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Volumn 6, Issue , 2015, Pages

Structure and boosting activity of a starch-degrading lytic polysaccharide monooxygenase

Author keywords

[No Author keywords available]

Indexed keywords

BETA AMYLASE; CARBOHYDRATE BINDING PROTEIN; LYTIC POLYSACCHARIDE MONOOXYGENASE; MALTOSE; OLIGOSACCHARIDE; STARCH; UNCLASSIFIED DRUG; UNSPECIFIC MONOOXYGENASE; ACID; CELLULOSE; COPPER; HISTIDINE; MIXED FUNCTION OXIDASE; OXYGEN; POLYSACCHARIDE;

EID: 84955324784     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms6961     Document Type: Article
Times cited : (259)

References (52)
  • 1
    • 33846951759 scopus 로고    scopus 로고
    • Biomass recalcitrance: Engineering plants and enzymes for biofuels production
    • Himmel, M. E. et al. Biomass recalcitrance: engineering plants and enzymes for biofuels production. Science 315, 804-807 (2007).
    • (2007) Science , vol.315 , pp. 804-807
    • Himmel, M.E.1
  • 3
    • 80053088478 scopus 로고    scopus 로고
    • Insights into the oxidative degradation of cellulose by a copper metalloenzyme that exploits biomass components
    • Quinlan, R. J. et al. Insights into the oxidative degradation of cellulose by a copper metalloenzyme that exploits biomass components. Proc. Natl Acad. Sci. USA 108, 15079-15084 (2011).
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 15079-15084
    • Quinlan, R.J.1
  • 4
    • 77957727454 scopus 로고    scopus 로고
    • An oxidative enzyme boosting the enzymatic conversion of recalcitrant polysaccharides
    • Vaaje-Kolstad, G. et al. An oxidative enzyme boosting the enzymatic conversion of recalcitrant polysaccharides. Science 330, 219-222 (2010).
    • (2010) Science , vol.330 , pp. 219-222
    • Vaaje-Kolstad, G.1
  • 6
    • 84897113991 scopus 로고    scopus 로고
    • Discovery of a new family of lytic polysaccharide mono-oxygenases
    • Hemsworth, G. R., Henrissat, B., Davies, G. J. & Walton, P. H. Discovery of a new family of lytic polysaccharide mono-oxygenases. Nat. Chem. Biol. 10, 122-126 (2014).
    • (2014) Nat. Chem. Biol. , vol.10 , pp. 122-126
    • Hemsworth, G.R.1    Henrissat, B.2    Davies, G.J.3    Walton, P.H.4
  • 7
    • 84875193804 scopus 로고    scopus 로고
    • Expansion of the enzymatic repertoire of the CAZy database to integrate auxiliary redox enzymes
    • Levasseur, A., Drula, E., Lombard, V., Coutinho, P. M. & Henrissat, B. Expansion of the enzymatic repertoire of the CAZy database to integrate auxiliary redox enzymes. Biotechnol. Biofuels 6, 41 (2013).
    • (2013) Biotechnol. Biofuels , vol.6 , pp. 41
    • Levasseur, A.1    Drula, E.2    Lombard, V.3    Coutinho, P.M.4    Henrissat, B.5
  • 8
    • 84855912007 scopus 로고    scopus 로고
    • Oxidative cleavage of cellulose by fungal copper-dependent polysaccharide monooxygenases
    • Beeson, W. T., Phillips, C. M., Cate, J. H. & Marletta, M. A. Oxidative cleavage of cellulose by fungal copper-dependent polysaccharide monooxygenases. J. Am. Chem. Soc. 134, 890-892 (2012).
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 890-892
    • Beeson, W.T.1    Phillips, C.M.2    Cate, J.H.3    Marletta, M.A.4
  • 9
    • 77950948151 scopus 로고    scopus 로고
    • Stimulation of lignocellulosic biomass hydrolysis by proteins of glycoside hydrolase family 61: Structure and function of a large, enigmatic family
    • Harris, P. V. et al. Stimulation of lignocellulosic biomass hydrolysis by proteins of glycoside hydrolase family 61: structure and function of a large, enigmatic family. Biochemistry 49, 3305-3316 (2010).
