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Volumn 289, Issue 9, 2014, Pages 6006-6019

Catalytic mechanism and mode of action of the periplasmic alginate epimerase AlgG

Author keywords

[No Author keywords available]

Indexed keywords

BIOFILM INFECTIONS; CATALYTIC MECHANISMS; ELECTROSTATIC SURFACES; EXOPOLYSACCHARIDES; PSEUDOMONAS AERUGINOSA; PSEUDOMONAS SYRINGAE; SUBSTRATE BINDING; SUBSTRATE DOCKING;

EID: 84896858114     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.533158     Document Type: Article
Times cited : (41)

References (84)
  • 1
    • 0001765872 scopus 로고
    • A polysaccharide resembling alginic acid from a Pseudomonas micro-organism
    • Linker, A., and Jones, R. S. (1964) A polysaccharide resembling alginic acid from a Pseudomonas micro-organism. Nature 204, 187-188
    • (1964) Nature , vol.204 , pp. 187-188
    • Linker, A.1    Jones, R.S.2
  • 2
    • 0000258671 scopus 로고
    • Exocellular alginic acid from Azotobacter vinelandii
    • Gorin, P. A., and Spencer, J. F. (1966) Exocellular alginic acid from Azotobacter vinelandii. Can. J. Chem. 44, 993-998
    • (1966) Can. J. Chem. , vol.44 , pp. 993-998
    • Gorin, P.A.1    Spencer, J.F.2
  • 3
    • 49549148780 scopus 로고
    • Uronic acid sequence in alginate from different sources
    • Haug, A., Larsen, B., and Smidsrod, O. (1974) Uronic acid sequence in alginate from different sources. Carbohydr. Res. 32, 217-225
    • (1974) Carbohydr. Res. , vol.32 , pp. 217-225
    • Haug, A.1    Larsen, B.2    Smidsrod, O.3
  • 4
    • 0023050603 scopus 로고
    • Monomer sequence and acetylation pattern in some bacterial alginates
    • Skjåk-Braek, G., Grasdalen, H., and Larsen, B. (1986) Monomer sequence and acetylation pattern in some bacterial alginates. Carbohydr. Res. 154, 239-250
    • (1986) Carbohydr. Res. , vol.154 , pp. 239-250
    • Skjåk-Braek, G.1    Grasdalen, H.2    Larsen, B.3
  • 5
    • 0035114574 scopus 로고    scopus 로고
    • Role of alginate O acetylation in resistance of mucoid Pseudomonas aeruginosa to opsonic phagocytosis
    • DOI 10.1128/IAI.69.3.1895-1901.2001
    • Pier, G. B., Coleman, F., Grout, M., Franklin, M., and Ohman, D. E. (2001) Role of alginate O acetylation in resistance of mucoid Pseudomonas aeruginosa to opsonic phagocytosis. Infect. Immun. 69, 1895-1901 (Pubitemid 32187652)
    • (2001) Infection and Immunity , vol.69 , Issue.3 , pp. 1895-1901
    • Pier, G.B.1    Coleman, F.2    Grout, M.3    Franklin, M.4    Ohman, D.E.5
  • 6
    • 0034838734 scopus 로고    scopus 로고
    • Hexuronyl C5-epimerases in alginate and glycosaminoglycan biosynthesis
    • DOI 10.1016/S0300-9084(01)01313-X
    • Valla, S., Li, J., Ertesvåg, H., Barbeyron, T., and Lindahl, U. (2001) Hexuronyl C5-epimerases in alginate and glycosaminoglycan biosynthesis. Biochimie 83, 819-830 (Pubitemid 32821248)
    • (2001) Biochimie , vol.83 , Issue.8 , pp. 819-830
    • Valla, S.1    Li, J.-P.2    Ertesvag, H.3    Barbeyron, T.4    Lindahl, U.5
  • 8
    • 0001637799 scopus 로고
    • Tailoring of alginates by enzymatic modification in vitro
    • Skjåk-Braek, G., Smidsrod, O., and Larsen, B. (1986) Tailoring of alginates by enzymatic modification in vitro. Int. J. Biol. Macromol. 8, 330-336
