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Volumn 71, Issue 12, 2005, Pages 8881-8887

Structural characterization of glucooligosaccharide oxidase from Acremonium strictum

Author keywords

[No Author keywords available]

Indexed keywords

CARBOHYDRATES; CATALYSIS; CLONING; DNA; OLIGOMERS; OXIDATION;

EID: 29144478790     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/AEM.71.12.8881-8887.2005     Document Type: Article
Times cited : (41)

References (25)
  • 1
    • 4644335054 scopus 로고    scopus 로고
    • A novel family of P-loop NTPases with an unusual phyletic distribution and transmembrane segments inserted within the NTPase domain
    • Aravind, L., L. M. Iyer, D. D. Leipe, and E. V. Koonin. 2004. A novel family of P-loop NTPases with an unusual phyletic distribution and transmembrane segments inserted within the NTPase domain. Genome Biol. 5:R30.
    • (2004) Genome Biol , vol.5
    • Aravind, L.1    Iyer, L.M.2    Leipe, D.D.3    Koonin, E.V.4
  • 2
    • 0842264011 scopus 로고    scopus 로고
    • Tobacco nectarin V is a flavin-containing berberine bridge enzyme-like protein with glucose oxidase activity
    • Carter, C. J., and R. W. Thornburg. 2004. Tobacco nectarin V is a flavin-containing berberine bridge enzyme-like protein with glucose oxidase activity. Plant Physiol. 134:460-469.
    • (2004) Plant Physiol , vol.134 , pp. 460-469
    • Carter, C.J.1    Thornburg, R.W.2
  • 3
    • 14344256284 scopus 로고    scopus 로고
    • Cresol methylhydroxylase: Alteration of the structure of the flavoprotein subunit upon its binding to the cytochrome subunit
    • Cunane, L. M., Z. W. Chen, W. S. McIntire, and F. S. Mathews. 2005. p-Cresol methylhydroxylase: alteration of the structure of the flavoprotein subunit upon its binding to the cytochrome subunit. Biochemistry 44:2963-2973.
    • (2005) Biochemistry , vol.44 , pp. 2963-2973
    • Cunane, L.M.1    Chen, Z.W.2    McIntire, W.S.3    Mathews, F.S.4
  • 5
    • 0034854206 scopus 로고    scopus 로고
    • Sequence-structure analysis of FAD-containing proteins
    • Dym, O., and D. Eisenberg. 2001. Sequence-structure analysis of FAD-containing proteins. Protein Sci. 10:1712-1728.
    • (2001) Protein Sci , vol.10 , pp. 1712-1728
    • Dym, O.1    Eisenberg, D.2
  • 6
    • 1942485882 scopus 로고    scopus 로고
    • Carbanion versus hydride transfer mechanisms in flavoprotein-catalyzed dehydrogenations
    • Fitzpatrick, P. F. 2004. Carbanion versus hydride transfer mechanisms in flavoprotein-catalyzed dehydrogenations. Bioorg. Chem. 32:125-139.
    • (2004) Bioorg. Chem. , vol.32 , pp. 125-139
    • Fitzpatrick, P.F.1
  • 7
    • 0033544926 scopus 로고    scopus 로고
    • Covalent flavinylation is essential for efficient redox catalysis in vanillyl-alcohol oxidase
    • Fraaije, M. W., R. H. H. van den Heuvel, W. J. H. van Berkel, and A. Mattevi. 1999. Covalent flavinylation is essential for efficient redox catalysis in vanillyl-alcohol oxidase. J. Biol. Chem. 274:35514-35520.
    • (1999) J. Biol. Chem. , vol.274 , pp. 35514-35520
    • Fraaije, M.W.1    Van Den Heuvel, R.H.H.2    Van Berkel, W.J.H.3    Mattevi, A.4
  • 8
    • 0034161331 scopus 로고    scopus 로고
    • Flavoenzymes: Diverse catalysts with recurrent features
    • Fraaije, M. W., and A. Mattevi. 2000. Flavoenzymes: diverse catalysts with recurrent features. Trends Biochem. Sci. 25:126-132.
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 126-132
    • Fraaije, M.W.1    Mattevi, A.2
  • 9
    • 0030937674 scopus 로고    scopus 로고
    • Characterization of hexose oxidase from the red seaweed Chondrus crispus
    • Groen, B. W., S. De Vries, and J. A. Duine. 1997. Characterization of hexose oxidase from the red seaweed Chondrus crispus. Eur. J. Biochem. 244:858-861.
