메뉴 건너뛰기




Volumn 58, Issue 2, 2010, Pages 1189-1201

Erratum: Cloning, sequencing, purification, and crystal structure of grenache (vitis vinifera) polyphenol oxidase (Journal of Agricultural and Food Chemistry (2010) 58 (1189) DOI: 10.1021/jf902939q));Cloning, sequencing, purification, and crystal structure of grenache (VITIS vinifera) polyphenol oxidase

Author keywords

Activation of proenzyme; Catechol oxidase; Copper enzymes; Enzymatic browning; Polyphenol oxidase; Posttranslatlonal processing; Vitls vinifera

Indexed keywords

IPOMOEA BATATAS; VITACEAE; VITIS VINIFERA;

EID: 74849091074     PISSN: 00218561     EISSN: 15205118     Source Type: Journal    
DOI: 10.1021/jf100480v     Document Type: Erratum
Times cited : (124)

References (57)
  • 1
    • 0028519224 scopus 로고
    • Molecular cloning and characterisation of grape berry polyphenol oxidase
    • Dry, I. B.; Robinson, S. P. Molecular cloning and characterisation of grape berry polyphenol oxidase. Plant MoI Biol 1994, 26 (1), 495-502.
    • (1994) Plant MoI Biol , vol.26 , Issue.1 , pp. 495-502
    • Dry, I.B.1    Robinson, S.P.2
  • 2
    • 0000034469 scopus 로고
    • The biochemistry and control of enzymatic browning
    • Martinez, M. V.; Whitaker, J. R. The biochemistry and control of enzymatic browning. Tgnds Food ScL Technol. 1.995, 6,195-200.
    • (1995) Tgnds Food ScL Technol. , vol.6 , pp. 195-200
    • Martinez, M.V.1    Whitaker, J.R.2
  • 5
    • 0029379574 scopus 로고
    • Polyphenol oxidase in potato. A multigene family that exhibits differential expression patterns
    • Thygesen, P. W.; Dry, I. B.; Robinson, S. P. Polyphenol oxidase in potato. A multigene family that exhibits differential expression patterns, Plant. Physiol. 1995, 109 (2), 525-531
    • (1995) Plant. Physiol. , vol.109 , Issue.2 , pp. 525-531
    • Thygesen, P.W.1    Dry, I.B.2    Robinson, S.P.3
  • 6
    • 0026930134 scopus 로고
    • Cloning and characterization, of cDNAs coding for Vicia faba polyphenol oxidase
    • Cary, J. W.; Lax, A. R.; Flurkey, W. H. Cloning and characterization, of cDNAs coding for Vicia faba polyphenol oxidase. Plant Mol Biol. 1992, 20(2), 245-253
    • (1992) Plant Mol Biol. , vol.20 , Issue.2 , pp. 245-253
    • Cary, J.W.1    Lax, A.R.2    Flurkey, W.H.3
  • 7
    • 0014690535 scopus 로고
    • The multiple forms of mushroom tyrosinase
    • Jolley, R. L.; Nelson, R. M.; Robb, D. A. The multiple forms of mushroom tyrosinase. J. Biol. Chem. 1969, 244 (12), 3251-3257.
    • (1969) J. Biol. Chem. , vol.244 , Issue.12 , pp. 3251-3257
    • Jolley, R.L.1    Nelson, R.M.2    Robb, D.A.3
  • 8
    • 0031213675 scopus 로고    scopus 로고
    • Sequence and structural features of plant and fungal tyrosinases
    • van Gelder, C.; Flurkey, W.; Wichers, H. Sequence and structural features of plant and fungal tyrosinases, Phytochemistry 1997, 45 (7), 1309-1323.