    • (1986) Int. J. Biol. Macromol. , vol.8 , pp. 330-336
    • Skjåk-Braek, G.1    Smidsrod, O.2    Larsen, B.3
  • 9
    • 0142214652 scopus 로고    scopus 로고
    • Characterization of Mannuronan C-5-Epimerase Genes from the Brown Alga Laminaria digitata
    • DOI 10.1104/pp.103.025981
    • Nyvall, P., Corre, E., Boisset, C., Barbeyron, T., Rousvoal, S., Scornet, D., Kloareg, B., and Boyen, C. (2003) Characterization of mannuronan C-5-epimerase genes from the brown alga Laminaria digitata. Plant Physiol. 133, 726-735 (Pubitemid 37325682)
    • (2003) Plant Physiology , vol.133 , Issue.2 , pp. 726-735
    • Nyvall, P.1    Corre, E.2    Boisset, C.3    Barbeyron, T.4    Rousvoal, S.5    Scornet, D.6    Kloareg, B.7    Boyen, C.8
  • 10
    • 53549135738 scopus 로고    scopus 로고
    • Expression profiling of the mannuronan C5-epimerase multigenic family in the brown alga Laminara digitata (Phaeophyceae) under biotic stress conditions
    • Tonon, T., Rousvoal, S., Roeder, V., and Boyen, C. (2008) Expression profiling of the mannuronan C5-epimerase multigenic family in the brown alga Laminara digitata (Phaeophyceae) under biotic stress conditions. J. Phycol. 44, 1250-1256
    • (2008) J. Phycol. , vol.44 , pp. 1250-1256
    • Tonon, T.1    Rousvoal, S.2    Roeder, V.3    Boyen, C.4
  • 11
    • 0021764892 scopus 로고
    • The purification and chemical characterisation of the alginate present in extracellular material produced by mucoid strains of Pseudomonas aeruginosa
    • Sherbrock-Cox, V., Russell, N. J., and Gacesa, P. (1984) The purification and chemical characterisation of the alginate present in extracellular material produced by mucoid strains of Pseudomonas aeruginosa. Carbohydr. Res. 135, 147-154
    • (1984) Carbohydr. Res. , vol.135 , pp. 147-154
    • Sherbrock-Cox, V.1    Russell, N.J.2    Gacesa, P.3
  • 12
    • 0023911283 scopus 로고
    • Alginate inhibition of the uptake of Pseudomonas aeruginosa by macrophages
    • Simpson, J. A., Smith, S. E., and Dean, R. T. (1988) Alginate inhibition of the uptake of Pseudomonas aeruginosa by macrophages. J. Gen. Microbiol. 134, 29-36 (Pubitemid 18031722)
    • (1988) Journal of General Microbiology , vol.134 , Issue.1 , pp. 29-36
    • Simpson, J.A.1    Smith, S.E.2    Dean, R.T.3
  • 14
    • 34247610845 scopus 로고    scopus 로고
    • Heparan sulphate proteoglycans fine-tune mammalian physiology
    • DOI 10.1038/nature05817, PII NATURE05817
    • Bishop, J. R., Schuksz, M., and Esko, J. D. (2007) Heparan sulphate proteoglycans fine-tune mammalian physiology. Nature 446, 1030-1037 (Pubitemid 46676065)
    • (2007) Nature , vol.446 , Issue.7139 , pp. 1030-1037
    • Bishop, J.R.1    Schuksz, M.2    Esko, J.D.3
  • 15
    • 0036744549 scopus 로고    scopus 로고
    • Dermatan sulfate: New functions from an old glycosaminoglycan
    • Trowbridge, J. M., and Gallo, R. L. (2002) Dermatan sulfate: new functions from an old glycosaminoglycan. Glycobiology 12, 117R-125R
    • (2002) Glycobiology , vol.12
    • Trowbridge, J.M.1    Gallo, R.L.2
  • 16
    • 0043210538 scopus 로고    scopus 로고
    • Targeted disruption of a murine glucuronyl C5-epimerase gene results in heparan sulfate lacking L-iduronic acid and in neonatal lethality
