Influencing the monophenolase/diphenolase activity ratio in tyrosinase

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1834, Issue 3, 2013, Pages 629-633

  Goldfeder, Mor ^a   Kanteev, Margarita ^a   Adir, Noam ^a   Fishman, Ayelet ^a  

^a TECHNION ISRAEL INSTITUTE OF TECHNOLOGY   (Israel)

Author keywords

Bacillus megaterium; Copper; Diphenol; Rational design; Tyrosinase

Indexed keywords

CATECHOL OXIDASE; COPPER; DIPHENOL DERIVATIVE; DIPHENOLASE; ENZYME VARIANT; MONOPHENOL DERIVATIVE; MONOPHENOL MONOOXYGENASE; PHENOL DERIVATIVE; QUINONE DERIVATIVE; UNCLASSIFIED DRUG;

ARTICLE; BACILLUS MEGATERIUM; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME ENGINEERING; ENZYME MECHANISM; ENZYME SPECIFICITY; ENZYME STRUCTURE; ENZYME SUBSTRATE; NONHUMAN; OXIDATION; PRIORITY JOURNAL; SWEET POTATO;

AMINO ACID SUBSTITUTION; BACILLUS MEGATERIUM; BACTERIAL PROTEINS; BIOCATALYSIS; CATALYTIC DOMAIN; CATECHOL OXIDASE; COPPER; CRYSTALLOGRAPHY, X-RAY; IPOMOEA BATATAS; KINETICS; LEVODOPA; MODELS, MOLECULAR; MONOPHENOL MONOOXYGENASE; MUTATION; OXIDATION-REDUCTION; OXIDOREDUCTASES; PLANT PROTEINS; SUBSTRATE SPECIFICITY; TYROSINE; VALINE;

BACILLUS MEGATERIUM; IPOMOEA BATATAS;

EID: 84872974999     PISSN: 15709639     EISSN: 18781454     Source Type: Journal    
DOI: 10.1016/j.bbapap.2012.12.021     Document Type: Article

References (32)