    • (1997) Phytochemistry , vol.45 , Issue.7 , pp. 1309-1323
    • Van Gelder, C.1    Flurkey, W.2    Wichers, H.3
  • 9
    • 0028486184 scopus 로고
    • Import, targeting, and processing of a plant polyphenol oxidase
    • Sommer, A.; Ne'eman, E.; Steffens, J. C.; Mayer, A. M.; Harel, E. Import, targeting, and processing of a plant polyphenol oxidase. Plant Physiol 1994, 105 (4), 1301-1311
    • (1994) Plant Physiol , vol.105 , Issue.4 , pp. 1301-1311
    • Sommer, A.1    Ne'Eman, E.2    Steffens, J.C.3    Mayer, A.M.4    Harel, E.5
  • 10
    • 0000703705 scopus 로고
    • Purification and characterization of a prophenoloxidase activating enzyme from crayfish blood cells
    • Aspán, A.; Sturtevant, J.; Smith, V.; Söderhäll, K. Purification and characterization of a prophenoloxidase activating enzyme from crayfish blood cells, Insert Biochem. 1990, 20 (7), 709-718.
    • (1990) Insert Biochem. , vol.20 , Issue.7 , pp. 709-718
    • Aspán, A.1    Sturtevant, J.2    Smith, V.3    Söderhäll, K.4
  • 11
    • 33846493669 scopus 로고    scopus 로고
    • Increasing resistance of tomato to lepidopteran insects by overexpression of polyphenol oxidase
    • Thipyapong, P.; Mahanil, S.; Bhonwong, A.; Attajarusit, J.; Stout, M. J.; Steffens, J. C. Increasing resistance of tomato to lepidopteran insects by overexpression of polyphenol oxidase. Acta Hortic. 2004, 724, 29-38.
    • (2004) Acta Hortic. , vol.724 , pp. 29-38
    • Thipyapong, P.1    Mahanil, S.2    Bhonwong, A.3    Attajarusit, J.4    Stout, M.J.5    Steffens, J.C.6
  • 12
    • 33749517866 scopus 로고    scopus 로고
    • Polyphenol oxidases in plants and fungi: Going places? A review
    • DOI 10.1016/j.phytochem.2006.08.006, PII S0031942206004560
    • (12) Mayer, A. Polyphenol oxidases in plants and fungi: Going places? A review, Phytochemistry 2006, 67, 2318-2331. (Pubitemid 44527933)
    • (2006) Phytochemistry , vol.67 , Issue.21 , pp. 2318-2331
    • Mayer, A.M.1
  • 13
    • 0022130941 scopus 로고
    • Kcat inactivation of mushroom polyphenol oxidase
    • Golan-Goldhirsh, A.; Whitaker, J. R. Kcat inactivation of mushroom polyphenol oxidase. J. Mol Catal. 1985, 32,141-147.
    • (1985) J. Mol Catal. , vol.32 , pp. 141-147
    • Golan-Goldhirsh, A.1    Whitaker, J.R.2
  • 14
    • 0001623476 scopus 로고
    • Aberrant processing of polyphenol oxidase in a varegated grapevine mutant
    • Rathgen, A.; Robinson, S. Aberrant processing of polyphenol oxidase in a varegated grapevine mutant. Plant Physiol 1992, 99, 1619-1625.
    • (1992) Plant Physiol , vol.99 , pp. 1619-1625
    • Rathgen, A.1    Robinson, S.2
  • 15
    • 0020688520 scopus 로고
    • Neurospora tyrosinase: Structural, spectroscopic and catalytic properties
    • Lerch, K. Neurospora tyrosinase: structural, spectroscopic and catalytic properties. Mol. Cell Biochem. 1983, 52 (2), 125-138
    • (1983) Mol. Cell Biochem. , vol.52 , Issue.2 , pp. 125-138
    • Lerch, K.1
  • 16
    • 0002435340 scopus 로고
    • Molecular and active-site structure
    • Lee, C. Y., Whitaker, J. R., Eds.; ACS Publications: Washington, DC
    • Lerch, K. Tyrosinase: Molecular and active-site structure. In Enzymatic Browning and Its Prevention; Lee, C. Y., Whitaker, J. R., Eds.; ACS Publications: Washington, DC, 1995; Vol.600, pp 64-80.