    • DOI 10.1074/jbc.C300219200
    • Li, J. P., Gong, F., Hagner-McWhirter, A., Forsberg, E., Abrink, M., Kisilevsky, R., Zhang, X., and Lindahl, U. (2003) Targeted disruption of a murine glucuronyl C5-epimerase gene results in heparan sulfate lacking L-iduronic acid and in neonatal lethality. J. Biol. Chem. 278, 28363-28366 (Pubitemid 36935735)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.31 , pp. 28363-28366
    • Li, J.-P.1    Gong, F.2    Hagner-McWhirter, A.3    Forsberg, E.4    Abrink, M.5    Kisilevsky, R.6    Zhang, X.7    Lindahl, U.8
  • 18
    • 0035997376 scopus 로고    scopus 로고
    • Order out of chaos: Assembly of ligand binding sites in heparan sulfate
    • DOI 10.1146/annurev.biochem.71.110601.135458
    • Esko, J. D., and Selleck, S. B. (2002) Order out of chaos: assembly of ligand binding sites in heparan sulfate. Annu. Rev. Biochem. 71, 435-471 (Pubitemid 34800227)
    • (2002) Annual Review of Biochemistry , vol.71 , pp. 435-471
    • Esko, J.D.1    Selleck, S.B.2
  • 19
    • 84860188732 scopus 로고    scopus 로고
    • Biosynthesis of the Pseudomonas aeruginosa extracellular polysaccharides, alginate, Pel, and Psl
    • Franklin, M. J., Nivens, D. E., Weadge, J. T., and Howell, P. L. (2011) Biosynthesis of the Pseudomonas aeruginosa extracellular polysaccharides, alginate, Pel, and Psl. Front. Microbiol. 2, 167
    • (2011) Front. Microbiol. , vol.2 , pp. 167
    • Franklin, M.J.1    Nivens, D.E.2    Weadge, J.T.3    Howell, P.L.4
  • 20
    • 0001323496 scopus 로고
    • Alginate-modifying enzymes.Aproposed unified mechanism of action for the lyases and epimerases
    • Gacesa, P. (1987) Alginate-modifying enzymes.Aproposed unified mechanism of action for the lyases and epimerases. FEBS Lett. 212, 199-202
    • (1987) FEBS Lett. , vol.212 , pp. 199-202
    • Gacesa, P.1
  • 21
    • 33746585660 scopus 로고    scopus 로고
    • Chemical mechanism and specificity of the C5-mannuronan epimerase reaction
    • DOI 10.1021/bi060748f
    • Jerga, A., Stanley, M. D., and Tipton, P. A. (2006) Chemical mechanism and specificity of the C5-mannuronan epimerase reaction. Biochemistry 45, 9138-9144 (Pubitemid 44156376)
    • (2006) Biochemistry , vol.45 , Issue.30 , pp. 9138-9144
    • Jerga, A.1    Stanley, M.D.2    Tipton, P.A.3
  • 22
    • 0034800374 scopus 로고    scopus 로고
    • InterProScan - An integration platform for the signature-recognition methods in InterPro
    • Zdobnov, E. M., and Apweiler, R. (2001) InterProScan - an integration platform for the signature-recognition methods in InterPro. Bioinformatics 17, 847-848 (Pubitemid 32970486)
    • (2001) Bioinformatics , vol.17 , Issue.9 , pp. 847-848
    • Zdobnov, E.M.1    Apweiler, R.2
  • 23
    • 53049084215 scopus 로고    scopus 로고
    • Structural and mutational characterization of the catalytic A-module of the mannuronan C-5-epimerase AlgE4 from Azotobacter vinelandii
    • Rozeboom, H. J., Bjerkan, T. M., Kalk, K. H., Ertesvåg, H., Holtan, S., Aachmann, F. L., Valla, S., and Dijkstra, B. W. (2008) Structural and mutational characterization of the catalytic A-module of the mannuronan C-5-epimerase AlgE4 from Azotobacter vinelandii. J. Biol. Chem. 283, 23819-23828
