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Volumn 34, Issue 2, 2010, Pages 308-328

Surveying allosteric cooperativity and cooperative inhibition in mushroom tyrosinase

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BASIDIOMYCOTA;

EID: 77953167382     PISSN: 01458884     EISSN: 17454514     Source Type: Journal    
DOI: 10.1111/j.1745-4514.2009.00280.x     Document Type: Article
Times cited : (15)

References (44)
  • 1
    • 23244445417 scopus 로고    scopus 로고
    • An empirical extremum principle for the Hill coefficient in ligand-protein interactions showing negative cooperativity
    • Abeliovich H. An empirical extremum principle for the Hill coefficient in ligand-protein interactions showing negative cooperativity. Biophys. J. 2005, 89:76-79.
    • (2005) Biophys. J. , vol.89 , pp. 76-79
    • Abeliovich, H.1
  • 3
    • 0032789591 scopus 로고    scopus 로고
    • Kinetic studies of hepatocyte UDP-glucuronosyltransferase: Evidence of an allosteric enzyme
    • Bruni S, Chang TMS. Kinetic studies of hepatocyte UDP-glucuronosyltransferase: Evidence of an allosteric enzyme. Artif. Cells Blood Substit. Immobil. Biotechnol. 1999, 27:343-356.
    • (1999) Artif. Cells Blood Substit. Immobil. Biotechnol. , vol.27 , pp. 343-356
    • Bruni, S.1    Chang, T.M.S.2
  • 5
    • 0016808110 scopus 로고
    • Diagnostic uses of Hill (Logit and Nernst) plots
    • Cornish-Bowden A, Koshland DE. Diagnostic uses of Hill (Logit and Nernst) plots. J. Mol. Biol. 1975, 95:201-212.
    • (1975) J. Mol. Biol. , vol.95 , pp. 201-212
    • Cornish-Bowden, A.1    Koshland, D.E.2
  • 6
    • 77953152503 scopus 로고    scopus 로고
    • US Patent.6,190,664 B1. Depigmenting cosmetic skin-care composition and use thereof
    • Damperiou C. 2001, US Patent.6,190,664 B1. Depigmenting cosmetic skin-care composition and use thereof
    • (2001)
    • Damperiou, C.1
  • 7
    • 3242801426 scopus 로고
    • A comparison of estimates of Michaelis-Menten kinetic constants from various linear transformations
    • Dowd JE, Riggs DS. A comparison of estimates of Michaelis-Menten kinetic constants from various linear transformations. J. Biol. Chem. 1965, 240:863-869.
    • (1965) J. Biol. Chem. , vol.240 , pp. 863-869
    • Dowd, J.E.1    Riggs, D.S.2
  • 9
    • 0024428239 scopus 로고
    • A kinetic-study of the suicide inactivation of an enzyme measured through coupling reactions - application to the suicide inactivation of tyrosinase
    • Escribano J, Tudela J, Garcia-Carmona F, Garcia-Canovas F. A kinetic-study of the suicide inactivation of an enzyme measured through coupling reactions - application to the suicide inactivation of tyrosinase. Biochem. J. 1989, 262:597-603.
    • (1989) Biochem. J. , vol.262 , pp. 597-603
    • Escribano, J.1    Tudela, J.2    Garcia-Carmona, F.3    Garcia-Canovas, F.4
  • 11
    • 84985294902 scopus 로고
    • Identification of tyrosinase in mushrooms by isoelectric-focusing
    • Flurkey WH. Identification of tyrosinase in mushrooms by isoelectric-focusing. J. Food Sci. 1991, 56:93-95.
    • (1991) J. Food Sci. , vol.56 , pp. 93-95
    • Flurkey, W.H.1
  • 14
    • 0012200165 scopus 로고    scopus 로고
    • Facile synthesis of catechol azo dyes
    • Haghbeen K, Tan EW. Facile synthesis of catechol azo dyes. J. Org. Chem. 1998, 63:4503-4505.
    • (1998) J. Org. Chem. , vol.63 , pp. 4503-4505
    • Haghbeen, K.1    Tan, E.W.2
  • 15
    • 0037216767 scopus 로고    scopus 로고
    • Direct spectrophotometric assay of monooxygenase and oxidase activities of mushroom tyrosinase in the presence of synthetic and natural substrates
    • Haghbeen K, Tan EW. Direct spectrophotometric assay of monooxygenase and oxidase activities of mushroom tyrosinase in the presence of synthetic and natural substrates. Anal. Biochem. 2003, 312:23-32.
    • (2003) Anal. Biochem. , vol.312 , pp. 23-32
    • Haghbeen, K.1    Tan, E.W.2
  • 17
    • 7744231644 scopus 로고    scopus 로고