    • (1995) Enzymatic Browning and Its Prevention , vol.600 , pp. 64-80
    • Tyrosinase, L.K.1
  • 17
    • 0000326880 scopus 로고
    • Polyphenol oxidase
    • Wong, D. W. S., Ed.; Chapman and Hall: New York
    • Whitaker, J. R. Polyphenol oxidase. In Food Enzymes: Structure and Mechanism; Wong, D. W. S., Ed.; Chapman and Hall: New York, 1995; pp 284-320.
    • (1995) Food Enzymes: Structure and Mechanism , pp. 284-320
    • Whitaker, J.R.1
  • 18
    • 0031760504 scopus 로고    scopus 로고
    • Crystal structure of a plant catechol oxidase containing a dicopper center
    • Klabunde, T.; Eicken, C.; Sacchettini, J. C.; Krebs, B. Crystal structure of a plant catechol oxidase containing a dicopper center. Nat. Struct. Biol 1998, 5 (12), 1084-1090
    • (1998) Nat. Struct. Biol , vol.5 , Issue.12 , pp. 1084-1090
    • Klabunde, T.1    Eicken, C.2    Sacchettini, J.C.3    Krebs, B.4
  • 19
    • 0020479141 scopus 로고
    • Primary structure of tyrosinase from Neurospora crassa: II Complete amino acid sequence and chemical structure of a tripeptide containing an unusual thioether
    • Lerch, K. Primary structure of tyrosinase from Neurospora crassa: II Complete amino acid sequence and chemical structure of a tripeptide containing an unusual thioether. J. Biol. Chem. 1982, 257, (10), 6414-6419.
    • (1982) J. Biol. Chem. , vol.257 , Issue.10 , pp. 6414-6419
    • Lerch, K.1
  • 20
    • 0024975122 scopus 로고
    • Crystal structure of hexameric haemocyanin from Panulirus interruptus refined at 3.2 A resolution
    • Volbeda, A.; Hol, W. G. Crystal structure of hexameric haemocyanin from Panulirus interruptus refined at 3.2 A resolution. J. Mol Biol. 1989, 209 (2), 249-279
    • (1989) J. Mol Biol. , vol.209 , Issue.2 , pp. 249-279
    • Volbeda, A.1    Hol, W.G.2
  • 21
    • 0028857352 scopus 로고
    • Yield and quality of RNA from, grape berries at different developmental stages
    • Franke, K. E.; Liu, Y.; Adams, D. O. Yield and quality of RNA from, grape berries at different developmental stages, Am. J. Enol. Vitic. 1995, 46(3), 315-318.
    • (1995) Am. J. Enol. Vitic. , vol.46 , Issue.3 , pp. 315-318
    • Franke, K.E.1    Liu, Y.2    Adams, D.O.3
  • 22
    • 0027143091 scopus 로고
    • DNA fingerprint characterization of some wine grape cultivars
    • Bowers, J. E.; Bandman, E. B.; Meredith, C. P. DNA Fingerprint Characterization of Some Wine Grape Cultivars. Am. J. Enol. Vitic. 1993, 44 (3), 266-274.
    • (1993) Am. J. Enol. Vitic. , vol.44 , Issue.3 , pp. 266-274
    • Bowers, J.E.1    Bandman, E.B.2    Meredith, C.P.3
  • 23
    • 0024212067 scopus 로고
    • Rapid production of full-length cDNAs from rare transcripts: Amplification, using a single gene-specific oligonucleotide primer
    • Frohman, M. A.; Dush, M. K..; Martin, G. R. Rapid production of full-length cDNAs from rare transcripts: amplification, using a single gene-specific oligonucleotide primer, Proc. Natl Acad. Sci U.S.A. 1988, 85 (23), 8998-9002.
    • (1988) Proc. Natl Acad. Sci U.S.A. , vol.85 , Issue.23 , pp. 8998-9002
    • Frohman, M.A.1    Dush, M.K.2    Martin, G.R.3
  • 24
    • 0002367719 scopus 로고
    • Optimization, of PCRs
    • M. A., Gelfand, D. H., Sninsky, J. J., White, T. J., Eds.; Academic Press, Inc.: San Diego
    • Innis, M. A.; Gelfand, D. H. Optimization, of PCRs. In PCR Protocols, a Guide to Methods and Applications; Innis, M. A., Gelfand, D. H., Sninsky, J. J., White, T. J., Eds.; Academic Press, Inc.: San Diego, 1990; pp 3-12.
