메뉴 건너뛰기




Volumn 183, Issue , 2015, Pages 49-57

Polyphenoloxidase from Riesling and Dornfelder wine grapes (Vitis vinifera) is a tyrosinase

Author keywords

Dornfelder; Grapes; Polyphenoloxidase; Riesling; Tyrosinase activity

Indexed keywords

DYES; MOLECULAR DYNAMICS;

EID: 84925357694     PISSN: 03088146     EISSN: 18737072     Source Type: Journal    
DOI: 10.1016/j.foodchem.2015.03.016     Document Type: Article
Times cited : (40)

References (48)
  • 1
    • 73949127552 scopus 로고    scopus 로고
    • Grape skins (Vitis vinifera L.) catalyze the in vitro enzymatic hydroxylation of p-coumaric acid to caffeic acid
    • A. Arnous, and A.S. Meyer Grape skins (Vitis vinifera L.) catalyze the in vitro enzymatic hydroxylation of p-coumaric acid to caffeic acid Biotechnology Letters 31 2009 1953 1960
    • (2009) Biotechnology Letters , vol.31 , pp. 1953-1960
    • Arnous, A.1    Meyer, A.S.2
  • 3
    • 1642463826 scopus 로고    scopus 로고
    • The prophenoloxidase-activating system in invertebrates
    • L. Cerenius, and K. Soderhall The prophenoloxidase-activating system in invertebrates Immunological Reviews 198 2004 116 126
    • (2004) Immunological Reviews , vol.198 , pp. 116-126
    • Cerenius, L.1    Soderhall, K.2
  • 4
    • 0034780048 scopus 로고    scopus 로고
    • Evidence for a tetrameric form of iceberg lettuce (Lactuca sativa L.) polyphenol oxidase: Purification and characterization
    • S. Chazarra, F. García-Carmona, and J. Cabanes Evidence for a tetrameric form of iceberg lettuce (Lactuca sativa L.) polyphenol oxidase: Purification and characterization Journal of Agriculture and Food Chemistry 49 2001 4870 4875
    • (2001) Journal of Agriculture and Food Chemistry , vol.49 , pp. 4870-4875
    • Chazarra, S.1    García-Carmona, F.2    Cabanes, J.3
  • 7
    • 78449267778 scopus 로고    scopus 로고
    • Possible role of phosphatidylserine-hemocyanin interaction in the innate immune response of Limulus polyphemus
    • C.J. Coates, S.M. Kelly, and J. Nairn Possible role of phosphatidylserine-hemocyanin interaction in the innate immune response of Limulus polyphemus Developmental and Comparative Immunology 35 2011 155 163
    • (2011) Developmental and Comparative Immunology , vol.35 , pp. 155-163
    • Coates, C.J.1    Kelly, S.M.2    Nairn, J.3
  • 8
    • 0032525161 scopus 로고    scopus 로고
    • Crystal structure of a function unit form Octopus hemocyanin
    • M. Cuff, K. Miller, and W. Hendrickson Crystal structure of a function unit form Octopus hemocyanin Journal of Molecular Biology 278 1998 855 870
    • (1998) Journal of Molecular Biology , vol.278 , pp. 855-870
    • Cuff, M.1    Miller, K.2    Hendrickson, W.3
  • 9
    • 0032476016 scopus 로고    scopus 로고
    • Tarantula hemocyanin shows phenoloxidase activity
    • H. Decker, and T. Rimke Tarantula hemocyanin shows phenoloxidase activity Journal of Biological Chemistry 273 1998 25889 25892
    • (1998) Journal of Biological Chemistry , vol.273 , pp. 25889-25892
    • Decker, H.1    Rimke, T.2
  • 10
    • 0035947641 scopus 로고    scopus 로고
    • SDS-induced phenoloxidase activity in hemocyanins from Limulus polyphemus, Eurypelma californicum and Cancer magister
    • H. Decker, M. Ryan, and E. Jaenicke SDS-induced phenoloxidase activity in hemocyanins from Limulus polyphemus, Eurypelma californicum and Cancer magister Journal of Biological Chemistry 276 2001 17796 17799
    • (2001) Journal of Biological Chemistry , vol.276 , pp. 17796-17799
    • Decker, H.1    Ryan, M.2    Jaenicke, E.3
  • 12
    • 77949272214 scopus 로고    scopus 로고
    • Structural and mechanistic insights into the oxy form of tyrosinase from molecular dynamics simulations
    • R.J. Deeth, and C. Diedrich Structural and mechanistic insights into the oxy form of tyrosinase from molecular dynamics simulations Journal of Biological Inorganic Chemistry 15 2010 117 129
    • (2010) Journal of Biological Inorganic Chemistry , vol.15 , pp. 117-129
    • Deeth, R.J.1    Diedrich, C.2
