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Volumn 160, Issue 7, 2010, Pages 1896-1908

The effect of trifluoroethanol on tyrosinase activity and conformation: Inhibition kinetics and computational simulations

Author keywords

Docking simulation; Inhibition kinetics; Secondary structure; Trifluoroethanol; Tyrosinase

Indexed keywords

ACTIVE SITE; BIPHASIC PROCESS; COMPUTATIONAL SIMULATION; CONFORMATIONAL CHANGE; DOCKING SIMULATIONS; ENZYME INACTIVATION; FIRST ORDER; HYDROPHOBIC SURFACES; INHIBITION KINETICS; INHIBITORY EFFECT; KINETIC STUDY; SECONDARY STRUCTURES; STRUCTURAL CHANGE; TERTIARY STRUCTURES; TRIFLUOROETHANOL;

EID: 77949914143     PISSN: 02732289     EISSN: None     Source Type: Journal    
DOI: 10.1007/s12010-009-8730-9     Document Type: Article
Times cited : (35)

References (37)
  • 2
    • 0034255229 scopus 로고    scopus 로고
    • Conformational changes and inactivation of calf intestinal alkaline phosphatase in trifluoroethanol solutions
    • DOI 10.1016/S1357-2725(00)00025-X, PII S135727250000025X
    • YX Zhang Y Zhu HM Zhou 2000 The International Journal of Biochemistry & Cell Biology 32 887 894 10.1016/S1357-2725(00)00025-X 10.1016/S1357- 2725(00)00025-X 1:CAS:528:DC%2BD3cXlsVOrtrg%3D (Pubitemid 30625123)
    • (2000) International Journal of Biochemistry and Cell Biology , vol.32 , Issue.8 , pp. 887-894
    • Zhang, Y.-X.1    Zhu, Y.2    Zhou, H.-M.3
  • 3
    • 0032444658 scopus 로고    scopus 로고
    • Trifluoroethanol and colleagues: Cosolvents come of age. Recent studies with peptides and proteins
    • DOI 10.1017/S003358359800345X
    • M Buck 1998 Quarterly Reviews of Biophysics 31 297 355 10.1017/S003358359800345X 10.1017/S003358359800345X 1:CAS:528:DyaK1MXjvVeitLk%3D (Pubitemid 29213772)
    • (1998) Quarterly Reviews of Biophysics , vol.31 , Issue.3 , pp. 297-355
    • Buck, M.1
  • 5
    • 0141919670 scopus 로고    scopus 로고
    • Structural biology of the cell adhesion protein CD2: From molecular recognition to protein folding and design
    • DOI 10.2174/1389203033487063
    • AL Wilkins W Yang JJ Yang 2003 Current Protein & Peptide Science 4 367 373 10.2174/1389203033487063 10.2174/1389203033487063 1:CAS:528: DC%2BD3sXot1Wksb4%3D (Pubitemid 37236350)
    • (2003) Current Protein and Peptide Science , vol.4 , Issue.5 , pp. 367-373
    • Wilkins, A.L.1    Yang, W.2    Yang, J.J.3
  • 6
    • 0027492170 scopus 로고
    • A partially folded state of hen egg white lysozyme in trifluoroethanol: Structural characterization and implications for protein folding
    • DOI 10.1021/bi00053a036
    • M Buck SE Radford CM Dobson 1993 Biochemistry 32 669 678 10.1021/bi00053a036 10.1021/bi00053a036 1:CAS:528:DyaK3sXjsFWjtA%3D%3D (Pubitemid 23034908)
    • (1993) Biochemistry , vol.32 , Issue.2 , pp. 669-678
    • Buck, M.1    Radford, S.E.2    Dobson, C.M.3
  • 7
    • 0028978422 scopus 로고
    • 10.1006/jmbi.1994.0015 10.1006/jmbi.1994.0015 1:CAS:528: DyaK2MXjtFWhtLg%3D
