메뉴 건너뛰기




Volumn 62, Issue 49, 2014, Pages 11941-11948

Amino acid sequence of anionic peroxidase from the windmill palm tree trachycarpus fortunei

Author keywords

amino acid sequencing; glycosylation; MALDI TOF; palm; peroxidase; top down mass spectrometry

Indexed keywords

ESTERIFICATION; FORESTRY; GLYCOSYLATION; MASS SPECTROMETRY; MILLING MACHINES;

EID: 84916631295     PISSN: 00218561     EISSN: 15205118     Source Type: Journal    
DOI: 10.1021/jf504511h     Document Type: Article
Times cited : (7)

References (39)
  • 1
    • 84872421776 scopus 로고    scopus 로고
    • Do vacuolar peroxidases act as plant caretakers?
    • Zipor, G.; Oren-Shamir, M. Do vacuolar peroxidases act as plant caretakers? Plant Sci. 2013, 199, 41-47
    • (2013) Plant Sci. , vol.199 , pp. 41-47
    • Zipor, G.1    Oren-Shamir, M.2
  • 2
    • 23944527027 scopus 로고    scopus 로고
    • Structural determinants of plant peroxidase function
    • Veitch, N. C. Structural determinants of plant peroxidase function Phytochem. Rev. 2004, 3, 3-18
    • (2004) Phytochem. Rev. , vol.3 , pp. 3-18
    • Veitch, N.C.1
  • 4
    • 84872042119 scopus 로고    scopus 로고
    • Electrochemical sensing of hydrogen peroxide using metal nanoparticles: A review
    • Chen, S.; Yuan, R.; Chai, Y.; Hu, F. Electrochemical sensing of hydrogen peroxide using metal nanoparticles: A review Microchim. Acta 2013, 180, 15-32
    • (2013) Microchim. Acta , vol.180 , pp. 15-32
    • Chen, S.1    Yuan, R.2    Chai, Y.3    Hu, F.4
  • 5
    • 36549002218 scopus 로고    scopus 로고
    • Advances in immunochemical technologies for analysis of organic pollutants in the environment
    • Farré, M.; Kantiani, L.; Barceló, D. Advances in immunochemical technologies for analysis of organic pollutants in the environment TrAC, Trends Anal. Chem. 2007, 26, 1100-1112
    • (2007) TrAC, Trends Anal. Chem. , vol.26 , pp. 1100-1112
    • Farré, M.1    Kantiani, L.2    Barceló, D.3
  • 6
    • 79956326552 scopus 로고    scopus 로고
    • Biosensors for the determination of phenolic metabolites
    • Giardi, M. T. Rea, G. Berra, B. Springer: New York
    • Litescu, S. C.; Eremia, S.; Radu, G. L. Biosensors for the determination of phenolic metabolites. In Bio-Farms for Nutraceuticals; Giardi, M. T.; Rea, G.; Berra, B., Eds.; Springer: New York, 2010; pp 234-240.
    • (2010) Bio-Farms for Nutraceuticals , pp. 234-240
    • Litescu, S.C.1    Eremia, S.2    Radu, G.L.3
  • 7
    • 84888095188 scopus 로고    scopus 로고
    • Development of sandwich ELISA for detection and quantification of invertebrate major allergen tropomyosin by a monoclonal antibody
    • Zhang, H.; Lu, Y.; Ushio, H.; Shiomi, K. Development of sandwich ELISA for detection and quantification of invertebrate major allergen tropomyosin by a monoclonal antibody Food Chem. 2014, 150, 151-157
    • (2014) Food Chem. , vol.150 , pp. 151-157
    • Zhang, H.1    Lu, Y.2    Ushio, H.3    Shiomi, K.4
  • 8
    • 79960938080 scopus 로고    scopus 로고
    • Development of two highly sensitive immunoassays for detection of copper ions and a suite of relevant immunochemicals
