper, A. (2005) Dissertation Universität Leiden, Leiden.
18. Decker H., Schweikardt T., and Tuczek F. The first crystal structure of tyrosinase: all questions answered?. Angew. Chem. Int. Ed. 45 (2006) 4546-4550
19. Itoh S., and Fukuzumi S. Monooxygenase activity of type 3 copper proteins. Acc. Chem. Res. 40 (2007) 592-600
20. Burmester T. Origin and evolution of arthropod hemocyanins and related proteins. J. Comp. Physiol. B 172 (2002) 95-107
21. Hazes B., Magnus K.A., Bonaventura C., Bonaventura J., Dauter Z., Kalk K.H., and Hol W.G. Crystal structure of deoxygenated Limulus polyphemus subunit II hemocyanin at 2.18 A resolution: clues for a Mechanismus for allosteric regulation. Protein Sci. 2 (1993) 597-619
22. Cuff M.E., Miller K.I., van Holde K.E., and Hendrickson W.A. Crystal structure of a functional unit from octopus hemocyanin. J. Mol. Biol. 278 (1998) 855-870
23. Magnus K.A., Hazes B., Ton-That H., Bonaventura C., Bonaventura J., and Hol W.G. Crystallographic analysis of oxygenated and desoxygenated states of arthropod hemocyanin shows unusual differences. Proteins 19 (1994) 302-309
24. Decker H., Ryan M., Jaenicke E., and Terwilliger N. SDS-induced phenoloxidase activity of hemocyanins from Limulus polyphemus, Eurypelma californicum, and Cancer magister. J. Biol. Chem. 276 (2001) 17796-17799
25. Decker H., and Rimke T. Tarantula hemocyanin shows phenoloxidase activity. J. Biol. Chem. 273 (1998) 25889-25892
26. Zlateva T., Di Muro P., Salvato B., and Beltramini M. The o-diphenol oxidase activity of arthropod hemocyanin. FEBS Lett. 384 (1996) 251-254
27. Nagai T., Osaki T., and Kawabata S. Functional conversion of hemocyanin to phenoloxidase by horeseshoe crab antimicrobial peptides. J. Biol. Chem. 276 (2001) 27166-27170
28. Salvato B., Santamaria M., Beltramini M., Aluzet G., and Casella L. The enzymatic properties of Octupus vulgaris hemocyanin: o-diphenol oxidase activity. Biochemistry 37 (1998) 14065-14077
29. Pless D.D., Aguilar M.B., Facón A., Álvarez E.L., and Heimer de la Cotera E.P. Latent phenoloxidase activity and N-terminal amino acid sequence of hemocyanin from Bathynomus giganteus, a primitive crustacean. Arch. Biochem. Biophys. 409 (2003) 402-410
30. Jaenicke E., and Decker H. Functional changes in the family of Type 3 copper proteins during evolution. Chembiochem 5 (2004) 163-169
31. Baviere M., Bazin B., and Aude R. Calcium effects on the solubility of sodium dodecyl sulfate in sodium chloride solutions. J. Colloid Interface Sci. 92 (1983) 580-583
32. Winder A., and Harris H. New assays for the tyrosine hydroxylase and dopa oxidase activities of tyrosinase. Eur. J. Biochem. 198 (1991) 317-326
33. Nellaiappan K., and Sugumaran M. On the presence of phenoloxidase in the hemolymph of the horseshoe crab, Limulus. Comp. Biochem. Physiol. 113 B (1996) 163-168
34. Mason H.S. The chemistry of melanin. III. Mechanism of the oxidation of dihydroxyphenylalanine by tyrosinase. J. Biol. Chem. 172 (1948) 83-99
35. Decker H., Markl J., Loewe R., and Linzen B. Hemocyanins in spiders, VIII. oxygen affinity of the individual subunits isolated from Eurypelma californicum hemocyanin. Hoppe Seylers Z. Physiol. Chem. 360 (1979) 1505-1507
36. Schartau W., and Leidescher T. Composition of the hemolymph of the tarantula Eurypelma californicum. J. Comp. Physiol. 152 (1983) 73-77
37. Cerenius L., and Söderhäll K. The prophenoloxidase-activating system in invertebrates. Immunol. Rev. 198 (2004) 116-126
38. Lorenzini D.M., Silva Jr. P.I., Soares M.B., Arruda P., Setubal J., and Daffre S. Discovery of immune-related genes expressed in hemocytes of the tarantula spider Acanthoscurria gomesiana. Dev. Comp. Immunol. 30 (2006) 545-556
39. Iwanaga S., and Lee B.L. Recent advances in the innate immunity of invertebrate animals. J. Biochem. Mol. Biol. 38 (2005) 128-150
40. Terwilliger N.B., and Ryan M.C. Functional and phylogenetic analyses of phenoloxidases from brachyuran sa(Cancer magister) and branchiopod (Artemia franciscana, Triops longicaudatus) crustaceans. Biol. Bull. 210 (2006) 38-50
41. Sterner R., Bardehele K., Paul R., and Decker H. Tris: an allosteric effector of tarantula haemocyanin. FEBS Lett. 339 (1994) 37-39
42. Sugumaran M., and Nellaiappan K. Lysolecithin - a potent activator of prophenoloxidase from the hemolymph of the lobster, Homarus americanus. Biochem. Biophys. Res. Commun. 176 (1991) 1371-1376
43. Baird S., Kelly S.M., Price N.C., Jaenicke E., Meesters C., Nillius D., Decker H., and Nairn J. Hemocyanin conformational changes associated with SDS-induced phenol oxidase activation. Biochim. Biophys. Acta 1774 (2007) 1380-1394
44. Morioka C., Tachi Y., Suzuki S., and Ito S. Significant enhancement of monooxygenase activity of oxygen carrier protein hemocyanin by urea. J. Am. Chem. Soc. 128 (2006) 6788-6789