    • K Shiraki K Nishikawa Y Goto 1995 Journal of Molecular Biology 245 180 194 10.1006/jmbi.1994.0015 10.1006/jmbi.1994.0015 1:CAS:528:DyaK2MXjtFWhtLg%3D
    • (1995) Journal of Molecular Biology , vol.245 , pp. 180-194
    • Shiraki, K.1    Nishikawa, K.2    Goto, Y.3
  • 8
    • 0034601093 scopus 로고    scopus 로고
    • 10.1002/1439-7633(20000703)1:1<49::AID-CBIC49>3.0.CO;2-A 10.1002/1439-7633(20000703)1:1<49::AID-CBIC49>3.0.CO;2-A 1:CAS:528:DC%2BD3cXlt1WrsLc%3D
    • CP Yiu MG Mateu AR Fersht 2000 ChemBioChem 1 49 55 10.1002/1439- 7633(20000703)1:1<49::AID-CBIC49>3.0.CO;2-A 10.1002/1439-7633(20000703)1: 1<49::AID-CBIC49>3.0.CO;2-A 1:CAS:528:DC%2BD3cXlt1WrsLc%3D
    • (2000) ChemBioChem , vol.1 , pp. 49-55
    • Yiu, C.P.1    Mateu, M.G.2    Fersht, A.R.3
  • 13
    • 33845977687 scopus 로고    scopus 로고
    • Role of electrostatic interactions in 2,2,2-trifluoroethanol-induced structural changes and aggregation of α-chymotrypsin
    • DOI 10.1016/j.abb.2006.10.031, PII S0003986106004176
    • N Rezaei-Ghaleh A Ebrahim-Habibi AA Moosavi-Movahedi M Nemat-Gorgani 2007 Archives of Biochemistry and Biophysics 457 160 169 10.1016/j.abb.2006.10.031 10.1016/j.abb.2006.10.031 1:CAS:528:DC%2BD2sXmtVGhsA%3D%3D (Pubitemid 46048696)
    • (2007) Archives of Biochemistry and Biophysics , vol.457 , Issue.2 , pp. 160-169
    • Rezaei-Ghaleh, N.1    Ebrahim-Habibi, A.2    Moosavi-Movahedi, A.A.3    Nemat-Gorgani, M.4
  • 15
    • 33947254483 scopus 로고    scopus 로고
    • Detection of the equilibrium folding intermediate of β-lactoglobulin in the presence of trifluoroethanol by mass spectrometry
    • DOI 10.1002/rcm.2940
    • G Invernizzi R Grandori 2007 Rapid Communications in Mass Spectrometry 21 1049 1052 10.1002/rcm.2940 10.1002/rcm.2940 1:CAS:528:DC%2BD2sXjsVSntLk%3D (Pubitemid 46426827)
    • (2007) Rapid Communications in Mass Spectrometry , vol.21 , Issue.6 , pp. 1049-1052
    • Invernizzi, G.1    Grandori, R.2
  • 16
    • 28444464509 scopus 로고    scopus 로고
    • Amyloid formation of a protein in the absence of initial unfolding and destabilization of the native state
    • DOI 10.1529/biophysj.105.067538
    • G Soldi F Bemporad S Torrassa A Relini M Ramazzotti N Taddei F Chiti 2005 Biophysical Journal 89 4234 4244 10.1529/biophysj.105.067538 10.1529/biophysj.105.067538 1:CAS:528:DC%2BD2MXhtlWms7zE (Pubitemid 41725642)
    • (2005) Biophysical Journal , vol.89 , Issue.6 , pp. 4234-4244
    • Soldi, G.1    Bemporad, F.2    Torrassa, S.3    Relini, A.4    Ramazzotti, M.5    Taddei, N.6    Chiti, F.7
  • 17
    • 0034255667 scopus 로고    scopus 로고
    • Tyrosinase/catecholoxidase activity of hemocyanins: Structural basis and molecular mechanism
    • DOI 10.1016/S0968-0004(00)01602-9, PII S0968000400016029
    • H Decker F Tuczek 2000 Trends in Biochemical Sciences 25 392 397 10.1016/S0968-0004(00)01602-9 10.1016/S0968-0004(00)01602-9 1:CAS:528: DC%2BD3cXlsVOqtr8%3D (Pubitemid 30497251)
    • (2000) Trends in Biochemical Sciences , vol.25 , Issue.8 , pp. 392-397