    • (1997) Eur. J. Biochem. , vol.244 , pp. 858-861
    • Groen, B.W.1    De Vries, S.2    Duine, J.A.3
  • 11
    • 4344582358 scopus 로고    scopus 로고
    • Crystal structure of the 270 kDa homotetrameric lignin-degrading enzyme pyranose 2-oxidase
    • Hallberg, B. M., C. Leitner, D. Haltrich, and C. Divne. 2004. Crystal structure of the 270 kDa homotetrameric lignin-degrading enzyme pyranose 2-oxidase. J. Mol. Biol. 341:781-796.
    • (2004) J. Mol. Biol. , vol.341 , pp. 781-796
    • Hallberg, B.M.1    Leitner, C.2    Haltrich, D.3    Divne, C.4
  • 12
    • 0029878517 scopus 로고    scopus 로고
    • A cluster of genes encoding major isozymes of lignin peroxidase and manganese peroxidase from the white-rot fungus Trametes versicolor
    • Johansson, T., and P. O. Nyman. 1996. A cluster of genes encoding major isozymes of lignin peroxidase and manganese peroxidase from the white-rot fungus Trametes versicolor. Gene 170:31-38.
    • (1996) Gene , vol.170 , pp. 31-38
    • Johansson, T.1    Nyman, P.O.2
  • 13
    • 0028785275 scopus 로고
    • Characterization and mechanism of the berberine bridge enzyme, a covalently flavinylated oxidase of benzophenanthridine alkaloid biosynthesis in plants
    • Kutchan, T. M., and H. Dittrich. 1995. Characterization and mechanism of the berberine bridge enzyme, a covalently flavinylated oxidase of benzophenanthridine alkaloid biosynthesis in plants. J. Biol. Chem. 270:24475-24481.
    • (1995) J. Biol. Chem. , vol.270 , pp. 24475-24481
    • Kutchan, T.M.1    Dittrich, H.2
  • 14
    • 0037424631 scopus 로고    scopus 로고
    • Sub-atomic resolution crystal structure of cholesterol oxidase: What atomic resolution crystallography reveals about enzyme mechanism and the role of the FAD cofactor in redox activity
    • Lario, P. I., N. Sampson, and A. Vrielink. 2003. Sub-atomic resolution crystal structure of cholesterol oxidase: what atomic resolution crystallography reveals about enzyme mechanism and the role of the FAD cofactor in redox activity. J. Mol. Biol. 326:1635-1650.
    • (2003) J. Mol. Biol. , vol.326 , pp. 1635-1650
    • Lario, P.I.1    Sampson, N.2    Vrielink, A.3
  • 15
    • 0034809461 scopus 로고    scopus 로고
    • Structural characterization of the 60-kDa bermuda grass pollen isoallergens, a covalent flavoprotein
    • Liaw, S., D. Y. Lee, L. P. Chow, G. X. Lau, and S. N. Su. 2001. Structural characterization of the 60-kDa bermuda grass pollen isoallergens, a covalent flavoprotein. Biochem. Biophys. Res. Commun. 280:738-743.
    • (2001) Biochem. Biophys. Res. Commun. , vol.280 , pp. 738-743
    • Liaw, S.1    Lee, D.Y.2    Chow, L.P.3    Lau, G.X.4    Su, S.N.5
  • 16
    • 0026068184 scopus 로고
    • Purification and characterization of a novel glucooligosaccharide oxidase from Acremonium strictum T1
    • Lin, S. F., T. Y. Yang, T. Inukai, M. Yamasaki, and Y. C. Tsai. 1991. Purification and characterization of a novel glucooligosaccharide oxidase from Acremonium strictum T1. Biochim. Biophys. Acta 1118:41-47.
    • (1991) Biochim. Biophys. Acta , vol.1118 , pp. 41-47
    • Lin, S.F.1    Yang, T.Y.2    Inukai, T.3    Yamasaki, M.4    Tsai, Y.C.5
  • 17
    • 4143057296 scopus 로고    scopus 로고
    • Structures of Michaelis and product complexes of plant cytokinin dehydrogenase: Implications for flavoenzyme catalysis
    • Malito, E., A. Coda, K. D. Bilyeu, M. W. Fraaíje, and A. Mattevi. 2004. Structures of Michaelis and product complexes of plant cytokinin dehydrogenase: implications for flavoenzyme catalysis. J. Mol. Biol. 341:1237-1249.
    • (2004) J. Mol. Biol. , vol.341 , pp. 1237-1249