    • (1990) PCR Protocols, A Guide to Methods and Applications; Innis , pp. 3-12
    • Innis, M.A.1    Gelfand, D.H.2
  • 27
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation, of microgram quantities of protein utilizing the principle of proteindye binding
    • Bradford, M. M. A rapid and sensitive method for the quantitation, of microgram quantities of protein utilizing the principle of proteindye binding, Anal. Biochem. 1976, 72, 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 28
    • 0002033148 scopus 로고
    • Enzyme-catalyzed oxidative browning of fruit products
    • Joslyn, M. A.; Ponting, A. Enzyme-catalyzed oxidative browning of fruit products. Adv. Food Res. 1950, 3, 1-44.
    • (1950) Adv. Food Res. , vol.3 , pp. 1-44
    • Joslyn, M.A.1    Ponting, A.2
  • 30
    • 0014939358 scopus 로고
    • Physicochemical and kinetic properties of mushroom tyrosinase
    • Duckworth, H.; Coleman, J. Physicochemical and kinetic properties of mushroom tyrosinase. J. Biol. Chem. 1970, 245 (7), 1613-1625.
    • (1970) J. Biol. Chem. , vol.245 , Issue.7 , pp. 1613-1625
    • Duckworth, H.1    Coleman, J.2
  • 31
    • 84988074679 scopus 로고
    • Improved silver staining of plant proteins, RNA and DNA in Polyacrylamide gels
    • Blum, H.; Beier, H.; Gross, H. J. Improved silver staining of plant proteins, RNA and DNA in Polyacrylamide gels. Electrophoresis 1987, 8 (2), 93-99.
    • (1987) Electrophoresis , vol.8 , Issue.2 , pp. 93-99
    • Blum, H.1    Beier, H.2    Gross, H.J.3
  • 32
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, N., The CCP4 Suite: Programs for Protein Crystallography, Acta Crystallogr. 1994, DSO, 760-763.
    • (1994) Acta Crystallogr. , vol.DSO , pp. 760-763
  • 33
    • 0029088608 scopus 로고
    • The 64 kDa polypeptide of spinach may not be the LHCII kinase, but a lumen-located polyphenol oxidase
    • Sokolenko, A.; Fulgosi, H.; Gal, A.; Altschmied, L.; Ohad, I.; Herrmann, R. G. The 64 kDa polypeptide of spinach may not be the LHCII kinase, but a lumen-located polyphenol oxidase. FEBS Lett. 1995, 371 (2), 176-180
    • (1995) FEBS Lett. , vol.371 , Issue.2 , pp. 176-180
    • Sokolenko, A.1    Fulgosi, H.2    Gal, A.3    Altschmied, L.4    Ohad, I.5    Herrmann, R.G.6
  • 34
    • 0034548365 scopus 로고    scopus 로고
    • Membrane localization of a rice calciumdependent protein kinase (CDPK) is mediated by myristoylation and palmitoylation
    • Martin, M.; Busconi, L. Membrane localization of a rice calciumdependent protein kinase (CDPK) is mediated by myristoylation and palmitoylation. Plant J. 2000, 24, 429-435.
    • (2000) Plant J. , vol.24 , pp. 429-435
    • Martin, M.1    Busconi, L.2
  • 35
    • 0028559432 scopus 로고
    • Expression of the tyrosinase-encoding gene in. a colorless melanophore mutant of the medaka fish, Oryzias latipes
    • Inagaki, H.; Bessho, Y.; Koga, A.; Hori, H. Expression of the tyrosinase-encoding gene in. a colorless melanophore mutant of the medaka fish, Oryzias latipes. Ggne 1994, 150 (2), 319-324.