    • Decker, H.1    Tuczek, F.2
  • 19
    • 34248547038 scopus 로고    scopus 로고
    • Tyrosinase and ocular diseases: Some novel thoughts on the molecular basis of oculocutaneous albinism type 1
    • DOI 10.1016/j.preteyeres.2007.01.001, PII S135094620700002X
    • K Ray M Chaki M Senqupta 2007 Progress in Retinal and Eye Research 26 323 358 10.1016/j.preteyeres.2007.01.001 10.1016/j.preteyeres.2007.01.001 1:CAS:528:DC%2BD2sXlsF2qu7g%3D (Pubitemid 46756377)
    • (2007) Progress in Retinal and Eye Research , vol.26 , Issue.4 , pp. 323-358
    • Ray, K.1    Chaki, M.2    Sengupta, M.3
  • 22
    • 25444479368 scopus 로고    scopus 로고
    • - binding
    • DOI 10.1016/j.biochi.2005.06.006, PII S030090840500146X
    • YD Park SY Kim YJ Lyou JY Lee JM Yang 2005 Biochimie 87 931 937 10.1016/j.biochi.2005.06.006 10.1016/j.biochi.2005.06.006 1:CAS:528: DC%2BD2MXhtVKjtrzM (Pubitemid 41377152)
    • (2005) Biochimie , vol.87 , Issue.11 , pp. 931-937
    • Park, Y.-D.1    Kim, S.-Y.2    Lyou, Y.-J.3    Lee, J.-Y.4    Yang, J.-M.5
  • 23
    • 0034881136 scopus 로고    scopus 로고
    • Folding pathway for partially folded rabbit muscle creatine kinase
    • DOI 10.1139/bcb-79-4-479
    • YD Park WB Ou TW Yu HM Zhou 2001 Biochemistry and Cell Biology 79 479 487 10.1139/bcb-79-4-479 10.1139/bcb-79-4-479 1:CAS:528:DC%2BD3MXmt1emu7s%3D (Pubitemid 32744983)
    • (2001) Biochemistry and Cell Biology , vol.79 , Issue.4 , pp. 479-487
    • Park, Y.-D.1    Ou, W.-B.2    Yu, T.-W.3    Zhou, H.-M.4
  • 24
    • 17144364275 scopus 로고    scopus 로고
    • Catalysis of creatine kinase refolding by protein disulfide isomerase involves disulfide cross-link and dimer to tetramer switch
    • DOI 10.1074/jbc.M413882200
    • TJ Zhao WB Ou Q Xie Y Liu YB Yan HM Zhou 2005 The Journal of Biological Chemistry 280 13470 13476 10.1074/jbc.M413882200 10.1074/jbc.M413882200 1:CAS:528:DC%2BD2MXivV2ktr0%3D (Pubitemid 40517236)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.14 , pp. 13470-13476
    • Zhao, T.-J.1    Ou, W.-B.2    Xie, Q.3    Liu, Y.4    Yan, Y.-B.5    Zhou, H.-M.6
  • 26
    • 0346101566 scopus 로고    scopus 로고
    • Effect of Thiohydroxyl Compounds on Tyrosinase: Inactivation and Reactivation Study
    • DOI 10.1023/B:JOPC.0000008726.99095.48
    • YD Park SJ Lee KH Park SY Kim MJ Hahn JM Yang 2003 Journal of Protein Chemistry 22 613 623 10.1023/B:JOPC.0000008726.99095.48 10.1023/B:JOPC. 0000008726.99095.48 1:CAS:528:DC%2BD3sXpvVGnu74%3D (Pubitemid 38036724)
    • (2003) Journal of Protein Chemistry , vol.22 , Issue.7-8 , pp. 613-623
    • Park, Y.-D.1    Lee, S.-J.2    Park, K.-H.3    Kim, S.-Y.4    Hahn, M.-J.5    Yang, J.-M.6
  • 27
    • 0141978673 scopus 로고    scopus 로고
    • Comparative protein structure modeling by iterative alignment, model building and model assessment
    • DOI 10.1093/nar/gkg460
    • B John A Sali 2003 Nucleic Acids Research 31 3982 3992 10.1093/nar/gkg460 10.1093/nar/gkg460 1:CAS:528:DC%2BD3sXltl2ksbo%3D (Pubitemid 37442277)