    • (2010) Biochemistry , vol.49 , pp. 3305-3316
    • Harris, P.V.1
  • 10
    • 84885472701 scopus 로고    scopus 로고
    • Recent insights into coppercontaining lytic polysaccharide mono-oxygenases
    • Hemsworth, G. R., Davies, G. J. & Walton, P. H. Recent insights into coppercontaining lytic polysaccharide mono-oxygenases. Curr. Opin. Struct. Biol. 23, 660-668 (2013).
    • (2013) Curr. Opin. Struct. Biol. , vol.23 , pp. 660-668
    • Hemsworth, G.R.1    Davies, G.J.2    Walton, P.H.3
  • 11
    • 84902578753 scopus 로고    scopus 로고
    • Spectroscopic and computational insight into the activation of O2 by the mononuclear Cu center in polysaccharide monooxygenases
    • Kjaergaard, C. H. et al. Spectroscopic and computational insight into the activation of O2 by the mononuclear Cu center in polysaccharide monooxygenases. Proc. Natl Acad. Sci. USA 111, 8797-8802 (2014).
    • (2014) Proc. Natl Acad. Sci. USA , vol.111 , pp. 8797-8802
    • Kjaergaard, C.H.1
  • 12
    • 84897970495 scopus 로고    scopus 로고
    • Copper active sites in biology
    • Solomon, E. I. et al. Copper active sites in biology. Chem. Rev. 114, 3659-3853 (2014).
    • (2014) Chem. Rev. , vol.114 , pp. 3659-3853
    • Solomon, E.I.1
  • 13
    • 84892745213 scopus 로고    scopus 로고
    • Determinants of regioselective hydroxylation in the fungal polysaccharide monooxygenases
    • Vu, V. V., Beeson, W. T., Phillips, C. M., Cate, J. H. D. & Marletta, M. A. Determinants of regioselective hydroxylation in the fungal polysaccharide monooxygenases. J. Am. Chem. Soc. 136, 562-565 (2013).
    • (2013) J. Am. Chem. Soc. , vol.136 , pp. 562-565
    • Vu, V.V.1    Beeson, W.T.2    Phillips, C.M.3    Cate, J.H.D.4    Marletta, M.A.5
  • 14
    • 84893460463 scopus 로고    scopus 로고
    • A C4-oxidizing lytic polysaccharide monooxygenase cleaving both cellulose and cello-oligosaccharides
    • Isaksen, T. et al. A C4-oxidizing lytic polysaccharide monooxygenase cleaving both cellulose and cello-oligosaccharides. J. Biol. Chem. 289, 2632-2642 (2014).
    • (2014) J. Biol. Chem. , vol.289 , pp. 2632-2642
    • Isaksen, T.1
  • 15
    • 84876724822 scopus 로고    scopus 로고
    • The copper active site of CBM33 polysaccharide oxygenases
    • Hemsworth, G. R. et al. The copper active site of CBM33 polysaccharide oxygenases. J. Am. Chem. Soc. 135, 6069-6077 (2013).
    • (2013) J. Am. Chem. Soc. , vol.135 , pp. 6069-6077
    • Hemsworth, G.R.1
  • 16
    • 84891926133 scopus 로고    scopus 로고
    • Quantum mechanical calculations suggest that lytic polysaccharide monooxygenases use a copper-oxyl, oxygen-rebound mechanism
    • Kim, S., Ståhlberg, J., Sandgren, M., Paton, R. S. & Beckham, G. T. Quantum mechanical calculations suggest that lytic polysaccharide monooxygenases use a copper-oxyl, oxygen-rebound mechanism. Proc. Natl Acad. Sci. USA 111, 149-154 (2014).
    • (2014) Proc. Natl Acad. Sci. USA , vol.111 , pp. 149-154
    • Kim, S.1    Ståhlberg, J.2    Sandgren, M.3    Paton, R.S.4    Beckham, G.T.5
  • 17
    • 77952093872 scopus 로고    scopus 로고
    • Oxidation of methane by a biological dicopper centre
    • Balasubramanian, R. et al. Oxidation of methane by a biological dicopper centre. Nature 465, 115-119 (2010).
    • (2010) Nature , vol.465 , pp. 115-119
    • Balasubramanian, R.1
  • 18
    • 84976228345 scopus 로고    scopus 로고
    • 1H, 13C, 15N resonance assignment of the chitin-active lytic polysaccharide monooxygenase BlLPMO10A from Bacillus licheniformis
    • Courtade, G. et al. 1H, 13C, 15N resonance assignment of the chitin-active lytic polysaccharide monooxygenase BlLPMO10A from Bacillus licheniformis. Biomol. NMR Assign. 1-4 (2014).