    • Zhao, H.; Nan, T.; Tan, G.; Gao, W.; Cao, Z.; Sun, S.; Li, Z.; Li, Q. X.; Wang, B. Development of two highly sensitive immunoassays for detection of copper ions and a suite of relevant immunochemicals Anal. Chim. Acta 2011, 702, 102-108
    • (2011) Anal. Chim. Acta , vol.702 , pp. 102-108
    • Zhao, H.1    Nan, T.2    Tan, G.3    Gao, W.4    Cao, Z.5    Sun, S.6    Li, Z.7    Li, Q.X.8    Wang, B.9
  • 10
    • 26944481128 scopus 로고    scopus 로고
    • Palm tree peroxidase-based biosensor with unique characteristics for hydrogen peroxide monitoring
    • Alpeeva, I. S.; Niculescu-Nistor, M.; Leon, J. C.; Csöregi, E.; Sakharov, I. Yu. Palm tree peroxidase-based biosensor with unique characteristics for hydrogen peroxide monitoring Biosens. Bioelectron. 2005, 21, 742-748
    • (2005) Biosens. Bioelectron. , vol.21 , pp. 742-748
    • Alpeeva, I.S.1    Niculescu-Nistor, M.2    Leon, J.C.3    Csöregi, E.4    Sakharov I.Yu.5
  • 11
    • 0041880315 scopus 로고    scopus 로고
    • Synthesis of polyelectrolyte complexes of polyaniline and sulfonated polystyrene by palm tree peroxidase
    • Sakharov, I. Yu.; Vorobiev, A. C.; Leon, J. J. C. Synthesis of polyelectrolyte complexes of polyaniline and sulfonated polystyrene by palm tree peroxidase Enzyme Microb. Technol. 2003, 33, 661-667
    • (2003) Enzyme Microb. Technol. , vol.33 , pp. 661-667
    • Sakharov I.Yu.1    Vorobiev, A.C.2    Leon, J.J.C.3
  • 18
    • 79957613599 scopus 로고    scopus 로고
    • MEGA5: Molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods
    • Tamura, K.; Peterson, D.; Peterson, N.; Stecher, G.; Nei, M.; Kumar, S. MEGA5: Molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods Mol. Biol. Evol. 2011, 28, 2731-2739
    • (2011) Mol. Biol. Evol. , vol.28 , pp. 2731-2739
    • Tamura, K.1    Peterson, D.2    Peterson, N.3    Stecher, G.4    Nei, M.5    Kumar, S.6
  • 19
    • 0015229022 scopus 로고
    • Human erythrocyte membrane glycoprotein: A re-evaluation of the molecular weight as determined by SDS polyacrylamide gel electrophoresis
    • Segrest, J. P.; Jackson, R. L.; Andrews, E. P.; Marchesi, V. T. Human erythrocyte membrane glycoprotein: A re-evaluation of the molecular weight as determined by SDS polyacrylamide gel electrophoresis Biochem. Biophys. Res. Commun. 1971, 44, 390-395
    • (1971) Biochem. Biophys. Res. Commun. , vol.44 , pp. 390-395
    • Segrest, J.P.1    Jackson, R.L.2    Andrews, E.P.3    Marchesi, V.T.4
  • 20
    • 0034783572 scopus 로고    scopus 로고
    • Peroxidase from leaves of royal palm tree Roystonea regia: Purification and some properties
    • Sakharov, I. Yu.; Vesga B, M. K.; Galaev, I. Yu.; Sakharova, I. V.; Pletjushkina, O. Y. Peroxidase from leaves of royal palm tree Roystonea regia: Purification and some properties Plant Sci. 2001, 161, 853-860
    • (2001) Plant Sci. , vol.161 , pp. 853-860
    • Sakharov I.Yu.1    Vesga, B.M.K.2    Galaev I.Yu.3    Sakharova, I.V.4    Pletjushkina, O.Y.5
  • 21
    • 77951064458 scopus 로고    scopus 로고
    • Top-down de novo protein sequencing of a 13.6 kDa camelid single heavy chain antibody by matrix-assisted laser desorption ionization-time-of-flight/time-of-flight mass spectrometry