    • Malito, E.1    Coda, A.2    Bilyeu, K.D.3    Fraaíje, M.W.4    Mattevi, A.5
  • 18
    • 0026071385 scopus 로고
    • Three-dimensional structure of p-cresol methylhydroxylase (flavocytochrome c) from Pseudomonas putida at 3.0-A resolution
    • Mathews, F. S., Z. W. Chen, H. D. Bellamy, and W. S. McIntire. 1991. Three-dimensional structure of p-cresol methylhydroxylase (flavocytochrome c) from Pseudomonas putida at 3.0-A resolution. Biochemistry 30:238-247.
    • (1991) Biochemistry , vol.30 , pp. 238-247
    • Mathews, F.S.1    Chen, Z.W.2    Bellamy, H.D.3    McIntire, W.S.4
  • 19
    • 0024448994 scopus 로고
    • Site-directed mutagenesis of the FAD-hinding histidine of 6-hydroxy-D-nicotine oxidase. Consequences on flavinylation and enzyme activity
    • Mauch, L., V. Bichler, and R. Brandsch. 1989. Site-directed mutagenesis of the FAD-hinding histidine of 6-hydroxy-D-nicotine oxidase. Consequences on flavinylation and enzyme activity. FEBS Lett. 257:86-88.
    • (1989) FEBS Lett , vol.257 , pp. 86-88
    • Mauch, L.1    Bichler, V.2    Brandsch, R.3
  • 20
    • 0031941120 scopus 로고    scopus 로고
    • Covalent attachment of flavin adenine dinucleotide (FAD) and flavin mononucleotide (FMN) to enzymes: The current state of affairs
    • Mewies, M., W. S. McIntire, and N. S. Scrutton. 1998. Covalent attachment of flavin adenine dinucleotide (FAD) and flavin mononucleotide (FMN) to enzymes: the current state of affairs. Protein Sci. 7:7-20.
    • (1998) Protein Sci , vol.7 , pp. 7-20
    • Mewies, M.1    McIntire, W.S.2    Scrutton, N.S.3
  • 21
    • 0001679398 scopus 로고
    • Application of enzymes as food antioxidants
    • Meyer, A. S., and A. Isaksen. 1995. Application of enzymes as food antioxidants. Trends Food Sci. Technol. 6:300-304.
    • (1995) Trends Food Sci. Technol. , vol.6 , pp. 300-304
    • Meyer, A.S.1    Isaksen, A.2
  • 22
    • 4344679385 scopus 로고    scopus 로고
    • Fluorescence glucose detection: Advances toward the ideal in vivo biosensor
    • Moschou, E. A., B. V. Sharma, S. K. Deo, and S. Daunert. 2004. Fluorescence glucose detection: advances toward the ideal in vivo biosensor. J. Fluoresc. 14:535-547.
    • (2004) J. Fluoresc. , vol.14 , pp. 535-547
    • Moschou, E.A.1    Sharma, B.V.2    Deo, S.K.3    Daunert, S.4
  • 24
    • 4544339836 scopus 로고    scopus 로고
    • The gene controlling marijuana psychoactivity: Molecular cloning and heterologous expression of Δ1-tetrahydrocannabinolic acid synthase from Cannabis saliva L
    • Sirikantaramas, S., S. Morimoto, Y. Shoyama, Y. Ishikawa, Y. Wada, and F. Taura. 2004. The gene controlling marijuana psychoactivity: molecular cloning and heterologous expression of Δ1-tetrahydrocannabinolic acid synthase from Cannabis saliva L. J. Biol. Chem. 279:39767-39774.
    • (2004) J. Biol. Chem. , vol.279 , pp. 39767-39774
    • Sirikantaramas, S.1    Morimoto, S.2    Shoyama, Y.3    Ishikawa, Y.4    Wada, Y.5    Taura, F.6
  • 25
    • 0033135955 scopus 로고    scopus 로고
    • 1.8 and 1.9 a resolution structures of the Penicillium amagasukiense and Aspergillus niger glucose oxidases as a basis for modelling substrate complexes
    • Wohlfahrt, G., S. Witt, J. Hendle, D. Schomburg, H. M. Kalisz, and H. J. Hecht, 1999. 1.8 and 1.9 A resolution structures of the Penicillium amagasukiense and Aspergillus niger glucose oxidases as a basis for modelling substrate complexes. Acta Crystallogr. D Biol. Crystallogr. 55:969-977.
    • (1999) Acta Crystallogr. D Biol. Crystallogr. , vol.55 , pp. 969-977
    • Wohlfahrt, G.1    Witt, S.2    Hendle, J.3    Schomburg, D.4    Kalisz, H.M.5    Hecht, H.J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.