    • (2008) J. Biol. Chem. , vol.283 , pp. 23819-23828
    • Rozeboom, H.J.1    Bjerkan, T.M.2    Kalk, K.H.3    Ertesvåg, H.4    Holtan, S.5    Aachmann, F.L.6    Valla, S.7    Dijkstra, B.W.8
  • 24
    • 0029059225 scopus 로고
    • A family of modular type mannuronan C-5-epimerase genes controls alginate structure in Azotobacter vinelandii
    • Ertesvåg, H., Høidal, H. K., Hals, I. K., Rian, A., Doseth, B., and Valla, S. (1995) A family of modular type mannuronan C-5-epimerase genes controls alginate structure in Azotobacter vinelandii. Mol. Microbiol. 16, 719-731
    • (1995) Mol. Microbiol. , vol.16 , pp. 719-731
    • Ertesvåg, H.1    Høidal, H.K.2    Hals, I.K.3    Rian, A.4    Doseth, B.5    Valla, S.6
  • 25
    • 0344196983 scopus 로고    scopus 로고
    • Cloning and expression of three new Azotobacter vinelandii genes closely related to a previously described gene family encoding mannuronan C-5- epimerases
    • Svanem, B. I., Skjåk-Braek, G., Ertesvåg, H., and Valla, S. (1999) Cloning and expression of three new Azotobacter vinelandii genes closely related to a previously described gene family encoding mannuronan C-5-epimerases. J. Bacteriol. 181, 68-77 (Pubitemid 29013655)
    • (1999) Journal of Bacteriology , vol.181 , Issue.1 , pp. 68-77
    • Svanem, B.I.G.1    Skjak-Braek, G.2    Ertesvag, H.3    Valla, S.4
  • 26
    • 0025328709 scopus 로고
    • Cloning of Pseudomonas aeruginosa algG, which controls alginate structure
    • Chitnis, C. E., and Ohman, D. E. (1990) Cloning of Pseudomonas aeruginosa algG, which controls alginate structure. J. Bacteriol. 172, 2894-2900 (Pubitemid 20179734)
    • (1990) Journal of Bacteriology , vol.172 , Issue.6 , pp. 2894-2900
    • Chitnis, C.E.1    Ohman, D.E.2
  • 27
    • 0029796042 scopus 로고    scopus 로고
    • A new Azotobacter vinelandii mannuronan C-5-epimerase gene (algG) is part of an alg gene cluster physically organized in a manner similar to that in Pseudomonas aeruginosa
    • Rehm, B. H., Ertesvåg, H., and Valla, S. (1996) A new Azotobacter vinelandii mannuronan C-5-epimerase gene (algG) is part of an alg gene cluster physically organized in a manner similar to that in Pseudomonas aeruginosa. J. Bacteriol. 178, 5884-5889 (Pubitemid 26337770)
    • (1996) Journal of Bacteriology , vol.178 , Issue.20 , pp. 5884-5889
    • Rehm, B.H.1    Ertesvag, H.2    Valla, S.3
  • 28
    • 0042849031 scopus 로고    scopus 로고
    • Characterization of the alginate biosynthetic gene cluster in Pseudomonas syringae pv. syringae
    • Peñaloza-Vázquez, A., Kidambi, S. P., Chakrabarty, A. M., and Bender, C. L. (1997) Characterization of the alginate biosynthetic gene cluster in Pseudomonas syringae pv. syringae. J. Bacteriol. 179, 4464-4472 (Pubitemid 27299061)
    • (1997) Journal of Bacteriology , vol.179 , Issue.14 , pp. 4464-4472
    • Penaloza-Vazquez, A.1    Kidambi, S.P.2    Chakrabarty, A.M.3    Bender, C.L.4
  • 29
    • 0035980652 scopus 로고    scopus 로고
    • Characterization of algG encoding C5-epimerase in the alginate biosynthetic gene cluster of Pseudomonas fluorescens
    • DOI 10.1016/S0378-1119(01)00685-0, PII S0378111901006850