    • (1994) Ggne , vol.150 , Issue.2 , pp. 319-324
    • Inagaki, H.1    Bessho, Y.2    Koga, A.3    Hori, H.4
  • 36
    • 0038523701 scopus 로고
    • Functional analysis of alternatively spliced tyrosinase gene transcripts
    • Muller, G.; Ruppert, S.; Schmid, E.; Schutz, G. Functional analysis of alternatively spliced tyrosinase gene transcripts. EMBO J. 1988, 7 (9), 2723-2730.
    • (1988) EMBO J. , vol.7 , Issue.9 , pp. 2723-2730
    • Muller, G.1    Ruppert, S.2    Schmid, E.3    Schutz, G.4
  • 37
    • 0029159295 scopus 로고
    • An apple polyphenol oxidase cDNA is up-regulated in wounded tissues
    • Boss, P. K.; Gardner, R. C.; Janssen, B. J.; Ross, G. S. An apple polyphenol oxidase cDNA is up-regulated in wounded tissues, Plant Mol. Biol 1995, 27 (2), 429-433
    • (1995) Plant Mol. Biol , vol.27 , Issue.2 , pp. 429-433
    • Boss, P.K.1    Gardner, R.C.2    Janssen, B.J.3    Ross, G.S.4
  • 38
    • 0029042098 scopus 로고
    • Spinach thylakoid polyphenol oxidase: Cloning, characterization, and relation to a putative protein kinase
    • Hind, G.; Marshak, D. R.; Coughlan, S. J. Spinach thylakoid polyphenol oxidase: cloning, characterization, and relation to a putative protein kinase, Biochemistry 1995, 34 (25), 8157-8164
    • (1995) Biochemistry , vol.34 , Issue.25 , pp. 8157-8164
    • Hind, G.1    Marshak, D.R.2    Coughlan, S.J.3
  • 39
    • 0037965469 scopus 로고    scopus 로고
    • Tyrosinases from, crustaceans form hexamers
    • Jaenicke, E.; Decker, H. Tyrosinases from, crustaceans form hexamers. Biochem. J. 2003, 371, 515-523.
    • (2003) Biochem. J. , vol.371 , pp. 515-523
    • Jaenicke, E.1    Decker, H.2
  • 40
    • 0000557828 scopus 로고
    • X-ray crystallographic studies of proteins
    • Matthews, B. X-ray crystallographic studies of proteins, Annu. Rev. Phys. Chem. 1976, 27, 493-523.
    • (1976) Annu. Rev. Phys. Chem. , vol.27 , pp. 493-523
    • Matthews, B.1
  • 41
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein, structures
    • Laskowski, R.; MacArthur, M.; Moss, D.; Thornton, J. PROCHECK: a program to check the stereochemical quality of protein, structures. J. Appl. Crystallogr. 1993, 26 (2), 283-291.
    • (1993) J. Appl. Crystallogr. , vol.26 , Issue.2 , pp. 283-291
    • Laskowski, R.1    MacArthur, M.2    Moss, D.3    Thornton, J.4
  • 42
    • 0026584720 scopus 로고
    • Phosphorylation of cytochrome b6 by the LHCII kinase associated with the cytochrome complex
    • Gal, A.; Herrmann, R.; Lottspeich, F.; Ohad, I, Phosphorylation of cytochrome b6 by the LHCII kinase associated with the cytochrome complex. FEBS Lett. 1992, 298 (1), 33-35.
    • (1992) FEBS Lett. , vol.298 , Issue.1 , pp. 33-35
    • Gal, A.1    Herrmann, R.2    Lottspeich, F.3    Ohad, I.4
  • 43
    • 29344448672 scopus 로고    scopus 로고
    • Comparative analysis of polyphenol oxidase from plant and fungal species
    • Marusek, C.; Trobaugh, N.; Flurkey, W.; Inlow, J. Comparative analysis of polyphenol oxidase from plant and fungal species. J. Inorg. Biochem. 2006, 100, 108-123.