    • Resemann, A.; Wunderlich, D.; Rothbauer, U.; Warscheid, B.; Leonhardt, H.; Fuchser, J.; Kuhlmann, K.; Suckau, D. Top-down de novo protein sequencing of a 13.6 kDa camelid single heavy chain antibody by matrix-assisted laser desorption ionization-time-of-flight/time-of-flight mass spectrometry Anal. Chem. 2010, 82, 3283-3292
    • (2010) Anal. Chem. , vol.82 , pp. 3283-3292
    • Resemann, A.1    Wunderlich, D.2    Rothbauer, U.3    Warscheid, B.4    Leonhardt, H.5    Fuchser, J.6    Kuhlmann, K.7    Suckau, D.8
  • 22
    • 79959242453 scopus 로고    scopus 로고
    • Top-down sequencing of O -glycoproteins by in-source decay matrix-assisted laser desorption ionization mass spectrometry for glycosylation site analysis
    • Hanisch, F.-G. Top-down sequencing of O -glycoproteins by in-source decay matrix-assisted laser desorption ionization mass spectrometry for glycosylation site analysis Anal. Chem. 2011, 83, 4829-4837
    • (2011) Anal. Chem. , vol.83 , pp. 4829-4837
    • Hanisch, F.-G.1
  • 23
  • 24
    • 29944447302 scopus 로고    scopus 로고
    • Asymmetric glycosylation of soybean seed coat peroxidase
    • Gray, J. S. S.; Montgomery, R. Asymmetric glycosylation of soybean seed coat peroxidase Carbohydr. Res. 2006, 341, 198-209
    • (2006) Carbohydr. Res. , vol.341 , pp. 198-209
    • Gray, J.S.S.1    Montgomery, R.2
  • 25
  • 28
    • 32144432437 scopus 로고    scopus 로고
    • The SWISS-MODEL workspace: A web-based environment for protein structure homology modelling
    • Arnold, K.; Bordoli, L.; Kopp, J.; Schwede, T. The SWISS-MODEL workspace: A web-based environment for protein structure homology modelling Bioinformatics 2006, 22, 195-201
    • (2006) Bioinformatics , vol.22 , pp. 195-201
    • Arnold, K.1    Bordoli, L.2    Kopp, J.3    Schwede, T.4
  • 29
    • 0031715982 scopus 로고    scopus 로고
    • Protein structure alignment by incremental combinatorial extension (CE) of the optimal path
    • Shindyalov, I. N.; Bourne, P. E. Protein structure alignment by incremental combinatorial extension (CE) of the optimal path Protein Eng. 1998, 11, 739-747
    • (1998) Protein Eng. , vol.11 , pp. 739-747
    • Shindyalov, I.N.1    Bourne, P.E.2
  • 30
    • 0027764344 scopus 로고
    • Protein sequence alignments: A strategy for the hierarchical analysis of residue conservation
    • Livingstone, C. D.; Barton, G. J. Protein sequence alignments: a strategy for the hierarchical analysis of residue conservation CABIOS, Comput. Appl. Biosci. 1993, 9, 745-756
    • (1993) CABIOS, Comput. Appl. Biosci. , vol.9 , pp. 745-756
    • Livingstone, C.D.1    Barton, G.J.2
  • 31
    • 65449188232 scopus 로고    scopus 로고
    • Jalview Version 2 - A multiple sequence alignment editor and analysis workbench
    • Waterhouse, A. M.; Procter, J. B.; Martin, D. M. A.; Clamp, M.; Barton, G. J. Jalview Version 2 - a multiple sequence alignment editor and analysis workbench Bioinformatics 2009, 25, 1189-1191
    • (2009) Bioinformatics , vol.25 , pp. 1189-1191
    • Waterhouse, A.M.1    Procter, J.B.2    Martin, D.M.A.3    Clamp, M.4    Barton, G.J.5
  • 32
    • 20444466524 scopus 로고    scopus 로고