    • Morea, A., Mathee, K., Franklin, M. J., Giacomini, A., O'Regan, M., and Ohman, D. E. (2001) Characterization of algG encoding C5-epimerase in the alginate biosynthetic gene cluster of Pseudomonas fluorescens. Gene 278, 107-114 (Pubitemid 33055784)
    • (2001) Gene , vol.278 , Issue.1-2 , pp. 107-114
    • Morea, A.1    Mathee, K.2    Franklin, M.J.3    Giacomini, A.4    O'Regan, M.5    Ohman, D.E.6
  • 31
    • 30744475705 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa C5-mannuronan epimerase: Steady-state kinetics and characterization of the product
    • DOI 10.1021/bi051862l
    • Jerga, A., Raychaudhuri, A., and Tipton, P. A. (2006) Pseudomonas aeruginosa C5-mannuronan epimerase: steady-state kinetics and characterization of the product. Biochemistry 45, 552-560 (Pubitemid 43100420)
    • (2006) Biochemistry , vol.45 , Issue.2 , pp. 552-560
    • Jerga, A.1    Raychaudhuri, A.2    Tipton, P.A.3
  • 33
    • 78651267246 scopus 로고    scopus 로고
    • Pseudomonas Genome Database: Improved comparative analysis and population genomics capability for Pseudomonas genomes
    • Winsor, G. L., Lam, D. K., Fleming, L., Lo, R., Whiteside, M. D., Yu, N. Y., Hancock, R. E., and Brinkman, F. S. (2011) Pseudomonas Genome Database: improved comparative analysis and population genomics capability for Pseudomonas genomes. Nucleic Acids Res. 39, D596-D600
    • (2011) Nucleic Acids Res. , vol.39
    • Winsor, G.L.1    Lam, D.K.2    Fleming, L.3    Lo, R.4    Whiteside, M.D.5    Yu, N.Y.6    Hancock, R.E.7    Brinkman, F.S.8
  • 34
    • 0024500497 scopus 로고
    • Molecular cloning and heterologous expression of a Klebsiella pneumoniae gene encoding alginate lyase
    • DOI 10.1016/0378-1119(89)90389-2
    • Caswell, R. C., Gacesa, P., Lutrell, K. E., and Weightman, A. J. (1989) Molecular cloning and heterologous expression of a Klebsiella pneumoniae gene encoding alginate lyase. Gene 75, 127-134 (Pubitemid 19077767)
    • (1989) Gene , vol.75 , Issue.1 , pp. 127-134
    • Caswell, R.C.1    Gacesa, P.2    Lutrell, K.E.3    Weightman, A.J.4
  • 35
    • 0034793650 scopus 로고    scopus 로고
    • Structure of E. coli 5′-methylthioadenosine/S-adenosylhomocysteine nucleosidase reveals similarity to the purine nucleoside phosphorylases
    • DOI 10.1016/S0969-2126(01)00656-6, PII S0969212601006566
    • Lee, J. E., Cornell, K. A., Riscoe, M. K., and Howell, P. L. (2001) Structure of E. coli 5′-methylthioadenosine/S-adenosylhomocysteine nucleosidase reveals similarity to the purine nucleoside phosphorylases. Structure 9, 941-953 (Pubitemid 32972160)
    • (2001) Structure , vol.9 , Issue.10 , pp. 941-953
    • Lee, J.E.1    Cornell, K.A.2    Riscoe, M.K.3    Howell, P.L.4
  • 37
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • DOI 10.1016/S0076-6879(97)76066-X
    • Otwinowski, Z., and Minor, W. (1997) Processing of x-ray diffraction data collection in oscillation mode. Methods Enzymol. 276, 307-326 (Pubitemid 27085611)
    • (1997) Methods in Enzymology , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 38
    • 4644366388 scopus 로고    scopus 로고
    • HKL2MAP: A graphical user interface for phasing with SHELX programs
    • Pape, T., and Schneider, T. R. (2004) HKL2MAP: a graphical user interface for phasing with SHELX programs. J. Appl. Crystallogr. 37, 843-844