    • (2006) J. Inorg. Biochem. , vol.100 , pp. 108-123
    • Marusek, C.1    Trobaugh, N.2    Flurkey, W.3    Inlow, J.4
  • 44
    • 34948873790 scopus 로고    scopus 로고
    • The regulation of skin pigmentation
    • Yamaguchi, T.; Brenner, M.; Hearing, V. J. The regulation of skin pigmentation. J. Biol. Chem. 2007, 282 (38), 27557-27561.
    • (2007) J. Biol. Chem. , vol.282 , Issue.38 , pp. 27557-27561
    • Yamaguchi, T.1    Brenner, M.2    Hearing, V.J.3
  • 48
    • 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
    • Ortega-García, F.; Blanco, S.; Ángeles Peinado, M.,; Peragón, J. Polyphenol oxidase and its relationship with, oleuropein concentration in fruits and leaves of olive (Olea europaea) cv. 'Picual' trees during fruit ripening. Trge Physiol. 2008, 25, 45-54.
    • (2008) Trge Physiol. , vol.25 , pp. 45-54
    • Ortega-García, F.1    Blanco, S.2    Ángeles Peinado, M.3    Peragón, J.4
  • 49
    • 33847076903 scopus 로고    scopus 로고
    • Identification of tunnels in proteins, nucleic acids, inorganic materials and molecular ensembles
    • Damborský, J.; Petřek, M,; Banáš, P.; Otyepka, M. Identification of tunnels in proteins, nucleic acids, inorganic materials and molecular ensembles, Biotechnol J. 2007, 2, 62-67.
    • (2007) Biotechnol J. , vol.2 , pp. 62-67
    • Damborský, J.1    Petřek, M.2    Banáš, P.3    Otyepka, M.4
  • 50
    • 0029137534 scopus 로고
    • Properties of carrot polyphenoloxidase
    • Söderhäll, I. Properties of carrot polyphenoloxidase. Phvtochemistry 1995, 39 (1), 33-38.
    • (1995) Phvtochemistry , vol.39 , Issue.1 , pp. 33-38
    • Söderhäll, I.1
  • 51
    • 0001286571 scopus 로고
    • Labelled tyrosinase from labelled substrate
    • Wood, B.; Ingraham, L. Labelled tyrosinase from labelled substrate. Nature 1965, 205, 291-292.
    • (1965) Nature , vol.205 , pp. 291-292
    • Wood, B.1    Ingraham, L.2
  • 53
    • 0032525161 scopus 로고    scopus 로고
    • Crystal structure of a functional unit from Octopus hemocyanin
    • Cuff, M.; Miller, K.; vanHolde, K..; Hendrickson, W. Crystal structure of a functional unit from Octopus hemocyanin. J. Mol Biol 1998, 278 (4), 855-870.
    • (1998) J. Mol Biol , vol.278 , Issue.4 , pp. 855-870
    • Cuff, M.1    Miller, K.2    VanHolde, K.3    Hendrickson, W.4
  • 54
    • 0001235603 scopus 로고
    • Broad bean leaf polyphenol oxidase is a 60-kilodalton protein susceptible to proteolytic cleavage
    • Robinson, S.; Dry, I. Broad bean leaf polyphenol oxidase is a 60-kilodalton protein susceptible to proteolytic cleavage. Plant Physiol. 1992, 99, 317-323.
    • (1992) Plant Physiol. , vol.99 , pp. 317-323
    • Robinson, S.1    Dry, I.2
  • 55
    • 0029901640 scopus 로고    scopus 로고
    • Analysis of compositionally biased regions in sequence databases
    • Wooten, J.; Federhen, S. Analysis of compositionally biased regions in sequence databases. Methods Enzymol 1996, 266, 554-571.
    • (1996) Methods Enzymol , vol.266 , pp. 554-571
    • Wooten, J.1    Federhen, S.2
  • 57
    • 0002219004 scopus 로고
    • Polyphenol oxidase and photosynthesis research
    • Trebst, A.; Depka, B. Polyphenol oxidase and photosynthesis research, Photosynth. Res. 1995, 46, 41-44.
    • (1995) Photosynth. Res. , vol.46 , pp. 41-44
    • Trebst, A.1    Depka, B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.