    • (2014) Biomol. NMR Assign , pp. 1-4
    • Courtade, G.1
  • 19
    • 84869205445 scopus 로고    scopus 로고
    • NMR structure of a lytic polysaccharide monooxygenase provides insight into copper binding, protein dynamics, and substrate interactions
    • Aachmann, F. L., Sørlie, M., Skjåk-Bræk, G., Eijsink, V. G. H. & Vaaje-Kolstad, G. NMR structure of a lytic polysaccharide monooxygenase provides insight into copper binding, protein dynamics, and substrate interactions. Proc. Natl Acad. Sci. USA 109, 18779-18784 (2012).
    • (2012) Proc. Natl Acad. Sci. USA , vol.109 , pp. 18779-18784
    • Aachmann, F.L.1    Sørlie, M.2    Skjåk-Bræk, G.3    Eijsink, V.G.H.4    Vaaje-Kolstad, G.5
  • 21
    • 84918563784 scopus 로고    scopus 로고
    • Fungal cellulose degradation by oxidative enzymes: From dysfunctional GH61 family to powerful lytic polysaccharide monooxygenase family
    • Morgenstern, I., Powlowski, J. & Tsang, A. Fungal cellulose degradation by oxidative enzymes: from dysfunctional GH61 family to powerful lytic polysaccharide monooxygenase family. Brief. Funct. Genomics 13, 471-481 (2014).
    • (2014) Brief. Funct. Genomics , vol.13 , pp. 471-481
    • Morgenstern, I.1    Powlowski, J.2    Tsang, A.3
  • 22
    • 84902205104 scopus 로고    scopus 로고
    • Structural and functional characterization of a conserved pair of bacterial cellulose-oxidizing lytic polysaccharide monooxygenases
    • Forsberg, Z. et al. Structural and functional characterization of a conserved pair of bacterial cellulose-oxidizing lytic polysaccharide monooxygenases. Proc. Natl Acad. Sci. USA 111, 8446-8451 (2014).
    • (2014) Proc. Natl Acad. Sci. USA , vol.111 , pp. 8446-8451
    • Forsberg, Z.1
  • 23
    • 84899647519 scopus 로고    scopus 로고
    • Discovery of LPMO activity on hemicelluloses shows the importance of oxidative processes in plant cell wall degradation
    • Agger, J. W. et al. Discovery of LPMO activity on hemicelluloses shows the importance of oxidative processes in plant cell wall degradation. Proc. Natl Acad. Sci. USA 111, 6287-6292 (2014).
    • (2014) Proc. Natl Acad. Sci. USA , vol.111 , pp. 6287-6292
    • Agger, J.W.1
  • 24
  • 25
    • 84902738221 scopus 로고    scopus 로고
    • Ensiling and hydrothermal pretreatment of grass: Consequences for enzymatic biomass conversion and total monosaccharide yields
    • Ambye-Jensen, M., Johansen, K., Didion, T., Kadar, Z. & Meyer, A. Ensiling and hydrothermal pretreatment of grass: consequences for enzymatic biomass conversion and total monosaccharide yields. Biotechnol. Biofuels 7, 95 (2014).
    • (2014) Biotechnol. Biofuels , vol.7 , pp. 95
    • Ambye-Jensen, M.1    Johansen, K.2    Didion, T.3    Kadar, Z.4    Meyer, A.5
  • 27
    • 77956806266 scopus 로고    scopus 로고
    • Application of microbial a-amylase in industry-a review
    • de Souza, P. M. & de Oliveira e Magalhaes, P. Application of microbial a-amylase in industry-a review. Braz. J. Microbiol. 41, 850-861 (2010).
    • (2010) Braz. J. Microbiol. , vol.41 , pp. 850-861
    • De Souza, P.M.1    De Oliveirae Magalhaes, P.2
  • 31
    • 84885472019 scopus 로고    scopus 로고
    • Advances in understanding the molecular basis of plant cell wall polysaccharide recognition by carbohydratebinding modules
    • Gilbert, H. J., Knox, J. P. & Boraston, A. B. Advances in understanding the molecular basis of plant cell wall polysaccharide recognition by carbohydratebinding modules. Curr. Opin. Struct. Biol. 23, 669-677 (2013).