    • Substrate share in the suicide inactivation of mushroom tyrosinase
    • Haghbeen K, Saboury AA, Karbassi F. Substrate share in the suicide inactivation of mushroom tyrosinase. Biochim. Bioph. Acta 2004b, 1675:139-146.
    • (2004) Biochim. Bioph. Acta , vol.1675 , pp. 139-146
    • Haghbeen, K.1    Saboury, A.A.2    Karbassi, F.3
  • 18
    • 33645163110 scopus 로고    scopus 로고
    • Fungal tyrosinases: New prospects in molecular characteristics, bioengineering and biotechnological applications
    • Halaouli S, Asther M, Sigoillot JC, Hamdi M, Lomascolo A. Fungal tyrosinases: New prospects in molecular characteristics, bioengineering and biotechnological applications. J. Appl. Microbiol. 2006, 100:219-232.
    • (2006) J. Appl. Microbiol. , vol.100 , pp. 219-232
    • Halaouli, S.1    Asther, M.2    Sigoillot, J.C.3    Hamdi, M.4    Lomascolo, A.5
  • 19
    • 0007292157 scopus 로고
    • Specificity of esterases 1. Identification of 2 pancreatic aliesterases
    • Hofstee BHJ. Specificity of esterases 1. Identification of 2 pancreatic aliesterases. J. Biol. Chem. 1952, 199:357-364.
    • (1952) J. Biol. Chem. , vol.199 , pp. 357-364
    • Hofstee, B.H.J.1
  • 21
    • 0037033008 scopus 로고    scopus 로고
    • Proteomics and models for enzyme cooperativity
    • Koshland DE, Hamadani K. Proteomics and models for enzyme cooperativity. J. Biol. Chem. 2002, 277:46841-46844.
    • (2002) J. Biol. Chem. , vol.277 , pp. 46841-46844
    • Koshland, D.E.1    Hamadani, K.2
  • 22
    • 0033933718 scopus 로고    scopus 로고
    • Flavonols from Heterotheca inuloides: Tyrosinase inhibitory activity and structural criteria
    • Kubo I, Kinst-Hori I, Chaudhuri SK, Kubo Y, Sanchez Y, Ogura T. Flavonols from Heterotheca inuloides: Tyrosinase inhibitory activity and structural criteria. Bioorg. Med. Chem. 2000, 8:1749-1755.
    • (2000) Bioorg. Med. Chem. , vol.8 , pp. 1749-1755
    • Kubo, I.1    Kinst-Hori, I.2    Chaudhuri, S.K.3    Kubo, Y.4    Sanchez, Y.5    Ogura, T.6
  • 23
    • 2542452214 scopus 로고    scopus 로고
    • 1st, Ed., Kluwer Academic/Plenum Publisher, New York, NY
    • Leskovac V. Comprehensive Enzyme Kinetics 2003, 1st, Ed., Kluwer Academic/Plenum Publisher, New York, NY
    • (2003) Comprehensive Enzyme Kinetics
    • Leskovac, V.1
  • 25
    • 77953158661 scopus 로고    scopus 로고
    • Fruit products, deterioration by browning
    • In, Springer US, New York, NY
    • Lozano J. Fruit products, deterioration by browning. Fruit Manufacturing 2006, 163-182. In, pp., Springer US, New York, NY
    • (2006) Fruit Manufacturing , pp. 163-182
    • Lozano, J.1
  • 26
    • 0025283332 scopus 로고
    • Benzoic acid inhibition of the alpha-isozyme, beta-isozyme, and gamma-isozyme of Agaricus bisporus tyrosinase
    • Menon S, Fleck RW, Young G, Strothkamp KG. Benzoic acid inhibition of the alpha-isozyme, beta-isozyme, and gamma-isozyme of Agaricus bisporus tyrosinase. Arch. Biochem. Biophys. 1990, 280:27-32.
    • (1990) Arch. Biochem. Biophys. , vol.280 , pp. 27-32
    • Menon, S.1    Fleck, R.W.2    Young, G.3    Strothkamp, K.G.4
  • 27
    • 73649152457 scopus 로고
    • Allosteric proteins and cellular control systems
    • Monod J, Changeux P, Jacob F. Allosteric proteins and cellular control systems. J. Mol. Biol. 1963, 6:306-329.
    • (1963) J. Mol. Biol. , vol.6 , pp. 306-329
    • Monod, J.1    Changeux, P.2    Jacob, F.3
  • 28
    • 0018861067 scopus 로고
    • Cooperativity in enzyme function: Equilibrium and kinetic aspects
    • Tabor H, Tabor CW. In, Part B, eds.) Academic Press, New York, NY
    • Neet KE. Cooperativity in enzyme function: Equilibrium and kinetic aspects. The Methods in Enzymology 1980, 139-191. Tabor HTabor CW. In, Vol. 64 Part B, eds.) pp., Academic Press, New York, NY
    • (1980) The Methods in Enzymology , vol.64 , pp. 139-191
    • Neet, K.E.1
  • 29
    • 77956994271 scopus 로고
    • Tyrosinase (mushroom)
    • Tabor H, Tabor CW. In, eds.) Academic Press, New York, NY
