Changes in tyrosinase specificity by ionic liquids and sodium dodecyl sulfate

Applied Microbiology and Biotechnology

Volumn 97, Issue 5, 2013, Pages 1953-1961

  Goldfeder, Mor ^a   Egozy, Mor ^a   Shuster Ben Yosef, Vered ^a   Adir, Noam ^a   Fishman, Ayelet ^a  

^a TECHNION ISRAEL INSTITUTE OF TECHNOLOGY   (Israel)

Author keywords

Bacillus megaterium; Diphenols; Ionic liquids; Sodium dodecyl sulphate; Tyrosinase

Indexed keywords

[BMIM][BF; ACTIVE SITE; ACTIVITY RATIOS; BACILLUS MEGATERIUM; DIPHENOLS; L-TYROSINE; MONOPHENOLS; NATURAL SUBSTRATES; NON-NATIVE; POLAR SUBSTRATES; PRODUCTION OF; SODIUM DODECYL SULPHATE; SURFACTANT MOLECULES; TYROSINASE; WATER-MISCIBLE IONIC LIQUIDS;

AGRICULTURAL CHEMICALS; AMINO ACIDS; BACTERIOLOGY; ENZYMES; PHENOLS; SODIUM; SODIUM DODECYL SULFATE; SUBSTRATES;

IONIC LIQUIDS;

CATECHOL; DODECYL SULFATE SODIUM; IONIC LIQUID; LEVODOPA; MONOPHENOL MONOOXYGENASE; PHENOL; TYROSINE;

BACTERIUM; BIOTECHNOLOGY; BIOTRANSFORMATION; CATALYSIS; CRYSTAL STRUCTURE; ENZYME ACTIVITY; MELANIN; PHENOL; SULFATE; SURFACTANT;

ARTICLE; BACILLUS MEGATERIUM; CHEMICAL STRUCTURE; CONTROLLED STUDY; CRYSTAL STRUCTURE; CRYSTALLIZATION; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME MECHANISM; ENZYME PURIFICATION; ENZYME SPECIFICITY; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; MISCIBILITY; MUTAGENESIS; NONHUMAN; PROTEIN EXPRESSION; WILD TYPE;

BACILLUS MEGATERIUM; CATALYTIC DOMAIN; IONIC LIQUIDS; MODELS, MOLECULAR; MONOPHENOL MONOOXYGENASE; PHENOLS; PROTEIN CONFORMATION; SODIUM DODECYL SULFATE; SUBSTRATE SPECIFICITY;

BACILLUS MEGATERIUM;

EID: 84874117024     PISSN: 01757598     EISSN: 14320614     Source Type: Journal    
DOI: 10.1007/s00253-012-4050-z     Document Type: Article

References (42)