  • 13
    • 0031982612 scopus 로고    scopus 로고
    • Determination of molecular parameters by fitting sedimentation data to finite element solutions of the Lamm equation
    • B. Demeler, and H. Saber Determination of molecular parameters by fitting sedimentation data to finite element solutions of the Lamm equation Biophysical Journal 74 1998 444 454
    • (1998) Biophysical Journal , vol.74 , pp. 444-454
    • Demeler, B.1    Saber, H.2
  • 14
    • 84865435097 scopus 로고    scopus 로고
    • Site-directed mutagenesis of a tetrameric dandelion polyphenol oxidase (PPO-6) reveals the site of subunit interaction
    • M.E. Dirks-Hofmeister, J.K. Inlow, and B.M. Moerschbacher Site-directed mutagenesis of a tetrameric dandelion polyphenol oxidase (PPO-6) reveals the site of subunit interaction Plant Molecular Biology 80 2012 203 217
    • (2012) Plant Molecular Biology , vol.80 , pp. 203-217
    • Dirks-Hofmeister, M.E.1    Inlow, J.K.2    Moerschbacher, B.M.3
  • 15
    • 0028519224 scopus 로고
    • Molecular cloning and characterisation of grape berry polyphenol oxidase
    • I.B. Dry, and S.P. Robinson Molecular cloning and characterisation of grape berry polyphenol oxidase Plant Molecular Biology 26 1994 495 502
    • (1994) Plant Molecular Biology , vol.26 , pp. 495-502
    • Dry, I.B.1    Robinson, S.P.2
  • 16
    • 0242663237 scopus 로고    scopus 로고
    • A point-charge force field for molecular mechanics simulations of proteins based on condensed-phase quantum mechanical calculations
    • Y. Duan, C. Wu, S. Chowdhury, M.C. Lee, G. Xiong, and W. Zhang A point-charge force field for molecular mechanics simulations of proteins based on condensed-phase quantum mechanical calculations Journal of Computational Chemistry 24 2003 1999 2012
    • (2003) Journal of Computational Chemistry , vol.24 , pp. 1999-2012
    • Duan, Y.1    Wu, C.2    Chowdhury, S.3    Lee, M.C.4    Xiong, G.5    Zhang, W.6
  • 18
    • 84905233254 scopus 로고    scopus 로고
    • Determination of tyrosinase substrate-binding modes reveals mechanistic differences between type-3 copper proteins
    • M. Goldfeder, M. Kanteev, S. Isaschar-Ovdat, N. Adir, and A. Fishman Determination of tyrosinase substrate-binding modes reveals mechanistic differences between type-3 copper proteins Nature Communications 5 2014 4505
    • (2014) Nature Communications , vol.5 , pp. 4505
    • Goldfeder, M.1    Kanteev, M.2    Isaschar-Ovdat, S.3    Adir, N.4    Fishman, A.5
  • 19
    • 84885102778 scopus 로고    scopus 로고
    • Advances in electronic structure theory: GAMESS a decade later
    • C.E. Dykstra, G. Frenking, K.S. Kim, G.E. Scuseria, Elsevier Amsterdam
    • M.S. Gordon, and M.W. Schmidt Advances in electronic structure theory: GAMESS a decade later C.E. Dykstra, G. Frenking, K.S. Kim, G.E. Scuseria, Theory and applications of computational chemistry: The first forty years 2005 Elsevier Amsterdam 1167 1189
    • (2005) Theory and Applications of Computational Chemistry: The First Forty Years , pp. 1167-1189
    • Gordon, M.S.1    Schmidt, M.W.2
  • 20
    • 0037070360 scopus 로고    scopus 로고
    • Diphenol activation of the monophenolase and diphenolase activities of field bean (Dolichos lablab) polyphenol oxidase
    • L.R. Gowda, and B. Paul Diphenol activation of the monophenolase and diphenolase activities of field bean (Dolichos lablab) polyphenol oxidase Journal of Agriculture and Food Chemistry 50 2002 1608 1614
    • (2002) Journal of Agriculture and Food Chemistry , vol.50 , pp. 1608-1614
    • Gowda, L.R.1    Paul, B.2
  • 21
    • 33645163110 scopus 로고    scopus 로고
    • Fungal tyrosinases: New prospects in molecular characteristics, bioengineering and biotechnological applications
    • S. Halaouli, M. Asther, J.C. Sigoillot, M. Hamdi, and A. Lomascolo Fungal tyrosinases: new prospects in molecular characteristics, bioengineering and biotechnological applications Journal of Applied Microbiology 100 2006 219 232
    • (2006) Journal of Applied Microbiology , vol.100 , pp. 219-232