    • Nelson RM, Mason HS. Tyrosinase (mushroom). The Methods in Enzymology 1970, 626-633. Tabor H, Tabor CW. In, Vol. 17, eds.) pp., Academic Press, New York, NY
    • (1970) The Methods in Enzymology , vol.17 , pp. 626-633
    • Nelson, R.M.1    Mason, H.S.2
  • 30
    • 0344739851 scopus 로고    scopus 로고
    • Kinetic inactivation study of mushroom tyrosinase: Intermediate detection by denaturants
    • Park Y, Jung J, Kim D, Kim W, Hahn M, Yang J. Kinetic inactivation study of mushroom tyrosinase: Intermediate detection by denaturants. J. Protein Chem. 2003, 22:463-471.
    • (2003) J. Protein Chem. , vol.22 , pp. 463-471
    • Park, Y.1    Jung, J.2    Kim, D.3    Kim, W.4    Hahn, M.5    Yang, J.6
  • 31
    • 0023802428 scopus 로고
    • Co-operativity in seminal ribonuclease function - kinetic-studies
    • Piccoli R, Di Donato A, D'alkessio G. Co-operativity in seminal ribonuclease function - kinetic-studies. Biochem. J. 1988, 253:329-336.
    • (1988) Biochem. J. , vol.253 , pp. 329-336
    • Piccoli, R.1    Di Donato, A.2    D'alkessio, G.3
  • 33
    • 0000018665 scopus 로고
    • Polypeptide composition of two fungal tyrosinases
    • Robb DA, Gutteridge S. Polypeptide composition of two fungal tyrosinases. Phytochemistry 1981, 20:1481-1485.
    • (1981) Phytochemistry , vol.20 , pp. 1481-1485
    • Robb, D.A.1    Gutteridge, S.2
  • 35
    • 33845810528 scopus 로고    scopus 로고
    • The inhibitory effect of benzenethiol on the cresolase and catecholase activities of mushroom tyrosinase
    • Saboury AA, Zolghadri S, Haghbeen K, Moosavi-Movahedi AA. The inhibitory effect of benzenethiol on the cresolase and catecholase activities of mushroom tyrosinase. J. Enzyme Inhib. Med. Chem 2006, 21:711-717.
    • (2006) J. Enzyme Inhib. Med. Chem , vol.21 , pp. 711-717
    • Saboury, A.A.1    Zolghadri, S.2    Haghbeen, K.3    Moosavi-Movahedi, A.A.4
  • 38
    • 0035887477 scopus 로고    scopus 로고
    • Bifunctional polyphenol oxidases: Novel functions in plant pigment biosynthesis
    • Strack D, Schliemann W. Bifunctional polyphenol oxidases: Novel functions in plant pigment biosynthesis. Angew. Chem. Int. Ed. Engl. 2001, 40:3791-3794.
    • (2001) Angew. Chem. Int. Ed. Engl. , vol.40 , pp. 3791-3794
    • Strack, D.1    Schliemann, W.2
  • 40
  • 42
    • 33846648506 scopus 로고    scopus 로고
    • 3D-QSAR and molecular docking studies of benzaldehydethiosemicarbazone, benzaldehyde, benzoic acid and their derivatives as phenoloxidase inhibitors
    • Xue CB, Li Z, Wan-Chun L, Xian-Ye X, Lin J, Ting X. 3D-QSAR and molecular docking studies of benzaldehydethiosemicarbazone, benzaldehyde, benzoic acid and their derivatives as phenoloxidase inhibitors. Bioorg. Med. Chem. 2007a, 15:2006-2015.
    • (2007) Bioorg. Med. Chem. , vol.15 , pp. 2006-2015
    • Xue, C.B.1    Li, Z.2    Wan-Chun, L.3    Xian-Ye, X.4    Lin, J.5    Ting, X.6
  • 43
    • 36949024466 scopus 로고    scopus 로고
    • Inhibition kinetics of cabbage butterfly (Pieris rapae L.) larvae phenoloxidase activity by 3-hydroxy-4-methoxybenzaldehyde thiosemicarbazone
    • Xue CB, Wan-Chun L, Lin J, Xian-Ye X, Ting X, Lei Y. Inhibition kinetics of cabbage butterfly (Pieris rapae L.) larvae phenoloxidase activity by 3-hydroxy-4-methoxybenzaldehyde thiosemicarbazone. Appl. Biochem. Biotechnol. 2007b, 43(2):101-114.
    • (2007) Appl. Biochem. Biotechnol. , vol.43 , Issue.2 , pp. 101-114
    • Xue, C.B.1    Wan-Chun, L.2    Lin, J.3    Xian-Ye, X.4    Ting, X.5    Lei, Y.6
  • 44
    • 0142214624 scopus 로고    scopus 로고
    • Kinetic evaluation of phenolase activity of tyrosinase using simplified catalytic reaction system
    • Yamazaki S, Itoh S. Kinetic evaluation of phenolase activity of tyrosinase using simplified catalytic reaction system. J. Am. Chem. Soc. 2003, 125:13034-13035.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 13034-13035
    • Yamazaki, S.1    Itoh, S.2


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