    • (2013) Curr. Opin. Struct. Biol. , vol.23 , pp. 669-677
    • Gilbert, H.J.1    Knox, J.P.2    Boraston, A.B.3
  • 32
    • 84905994561 scopus 로고    scopus 로고
    • Discovery of a eukaryotic pyrroloquinoline quinonedependent oxidoreductase belonging to a new auxiliary activity family in the database of carbohydrate-active enzymes
    • Matsumura, H. et al. Discovery of a eukaryotic pyrroloquinoline quinonedependent oxidoreductase belonging to a new auxiliary activity family in the database of carbohydrate-active enzymes. PLoS ONE 9, e104851 (2014).
    • (2014) PLoS ONE , vol.9 , pp. e104851
    • Matsumura, H.1
  • 33
    • 69449083006 scopus 로고    scopus 로고
    • The carbohydrate-binding module family 20-diversity, structure, and function
    • Christiansen, C. et al. The carbohydrate-binding module family 20-diversity, structure, and function. FEBS J. 276, 5006-5029 (2009).
    • (2009) FEBS J. , vol.276 , pp. 5006-5029
    • Christiansen, C.1
  • 34
    • 84861987031 scopus 로고    scopus 로고
    • Structural basis for substrate targeting and catalysis by fungal polysaccharide monooxygenases
    • Li, X., Beeson, 4th W. T., Phillips, C. M., Marletta, M. A. & Cate, J. H. Structural basis for substrate targeting and catalysis by fungal polysaccharide monooxygenases. Structure 20, 1051-1061 (2012).
    • (2012) Structure , vol.20 , pp. 1051-1061
    • Li, X.1    Beeson, W.T.2    Phillips, C.M.3    Marletta, M.A.4    Cate, J.H.5
  • 35
    • 84903852138 scopus 로고    scopus 로고
    • Structural and electronic snapshots during the transition from a Cu (II) to Cu (I) metal center of a lytic polysaccharide monooxygenase by X-ray photo-reduction
    • Gudmundsson, M. et al. Structural and electronic snapshots during the transition from a Cu (II) to Cu (I) metal center of a lytic polysaccharide monooxygenase by X-ray photo-reduction. J. Biol. Chem. 289, 18782-18792 (2014).
    • (2014) J. Biol. Chem. , vol.289 , pp. 18782-18792
    • Gudmundsson, M.1
  • 36
    • 77956377452 scopus 로고    scopus 로고
    • The molecular structures of starch components and their contribution to the architecture of starch granules: A comprehensive review
    • Pérez, S. & Bertoft, E. The molecular structures of starch components and their contribution to the architecture of starch granules: A comprehensive review. Starch Stärke 62, 389-420 (2010).
    • (2010) Starch Stärke , vol.62 , pp. 389-420
    • Pérez, S.1    Bertoft, E.2
  • 37
    • 0016369980 scopus 로고
    • Structural implications derived from the analysis of electron paramagnetic resonance spectra of natural and artificial copper proteins
    • Peisach, J. & Blumberg, W. E. Structural implications derived from the analysis of electron paramagnetic resonance spectra of natural and artificial copper proteins. Arch. Biochem. Biophys. 165, 691-708 (1974).
    • (1974) Arch. Biochem. Biophys. , vol.165 , pp. 691-708
    • Peisach, J.1    Blumberg, W.E.2
  • 38
    • 84898944979 scopus 로고    scopus 로고
    • Comparative study of two chitin-active and two celluloseactive AA10-type lytic polysaccharide monooxygenases
    • Forsberg, Z. et al. Comparative study of two chitin-active and two celluloseactive AA10-type lytic polysaccharide monooxygenases. Biochemistry 53, 1647-1656 (2014).
    • (2014) Biochemistry , vol.53 , pp. 1647-1656
    • Forsberg, Z.1
  • 39
    • 7444225775 scopus 로고    scopus 로고
    • Novel buffer systems for macromolecular crystallization
    • Newman, J. Novel buffer systems for macromolecular crystallization. Acta Crystallogr. D Biol. Crystallogr. 60, 610-612 (2004).
    • (2004) Acta Crystallogr. D Biol. Crystallogr. , vol.60 , pp. 610-612
    • Newman, J.1
  • 40
    • 33947537616 scopus 로고    scopus 로고
    • An automated microseed matrixscreening method for protein crystallization
    • D'Arcy, A., Frederic, V. A. & Marsh, M. An automated microseed matrixscreening method for protein crystallization. Acta Crystallogr. D Biol. Crystallogr. 63, 550-554 (2007).