    • Halaouli, S.1    Asther, M.2    Sigoillot, J.C.3    Hamdi, M.4    Lomascolo, A.5
  • 22
    • 79959257956 scopus 로고    scopus 로고
    • Crystal structure of Agaricus bisporus mushroom tyrosinase: Identity of the tetramer subunits and interaction with tropolone
    • W.T. Ismaya, H.J. Rozeboom, A. Weijn, J.J. Mes, F. Fusetti, and H.J. Wichers Crystal structure of Agaricus bisporus mushroom tyrosinase: Identity of the tetramer subunits and interaction with tropolone Biochemistry 50 2011 5477 5486
    • (2011) Biochemistry , vol.50 , pp. 5477-5486
    • Ismaya, W.T.1    Rozeboom, H.J.2    Weijn, A.3    Mes, J.J.4    Fusetti, F.5    Wichers, H.J.6
  • 23
    • 84870187723 scopus 로고    scopus 로고
    • Purification and structural characterisation of lipid transfer protein from red wine and grapes
    • N. Jaeckels, S. Tenzer, S. Rosfa, H. Schild, H. Decker, and P. Wigand Purification and structural characterisation of lipid transfer protein from red wine and grapes Food Chemistry 138 2013 263 269
    • (2013) Food Chemistry , vol.138 , pp. 263-269
    • Jaeckels, N.1    Tenzer, S.2    Rosfa, S.3    Schild, H.4    Decker, H.5    Wigand, P.6
  • 24
  • 25
    • 0037146488 scopus 로고    scopus 로고
    • Highly sensitive and fast protein detection with coomassie brilliant blue in sodium dodecyl sulfate-polyacrylamide gel electrophoresis
    • D. Kang, Y.S. Gho, M. Suh, and C. Kang Highly sensitive and fast protein detection with coomassie brilliant blue in sodium dodecyl sulfate-polyacrylamide gel electrophoresis Bulletin of the Korean Chemical Society 23 2002 1511 1512
    • (2002) Bulletin of the Korean Chemical Society , vol.23 , pp. 1511-1512
    • Kang, D.1    Gho, Y.S.2    Suh, M.3    Kang, C.4
  • 26
    • 10344223464 scopus 로고    scopus 로고
    • Making optimal use of empirical energy functions: Force-field parameterization in crystal space
    • E. Krieger, T. Darden, S. Nabuurs, A. Finkelstein, and G. Vriend Making optimal use of empirical energy functions: Force-field parameterization in crystal space Proteins 57 2004 678 683
    • (2004) Proteins , vol.57 , pp. 678-683
    • Krieger, E.1    Darden, T.2    Nabuurs, S.3    Finkelstein, A.4    Vriend, G.5
  • 27
    • 80053368395 scopus 로고    scopus 로고
    • Isolation and characterization of latent and active polyphenoloxidase in BRS Clara (CNPUV 154-147 × Centennial seedless) and BRS Morena (Marroo seedless × Centennial seedless) seedless table grapes
    • E.S. Lago-Vanzela, F.C. Pavezzi, N. Martin, E. Gomes, and R. Da Silva Isolation and characterization of latent and active polyphenoloxidase in BRS Clara (CNPUV 154-147 × Centennial seedless) and BRS Morena (Marroo seedless × Centennial seedless) seedless table grapes Plant Physiology and Biochemistry 49 2011 1251 1258
    • (2011) Plant Physiology and Biochemistry , vol.49 , pp. 1251-1258
    • Lago-Vanzela, E.S.1    Pavezzi, F.C.2    Martin, N.3    Gomes, E.4    Da Silva, R.5
  • 28
    • 0027981519 scopus 로고
    • Crystallographic analysis of oxygenated and deoxygenated states of arthropod hemocyanin shows unusual differences
    • K. Magnus, B. Hazes, H. Ton-That, C. Bonaventura, J. Bonaventura, and W. Hol Crystallographic analysis of oxygenated and deoxygenated states of arthropod hemocyanin shows unusual differences Proteins 19 1994 302 309
    • (1994) Proteins , vol.19 , pp. 302-309
    • Magnus, K.1    Hazes, B.2    Ton-That, H.3    Bonaventura, C.4    Bonaventura, J.5    Hol, W.6
  • 31
    • 84901953445 scopus 로고    scopus 로고
    • Crystal structure of a crustacean prophenoloxidase provides a clue to understanding the functionality of the type 3 copper proteins
    • T. Masuda, K. Momoji, T. Hirata, and B. Mikami Crystal structure of a crustacean prophenoloxidase provides a clue to understanding the functionality of the type 3 copper proteins FEBS Journal 281 2014 2659 2673
    • (2014) FEBS Journal , vol.281 , pp. 2659-2673
    • Masuda, T.1    Momoji, K.2    Hirata, T.3    Mikami, B.4