1. Adams PD, Afonine PV, Bunkoczi G, Chen VB, Davis IW, Echols N, Headd JJ, Hung LW, Kapral GJ, Grosse-Kunstleve RW, McCoy AJ, Moriarty NW, Oeffner R, Read RJ, Richardson DC, Richardson JS, Terwilliger TC, Zwart PH (2010) PHENIX: a comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr Sect D Biol Crystallogr 66: 213-221.
2. Brünger AT, Adams PD, Clore GM, DeLano WL, Gros P, Grosse-Kunstleve RW, Jiang JS, Kuszewski J, Nilges M, Pannu NS, Read RJ, Rice LM, Simonson T, Warren GL (1998) Crystallography & NMR system: A new software suite for macromolecular structure determination. Acta Crystallogr Sect D Biol Crystallogr 54: 905-921.
3. Burton SG (2003) Oxidizing enzymes as biocatalysts. Trends Biotechnol 21: 543-549.
4. Claus H, Decker H (2006) Bacterial tyrosinases. Syst Appl Microbiol 29: 3-14.
5. Cong Y, Zhang Q, Woolford D, Schweikardt T, Khant H, Dougherty M, Ludtke SJ, Chiu W, Decker H (2009) Structural mechanism of SDS-induced enzyme activity of scorpion hemocyanin revealed by electron cryomicroscopy. Structure 17: 749-758.
6. Decker H, Tuczek F (2000) Tyrosinase/catecholoxidase activity of hemocyanins: structural basis and molecular mechanism. Trends Biochem Sci 25: 392-397.
7. Decker H, Schweikardt T, Nillius D, Salzbrunn U, Jaenicke E, Tuczek F (2007) Similar enzyme activation and catalysis in hemocyanins and tyrosinases. Gene 398: 183-191.
8. Emsley P, Cowtan K (2004) Coot: model-building tools for molecular graphics. Acta Crystallogr Sect D Biol Crystallogr 60: 2126-2132.
9. Gandia-Herrero F, Jimenez-Atienzar M, Cabanes J, Garcia-Carmona F, Escribano J (2005) Differential activation of a latent polyphenol oxidase mediated by sodium dodecyl sulfate. J Agric Food Chem 53: 6825-6830.
10. Halaouli S, Asther M, Sigoillot JC, Hamdi M, Lomascolo. A (2006) Fungal tyrosinases: new prospects in molecular characteristics, bioengineering and biotechnological applications. J Appl Microbiol 100: 219-232.
11. Hernandez-Romero D, Sanchez-Amat A, Solano F (2006) A tyrosinase with an abnormally high tyrosine hydroxylase/dopa oxidase ratio. FEBS J 273: 257-270.
12. Itoh S, Fukuzumi S (2007) Monooxygenase activity of type 3 copper proteins. Acc Chem Res 40: 592-600.
13. Karbassi F, Haghbeen K, Saboury AA, Rezaei-Tavirani M, Ranjbar B (2004) Calorimetric, spectrophotometric and circular dichroism studies on the impact of sodium dodecyl sulfate on the mushroom tyrosinase structure. Biologia 59: 319-326.
14. Kawamura-Konishi Y, Tsuji M, Hatana S, Asanuma M, Kakuta D, Kawano T, Mukouyama EB, Goto H, Suzuki H (2007) Purification, characterization, and molecular cloning of tyrosinase from Pholiota nameko. Biosci, Biotechnol, Biochem 71: 1752-1760.
15. Klabunde T, Eicken C, Sacchettini JC, Krebs B (1998) Crystal structure of plant catechol oxidase containing a dicopper center. Nat Struct Biol 5: 1084-1090.
16. Leslie AGW (1992) Joint CCP4 + ESF-EAMCB Newsletter on protein crystallography: No. 26.
17. Lopez-Serrano D, Sanchez-Amat A, Solano F (2002) Cloning and molecular characterization of a SDS-activated tyrosinase from Marinomonas mediterranea. Pigment Cell Res 15: 104-111.
18. Martinez MV, Whitaker JR (1995) The biochemistry and control of enzymatic browning. Trends Food Sci Technol 6: 195-200.
19. McCoy AJ (2007) Solving structures of protein complexes by molecular replacement with Phaser. Acta Crystallogr Sect D Biol Crystallogr 63: 32-41.
20. Moore BM, Flurkey WH (1990) 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: 4982-4988.
21. Murshudov GN, Vagin AA, Dodson EJ (1997) Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr Sect D Biol Crystallogr 53: 240-255.
22. 50 values with purity of mushroom tyrosinase. Int J Mol Sci 10: 3811-3823.