    • (2007) Acta Crystallogr. D Biol. Crystallogr. , vol.63 , pp. 550-554
    • D'Arcy, A.1    Frederic, V.A.2    Marsh, M.3
  • 42
    • 76449098262 scopus 로고    scopus 로고
    • PHENIX: A comprehensive Python-based system for macromolecular structure solution
    • Adams, P. D. et al. PHENIX: A comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr. D Biol. Crystallogr. 66, 213-221 (2010).
    • (2010) Acta Crystallogr. D Biol. Crystallogr. , vol.66 , pp. 213-221
    • Adams, P.D.1
  • 44
    • 79953737180 scopus 로고    scopus 로고
    • Overview of the CCP4 suite and current developments
    • Winn, M. D. et al. Overview of the CCP4 suite and current developments. Acta Crystallogr. D Biol. Crystallogr. 67, 235-242 (2011).
    • (2011) Acta Crystallogr. D Biol. Crystallogr. , vol.67 , pp. 235-242
    • Winn, M.D.1
  • 46
    • 0042121237 scopus 로고    scopus 로고
    • Multiple sequence alignment with the Clustal series of programs
    • Chenna, R. et al. Multiple sequence alignment with the Clustal series of programs. Nucleic Acids Res. 31, 3497-3500 (2003).
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3497-3500
    • Chenna, R.1
  • 47
    • 0035012982 scopus 로고    scopus 로고
    • STRAP: Editor for structural alignments of proteins
    • Gille, C. & Frommel, C. STRAP: editor for STRuctural Alignments of Proteins. Bioinformatics 17, 377-378 (2001).
    • (2001) Bioinformatics , vol.17 , pp. 377-378
    • Gille, C.1    Frommel, C.2
  • 48
    • 34447326804 scopus 로고
    • A simple and rapid method for the permethylation of carbohydrates
    • Ciucanu, I. & Kerek, F. A simple and rapid method for the permethylation of carbohydrates. Carbohydr. Res. 131, 209-217 (1984).
    • (1984) Carbohydr. Res. , vol.131 , pp. 209-217
    • Ciucanu, I.1    Kerek, F.2
  • 49
    • 78649329362 scopus 로고    scopus 로고
    • Carbohydrate structural analysis of wheat flour arabinogalactan protein
    • Tryfona, T. et al. Carbohydrate structural analysis of wheat flour arabinogalactan protein. Carbohydr. Res. 345, 2648-2656 (2010).
    • (2010) Carbohydr. Res. , vol.345 , pp. 2648-2656
    • Tryfona, T.1
  • 50
    • 84867129575 scopus 로고    scopus 로고
    • Structural characterization of Arabidopsis leaf arabinogalactan polysaccharides
    • Tryfona, T. et al. Structural characterization of Arabidopsis leaf arabinogalactan polysaccharides. Plant Physiol. 160, 653-666 (2012).
    • (2012) Plant Physiol. , vol.160 , pp. 653-666
    • Tryfona, T.1
  • 51
    • 79957736765 scopus 로고    scopus 로고
    • The plant cell wall
    • ed Popper, Z. A Ch. Humana Press 5
    • Goubet, F., Dupree, P. & Johansen, K. in The Plant Cell Wall. Methods in Molecular Biology, Vol. 715 (ed Popper, Z. A.) Ch. 5, 81-92 (Humana Press, 2011).
    • (2011) Methods in Molecular Biology , vol.715 , pp. 81-92
    • Goubet, F.1    Dupree, P.2    Johansen, K.3
  • 52
    • 0036145787 scopus 로고    scopus 로고
    • Polysaccharide analysis using carbohydrate gel electrophoresis: A method to study plant cell wall polysaccharides and polysaccharide hydrolases
    • Goubet, F., Jackson, P., Deery, M. J. & Dupree, P. Polysaccharide analysis using carbohydrate gel electrophoresis: A method to study plant cell wall polysaccharides and polysaccharide hydrolases. Anal. Biochem. 300, 53-68 (2002).
    • (2002) Anal. Biochem. , vol.300 , pp. 53-68
    • Goubet, F.1    Jackson, P.2    Deery, M.J.3    Dupree, P.4


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