    • (2004) J. Appl. Crystallogr. , vol.37 , pp. 843-844
    • Pape, T.1    Schneider, T.R.2
  • 42
    • 66549119395 scopus 로고    scopus 로고
    • Advances and pitfalls of protein structural alignment
    • Hasegawa, H., and Holm, L. (2009) Advances and pitfalls of protein structural alignment. Curr. Opin. Struct. Biol. 19, 341-348
    • (2009) Curr. Opin. Struct. Biol. , vol.19 , pp. 341-348
    • Hasegawa, H.1    Holm, L.2
  • 43
    • 3242886771 scopus 로고    scopus 로고
    • PDB2PQR: An automated pipeline for the setup of Poisson-Boltzmann electrostatics calculations
    • DOI 10.1093/nar/gkh381
    • Dolinsky, T. J., Nielsen, J. E., McCammon, J. A., and Baker, N. A. (2004) PDB2PQR: an automated pipeline for the setup of Poisson-Boltzmann electrostatics calculations. Nucleic Acids Res. 32, W665-W667 (Pubitemid 38997419)
    • (2004) Nucleic Acids Research , vol.32 , Issue.WEB SERVER ISS.
    • Dolinsky, T.J.1    Nielsen, J.E.2    McCammon, J.A.3    Baker, N.A.4
  • 45
    • 77954257799 scopus 로고    scopus 로고
    • ConSurf 2010: Calculating evolutionary conservation in sequence and structure of proteins and nucleic acids
    • Ashkenazy, H., Erez, E., Martz, E., Pupko, T., and Ben-Tal, N. (2010) ConSurf 2010: calculating evolutionary conservation in sequence and structure of proteins and nucleic acids. Nucleic Acids Res. 38, W529-W533
    • (2010) Nucleic Acids Res. , vol.38
    • Ashkenazy, H.1    Erez, E.2    Martz, E.3    Pupko, T.4    Ben-Tal, N.5
  • 46
    • 0034623005 scopus 로고    scopus 로고
    • T-Coffee: A novel method for fast and accurate multiple sequence alignment
    • Notredame, C., Higgins, D. G., and Heringa, J. (2000) T-Coffee: a novel method for fast and accurate multiple sequence alignment. J. Mol. Biol. 302, 205-217
    • (2000) J. Mol. Biol. , vol.302 , pp. 205-217
    • Notredame, C.1    Higgins, D.G.2    Heringa, J.3
  • 47
    • 0000858160 scopus 로고
    • Alginic acid metabolism in bacteria. I. Enzymatic formation of unsaturated oligosaccharides and 4-deoxy-L-erythro-5-hexoseulose uronic acid
    • Preiss, J., and Ashwell, G. (1962) Alginic acid metabolism in bacteria. I. Enzymatic formation of unsaturated oligosaccharides and 4-deoxy-L-erythro-5- hexoseulose uronic acid. J. Biol. Chem. 237, 309-316
    • (1962) J. Biol. Chem. , vol.237 , pp. 309-316
    • Preiss, J.1    Ashwell, G.2
  • 49
    • 0141958921 scopus 로고    scopus 로고
    • Influence of solution and gas phase processes on protein-carbohydrate binding affinities determined by nanoelectrospray fourier transform ion cyclotron resonance mass spectrometry
    • DOI 10.1021/ac034300l
    • Wang, W., Kitova, E. N., and Klassen, J. S. (2003) Influence of solution and gas phase processes on protein-carbohydrate binding affinities determined by nanoelectrospray Fourier transform ion cyclotron resonance mass spectrometry. Anal. Chem. 75, 4945-4955 (Pubitemid 37238544)
    • (2003) Analytical Chemistry , vol.75 , Issue.19 , pp. 4945-4955
    • Wang, W.1    Kitova, E.N.2    Klassen, J.S.3
  • 50
    • 84860557228 scopus 로고    scopus 로고
    • Reliable determinations of protein-ligand interactions by direct ESI-MS measurements. Are we there yet?