1. H. Claus, and H. Decker Bacterial tyrosinases Syst. Appl. Microbiol. 29 2006 3 14
2. S.G. Burton Oxidizing enzymes as biocatalysts Trends Biotechnol. 21 2003 543 549
3. E. Selinheimo, D. NiEidhin, C. Steffensen, J. Nielsen, A. Lomascolo, S. Halaouli, E. Record, D. O'Beirne, J. Buchert, and K. Kruus Comparison of the characteristics of fungal and plant tyrosinases J. Biotechnol. 130 2007 471 480
4. M.V. Martinez, and J.R. Whitaker The biochemistry and control of enzymatic browning Trends Food Sci. Technol. 6 1995 195 200
5. H. Decker, and F. Tuczek Tyrosinase/catecholoxidase activity of hemocyanins: structural basis and molecular mechanism Trends Biochem. Sci. 25 2000 392 397
6. C. Olivares, J.C. Garcia-Borron, and F. Solano Identification of active site residues involved in metal cofactor binding and stereospecific substrate recognition in mammalian tyrosinase. Implications to the catalytic cycle Biochemistry 41 2002 679 686
7. C. Olivares, and F. Solano New insights into the active site structure and catalytic mechanism of tyrosinase and its related proteins Pigment Cell Melanoma Res. 22 2009 750 760
8. H. Decker, T. Schweikardt, D. Nillius, U. Salzbrunn, E. Jaenicke, and F. Tuczek Similar enzyme activation and catalysis in hemocyanins and tyrosinases Gene 398 2007 183 191
9. S. Itoh, and S. Fukuzumi Monooxygenase activity of type 3 copper proteins Acc. Chem. Res. 40 2007 592 600
10. K.E. van Holde, K.I. Miller, and H. Decker Hemocyanins and invertebrate evolution J. Biol. Chem. 276 2001 15563 15566
11. T. Klabunde, C. Eicken, J.C. Sacchettini, and B. Krebs Crystal structure of plant catechol oxidase containing a dicopper center Nat. Struct. Biol. 5 1998 1084 1090
12. S. Halaouli, M. Asther, J.C. Sigoillot, M. Hamdi, and A. Lomascolo Fungal tyrosinases: new prospects in molecular characteristics, bioengineering and biotechnological applications J. Appl. Microbiol. 100 2006 219 232
13. Y. Kawamura-Konishi, M. Tsuji, S. Hatana, M. Asanuma, D. Kakuta, T. Kawano, E.B. Mukouyama, H. Goto, and H. Suzuki Purification, characterization, and molecular cloning of tyrosinase from Pholiota nameko Biosci. Biotechnol. Biochem. 71 2007 1752 1760
14. L.C. Nolan, and K.E. O'Connor 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 2007 1045 1050
15. G. Wang, A. Aazaz, Z. Peng, and P. Shen Cloning and overexpression of a tyrosinase gene mel from Pseudomonas maltophila FEMS Microbiol. Lett. 185 2000 23 27
16. C.A. Ramsden, M.R.L. Stratford, and P.A. Riley The influence of catechol structure on the suicide-inactivation of tyrosinase Org. Biomol. Chem. 7 2009 3388 3390
17. D. Hernandez-Romero, A. Sanchez-Amat, and F. Solano A tyrosinase with an abnormally high tyrosine hydroxylase/dopa oxidase ratio FEBS J. 273 2006 257 270
18. V. Shuster Ben-Yosef, M. Sendovski, and A. Fishman Directed evolution of tyrosinase for enhanced monophenolase/diphenolase activity ratio Enzyme Microb. Technol. 47 2010 372 376
19. V. Shuster, and A. Fishman Isolation, cloning and characterization of a tyrosinase with improved activity in organic solvents from Bacillus megaterium J. Mol. Microbiol. Biotechnol. 17 2009 188 200
20. M. Sendovski, M. Kanteev, V.S. Ben-Yosef, N. Adir, and A. Fishman First structures of an active bacterial tyrosinase reveal copper plasticity J. Mol. Biol. 405 2011 227 237
21. M. Sendovski, M. Kanteev, V. Shuster, N. Adir, and A. Fishman Primary X-ray crystallographic analysis of a bacterial tyrosinase from Bacillus megaterium Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 66 2010 1101 1103
22. J.N. Rodriguez-Lopez, J. Escribano, and F. Garciacanovas A continuous spectrophotometric method for the determination of monophenolase activity of tyrosinase using 3-methyl-2-benzothiazolinone hydrazone Anal. Biochem. 216 1994 205 212
23. A.G.W. Leslie Joint CCP4 + ESF-EAMCB Newsletter on protein crystallography 1992 (No. 26)
24. A.J. McCoy Solving structures of protein complexes by molecular replacement with Phaser Acta Crystallogr., Sect. D Biol. Crystallogr. 63 2007 32 41
25. P.D. Adams, P.V. Afonine, G. Bunkoczi, V.B. Chen, I.W. Davis, N. Echols, J.J. Headd, L.W. Hung, G.J. Kapral, R.W. Grosse-Kunstleve, A.J. McCoy, N.W. Moriarty, R. Oeffner, R.J. Read, D.C. Richardson, J.S. Richardson, T.C. Terwilliger, and P.H. Zwart PHENIX: a comprehensive Python-based system for macromolecular structure solution Acta Crystallogr., Sect. D Biol. Crystallogr. 66 2010 213 221
26. P. Emsley, and K. Cowtan Coot: model-building tools for molecular graphics Acta Crystallogr., Sect. D Biol. Crystallogr. 60 2004 2126 2132
27. Y. Matoba, T. Kumagai, A. Yamamoto, H. Yoshitsu, and M. Sugiyama Crystallographic evidence that the dinuclear copper center of tyrosinase is flexible during catalysis J. Biol. Chem. 281 2006 8981 8990
28. W.T. Ismaya, H.t.J. Rozeboom, A. Weijn, J.J. Mes, F. Fusetti, H.J. Wichers, and B.W. Dijkstra Crystal structure of Agaricus bisporus mushroom tyrosinase: identity of the tetramer subunits and interaction with tropolone Biochemistry 50 2011 5477 5486
29. H. Decker, T. Schweikardt, and F. Tuczek The first crystal structure of tyrosinase: all questions answered? Angew. Chem. Int. Ed Engl. 45 2006 4546 4550
30. J.L. Muñoz-Muñoz, J. Berna, F. Garcia-Molina, P.A. Garcia-Ruiz, J. Tudela, J.N. Rodriguez-Lopez, and F. Garcia-Canovas Unravelling the suicide inactivation of tyrosinase: a discrimination between mechanisms J. Mol. Catal. B: Enzym. 75 2012 11 19
31. C.A. Ramsden, and P.A. Riley Mechanistic studies of tyrosinase suicide inactivation Arkivoc 1 2010 260 274
32. J.L. Muñoz-muñoz, F. García-molina, P.A. García-ruiz, M. Molina-alarcón, J. Tudela, F. García- cánovas, and J.N. Rodríguez-lópez Phenolic substrates and suicide inactivation of tyrosinase: kinetics and mechanism Biochem. J. 416 2008 431 440