    • (2003) Nucleic Acids Research , vol.31 , Issue.14 , pp. 3982-3992
    • John, B.1    Sali, A.2
  • 28
    • 0031718310 scopus 로고    scopus 로고
    • Homology modeling, model and software evaluation: Three related resources
    • DOI 10.1093/bioinformatics/14.6.523
    • R Rodriguez G Chinea N Lopez T Pons G Vriend 1998 Bioinformatics (Oxford, England) 14 523 528 10.1093/bioinformatics/14.6.523 10.1093/bioinformatics/14. 6.523 1:CAS:528:DyaK1cXmtFWlt7w%3D (Pubitemid 28416766)
    • (1998) Bioinformatics , vol.14 , Issue.6 , pp. 523-528
    • Rodriguez, R.1    Chinea, G.2    Lopez, N.3    Pons, T.4    Vriend, G.5
  • 29
    • 33947716119 scopus 로고    scopus 로고
    • Software news and update a semiempirical free energy force field with charge-based desolvation
    • DOI 10.1002/jcc.20634
    • R Huey GM Morris AJ Olson DS Goodsell 2007 Journal of Computational Chemistry 28 1145 1152 10.1002/jcc.20634 10.1002/jcc.20634 1:CAS:528: DC%2BD2sXjsVSms78%3D (Pubitemid 46506716)
    • (2007) Journal of Computational Chemistry , vol.28 , Issue.6 , pp. 1145-1152
    • Huey, R.1    Morris, G.M.2    Olson, A.J.3    Goodsell, D.S.4
  • 31
    • 42149150001 scopus 로고    scopus 로고
    • 10.1021/ci700193u 10.1021/ci700193u 1:CAS:528:DC%2BD1cXisVWlurs%3D
    • XQ Xie JZJ Chen 2008 Chem Inf Model 48 465 475 10.1021/ci700193u 10.1021/ci700193u 1:CAS:528:DC%2BD1cXisVWlurs%3D
    • (2008) Chem Inf Model , vol.48 , pp. 465-475
    • Xie, X.Q.1    Chen, J.Z.J.2
  • 32
    • 33646166939 scopus 로고    scopus 로고
    • Biochemistry
    • 10.1134/S000629790613013X 1:CAS:528:DC%2BD28XislSlurg%3D
    • X Wei S Ding Y Jiang XG Zeng HM Zhou 2006 Biochemistry Biokhimiia 71 S77 S82 10.1134/S000629790613013X 1:CAS:528:DC%2BD28XislSlurg%3D
    • (2006) Biokhimiia , vol.71
    • Wei, X.1    Ding, S.2    Jiang, Y.3    Zeng, X.G.4    Zhou, H.M.5
  • 36
    • 0344739851 scopus 로고    scopus 로고
    • Kinetic Inactivation Study of Mushroom Tyrosinase: Intermediate Detection by Denaturants
    • DOI 10.1023/B:JOPC.0000005462.05642.89
    • YD Park JY Jung DW Kim WS Kim MJ Hahn JM Yang 2003 Journal of Protein Chemistry 22 463 471 10.1023/B:JOPC.0000005462.05642.89 10.1023/B:JOPC. 0000005462.05642.89 1:CAS:528:DC%2BD3sXptlGlurY%3D (Pubitemid 37516776)
    • (2003) Journal of Protein Chemistry , vol.22 , Issue.5 , pp. 463-471
    • Park, Y.-D.1    Jung, J.-Y.2    Kim, D.-W.3    Kim, W.-S.4    Hahn, M.-J.5    Yang, J.-M.6
  • 37
    • 0029981024 scopus 로고    scopus 로고
    • Unfolding and refolding of Coprinus cinereus peroxidase at high pH, in urea, and at high temperature. Effect of organic and ionic additives on these processes
    • DOI 10.1021/bi953067l
    • JW Tams KG Welinder 1996 Biochemistry 35 7573 7579 10.1021/bi953067l 10.1021/bi953067l 1:CAS:528:DyaK28XjtVCiu7Y%3D (Pubitemid 26189826)
    • (1996) Biochemistry , vol.35 , Issue.23 , pp. 7573-7579
    • Tams, J.W.1    Welinder, K.G.2


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