    • Fifteen Years of Raman Spectroscopy of Engineered Heme Containing Peroxidases: What Have We Learned?
    • Smulevich, G.; Feis, A.; Howes, B. D. Fifteen Years of Raman Spectroscopy of Engineered Heme Containing Peroxidases: What Have We Learned? Acc. Chem. Res. 2005, 38, 433-440
    • (2005) Acc. Chem. Res. , vol.38 , pp. 433-440
    • Smulevich, G.1    Feis, A.2    Howes, B.D.3
  • 35
    • 0033521007 scopus 로고    scopus 로고
    • The structures of the horseradish peroxidase c-ferulic acid complex and the ternary complex with cyanide suggest how peroxidases oxidize small phenolic substrates
    • Henriksen, A.; Smith, A. T.; Gajhede, M. The structures of the horseradish peroxidase c-ferulic acid complex and the ternary complex with cyanide suggest how peroxidases oxidize small phenolic substrates J. Biol. Chem. 1999, 274, 35005-35011
    • (1999) J. Biol. Chem. , vol.274 , pp. 35005-35011
    • Henriksen, A.1    Smith, A.T.2    Gajhede, M.3
  • 36
    • 0030068091 scopus 로고    scopus 로고
    • Role of arginine 38 in horseradish peroxidase: A critical residue for substrate binding and catalysis
    • Rodriguez-Lopez, J. N.; Smith, A. T.; Thorneley, R. N. F. Role of arginine 38 in horseradish peroxidase: A critical residue for substrate binding and catalysis J. Biol. Chem. 1996, 271, 4023-4030
    • (1996) J. Biol. Chem. , vol.271 , pp. 4023-4030
    • Rodriguez-Lopez, J.N.1    Smith, A.T.2    Thorneley, R.N.F.3
  • 37
    • 0035909072 scopus 로고    scopus 로고
    • Differential activity and structure of highly similar peroxidases. Spectroscopic, crystallographic, and enzymatic analyses of lignifying Arabidopsis thaliana peroxidase A2 and horseradish peroxidase A2
    • Nielsen, K. L.; Indiani, C.; Henriksen, A.; Feis, A.; Becucci, M.; Gajhede, M.; Smulevich, G.; Welinder, K. G. Differential activity and structure of highly similar peroxidases. Spectroscopic, crystallographic, and enzymatic analyses of lignifying Arabidopsis thaliana peroxidase A2 and horseradish peroxidase A2 Biochemistry 2001, 40, 11013-11021
    • (2001) Biochemistry , vol.40 , pp. 11013-11021
    • Nielsen, K.L.1    Indiani, C.2    Henriksen, A.3    Feis, A.4    Becucci, M.5    Gajhede, M.6    Smulevich, G.7    Welinder, K.G.8
  • 38
    • 0029017982 scopus 로고
    • Aromatic donor molecule binding sites of haem peroxidases
    • Veitch, N. C. Aromatic donor molecule binding sites of haem peroxidases Biochem. Soc. Trans. 1995, 23, 232-240
    • (1995) Biochem. Soc. Trans. , vol.23 , pp. 232-240
    • Veitch, N.C.1
  • 39
    • 0035100890 scopus 로고    scopus 로고
    • Structure of soybean seed coat peroxidase: A plant peroxidase with unusual stability and haem-apoprotein interactions
    • Henriksen, A.; Mirza, O.; Indiani, C.; Teilum, K.; Smulevich, G.; Welinder, K. G.; Gajhede, M. Structure of soybean seed coat peroxidase: A plant peroxidase with unusual stability and haem-apoprotein interactions Protein Sci. 2001, 10, 108-115
    • (2001) Protein Sci. , vol.10 , pp. 108-115
    • Henriksen, A.1    Mirza, O.2    Indiani, C.3    Teilum, K.4    Smulevich, G.5    Welinder, K.G.6    Gajhede, M.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.