23. Nillius D, Jaenicke E, Decker H (2008) Switch between tyrosinase and catecholoxidase activity of scorpion hemocyanin by allosteric effectors. FEBS Lett 582: 749-754.
24. Nolan LC, O'Connor KE (2007) Use of Pseudomonas mendocina, or recombinant Escherichia coli cells expressing toluene-4-monooxygenase, and a cell-free tyrosinase for the synthesis of 4-fluorocatechol from fluorobenzene. Biotechnol Lett 29: 1045-1050.
25. Olivares C, Solano F (2009) New insights into the active site structure and catalytic mechanism of tyrosinase and its related proteins. Pigm Cell Melanoma R 22: 750-760.
26. Olivares C, Garcia-Borron JC, Solano F (2002) Identification of active site residues involved in metal cofactor binding and stereospecific substrate recognition in mammalian tyrosinase. Implications to the catalytic cycle. Biochemistry 41: 679-686.
27. Rodriguez-Lopez JN, Escribano J, Garciacanovas F (1994) A continuous spectrophotometric method for the determination of monophenolase activity of tyrosinase using 3-methyl-2-benzothiazolinone hydrazone. Anal Biochem 216: 205-212.
28. Saeidian S, Keyhani E, Keyhani J (2007) Effect of ionic detergents, nonionic detergents, and chaotropic agents on polyphenol oxidase activity from dormant saffron (Crocus stivus L.) corms. J Agric Food Chem 55: 3713-3719.
29. Selinheimo E, NiEidhin D, Steffensen C, Nielsen J, Lomascolo A, Halaouli S, Record E, O'Beirne D, Buchert J, Kruus K (2007) Comparison of the characteristics of fungal and plant tyrosinases. J Biotechnol 130: 471-480.
30. Sendovski M, Kanteev M, Shuster V, Adir N, Fishman A (2010) Primary x-ray crystallographic analysis of a bacterial tyrosinase from Bacillus megaterium. Acta Crystallogr Sect F Struct Biol Crystallogr 66: 1101-1103.
31. Sendovski M, Kanteev M, Shuster Ben-Yosef V, Adir N, Fishman A (2011) First structures of an active bacterial tyrosinase reveal copper plasticity. J Mol Biol 405: 227-237.
32. Shuster Ben-Yosef V, Sendovski M, Fishman A (2010) Directed evolution of tyrosinase for enhanced monophenolase/diphenolase activity ratio. Enzyme Microb Technol 47: 372-376.
33. Shuster V, Fishman A (2009) Isolation, cloning and characterization of a tyrosinase with improved activity in organic solvents from Bacillus megaterium. J Mol Microbiol Biotechnol 17: 188-200.
34. Skubak P, Murshudov GN, Pannu NS (2004) Direct incorporation of experimental phase information in model refinement. Acta Crystallogr Sect F Struct Biol Crystallogr 60: 2196-2201.
35. van Holde KE, Miller KI, Decker H (2001) Hemocyanins and invertebrate evolution. J Biol Chem 276: 15563-15566.
36. Wang G, Aazaz A, Peng Z, Shen P (2000) Cloning and overexpression of a tyrosinase gene mel from Pseudomonas maltophila. FEMS Microbiol Lett 185: 23-27.
37. Xiang J, Fan J-B, Chen N, Chen J, Liang Y (2006) Interaction of cellulase with sodium dodecyl sulfate at critical micelle concentration level. Colloids Surf B Biointerfaces 49: 175-180.
38. Yang Z (2009) Hofmeister effects: an explanation for the impact of ionic liquids on biocatalysis. J Biotechnol 144: 12-22.
39. Yang Z, Pan W (2005) Ionic liquids: green solvents for nonaqueous biocatalysis. Enzyme Microb Technol 37: 19-28.
40. Yang Z, Yue YJ, Xing M (2008) Tyrosinase activity in ionic liquids. Biotechnol Lett 30: 153-158.
41. Yang Z, Yue YJ, Huang WC, Zhuang XM, Chen ZT, Xing M (2009) Importance of the ionic nature of ionic liquids in affecting enzyme performance. J Biochem (Tokyo) 145: 355-364.
42. Zhou J, Shi P, Zhang R, Huang H, Meng K, Yang P, Yao B (2011) Symbiotic Streptomyces sp. TN119 GH 11 xylanase: a new pH-stable, protease- and SDS-resistant xylanase. J Ind Microbiol Biotechnol 38: 523-530.