  • 32
    • 33646827679 scopus 로고    scopus 로고
    • Crystallographic evidence that the dinuclear copper center of tyrosinase is flexible during catalysis
    • Y. Matoba, T. Kumagai, A. Yamamoto, H. Yoshitsu, and M. Sugiyama Crystallographic evidence that the dinuclear copper center of tyrosinase is flexible during catalysis Journal of Biological Chemistry 281 2006 8981 8990
    • (2006) Journal of Biological Chemistry , vol.281 , pp. 8981-8990
    • Matoba, Y.1    Kumagai, T.2    Yamamoto, A.3    Yoshitsu, H.4    Sugiyama, M.5
  • 33
    • 33749517866 scopus 로고    scopus 로고
    • Polyphenol oxidases in plants and fungi: Going places? A review
    • A.M. Mayer Polyphenol oxidases in plants and fungi: Going places? A review Phytochemistry 67 2006 2318 2331
    • (2006) Phytochemistry , vol.67 , pp. 2318-2331
    • Mayer, A.M.1
  • 34
    • 0035983821 scopus 로고    scopus 로고
    • Laccase: New functions for an old enzyme
    • A.M. Mayer, and R.C. Staples Laccase: New functions for an old enzyme Phytochemistry 60 2002 551 565
    • (2002) Phytochemistry , vol.60 , pp. 551-565
    • Mayer, A.M.1    Staples, R.C.2
  • 37
    • 40449104572 scopus 로고    scopus 로고
    • Polyphenol oxidase and its relationship with oleuropein concentration in fruits and leaves of olive (Olea europaea) cv. 'Picual' trees during fruit ripening
    • F. Ortega-García, S. Blanco, M.A. Peinado, and J. Peragón Polyphenol oxidase and its relationship with oleuropein concentration in fruits and leaves of olive (Olea europaea) cv. 'Picual' trees during fruit ripening Tree Physiology 28 2008 45 54
    • (2008) Tree Physiology , vol.28 , pp. 45-54
    • Ortega-García, F.1    Blanco, S.2    Peinado, M.A.3    Peragón, J.4
  • 38
  • 40
    • 84897972480 scopus 로고    scopus 로고
    • Tyrosinase: The four oxidation states of the active site and their relevance to enzymatic activation, oxidation and inactivation
    • C.A. Ramsden, and P.A. Riley Tyrosinase: the four oxidation states of the active site and their relevance to enzymatic activation, oxidation and inactivation Bioorganic & Medicinal Chemistry 22 2014 2388 2395
    • (2014) Bioorganic & Medicinal Chemistry , vol.22 , pp. 2388-2395
    • Ramsden, C.A.1    Riley, P.A.2
  • 41
    • 79959386984 scopus 로고    scopus 로고
    • Copper-O2 reactivity of tyrosinase models towards external monophenolic substrates: Molecular mechanism and comparison with the enzyme
    • M. Rolff, J. Schottenheim, H. Decker, and F. Tuczek Copper-O2 reactivity of tyrosinase models towards external monophenolic substrates: Molecular mechanism and comparison with the enzyme Chemical Society Reviews 40 2011 4077 4098
    • (2011) Chemical Society Reviews , vol.40 , pp. 4077-4098
    • Rolff, M.1    Schottenheim, J.2    Decker, H.3    Tuczek, F.4
  • 44
    • 0031213675 scopus 로고    scopus 로고
    • Sequence and structural features of plant and fungal tyrosinases
    • C.W.G. van Gelder, W.H. Flurkey, and H.J. Wichers Sequence and structural features of plant and fungal tyrosinases Phytochemistry 45 1997 1309 1323
    • (1997) Phytochemistry , vol.45 , pp. 1309-1323
    • Van Gelder, C.W.G.1    Flurkey, W.H.2    Wichers, H.J.3
  • 46
    • 74849091074 scopus 로고    scopus 로고
    • Cloning, sequencing, purification, and crystal structure of Grenache (Vitis vinifera) polyphenol oxidase
    • Erratum. In: Journal of Agriculture and Food Chemistry, 58, 3867
    • V.M. Virador, J.P. Reyes Grajeda, A. Blanco-Labra, E. Mendiola-Olaya, G.M. Smith, and A. Moreno Cloning, sequencing, purification, and crystal structure of Grenache (Vitis vinifera) polyphenol oxidase Journal of Agriculture and Food Chemistry 58 2010 1189 1201 Erratum. In: Journal of Agriculture and Food Chemistry, 58, 3867
    • (2010) Journal of Agriculture and Food Chemistry , vol.58 , pp. 1189-1201
    • Virador, V.M.1    Reyes Grajeda, J.P.2    Blanco-Labra, A.3    Mendiola-Olaya, E.4    Smith, G.M.5    Moreno, A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.