    • Kitova, E. N., El-Hawiet, A., Schnier, P. D., and Klassen, J. S. (2012) Reliable determinations of protein-ligand interactions by direct ESI-MS measurements. Are we there yet? J. Am. Soc. Mass Spectrom. 23, 431-441
    • (2012) J. Am. Soc. Mass Spectrom. , vol.23 , pp. 431-441
    • Kitova, E.N.1    El-Hawiet, A.2    Schnier, P.D.3    Klassen, J.S.4
  • 51
    • 33646589615 scopus 로고    scopus 로고
    • Method for distinguishing specific from nonspecific protein-ligand complexes in nanoelectrospray ionization mass spectrometry
    • DOI 10.1021/ac0522005
    • Sun, J., Kitova, E. N., Wang, W., and Klassen, J. S. (2006) Method for distinguishing specific from nonspecific protein-ligand complexes in nanoelectrospray ionization mass spectrometry. Anal. Chem. 78, 3010-3018 (Pubitemid 43726119)
    • (2006) Analytical Chemistry , vol.78 , Issue.9 , pp. 3010-3018
    • Sun, J.1    Kitova, E.N.2    Wang, W.3    Klassen, J.S.4
  • 52
    • 0027329090 scopus 로고
    • New domain motif: The structure of pectate lyase C, a secreted plant virulence factor
    • Yoder, M. D., Keen, N. T., and Jurnak, F. (1993) New domain motif: the structure of pectate lyase C, a secreted plant virulence factor. Science 260, 1503-1507 (Pubitemid 23273264)
    • (1993) Science , vol.260 , Issue.5113 , pp. 1503-1507
    • Yoder, M.D.1    Keen, N.T.2    Jurnak, F.3
  • 53
    • 21144450242 scopus 로고    scopus 로고
    • Epimerase active domain of Pseudomonas aeruginosa AlgG, a protein that contains a right-handed β-helix
    • DOI 10.1128/JB.187.13.4573-4583.2005
    • Douthit, S. A., Dlakic, M., Ohman, D. E., and Franklin, M. J. (2005) Epimerase active domain of Pseudomonas aeruginosa AlgG, a protein that contains a right-handed β-helix. J. Bacteriol. 187, 4573-4583 (Pubitemid 40880969)
    • (2005) Journal of Bacteriology , vol.187 , Issue.13 , pp. 4573-4583
    • Douthit, S.A.1    Dlakic, M.2    Ohman, D.E.3    Franklin, M.J.4
  • 55
    • 0036470163 scopus 로고    scopus 로고
    • CASH - A β-helix domain widespread among carbohydrate-binding proteins
    • DOI 10.1016/S0968-0004(01)02046-1, PII S0968000401020461
    • Ciccarelli, F. D., Copley, R. R., Doerks, T., Russell, R. B., and Bork, P. (2002) CASH - a β-helix domain widespread among carbohydrate-binding proteins. Trends Biochem. Sci. 27, 59-62 (Pubitemid 34164317)
    • (2002) Trends in Biochemical Sciences , vol.27 , Issue.2 , pp. 59-62
    • Ciccarelli, F.D.1    Copley, R.R.2    Doerks, T.3    Russell, R.B.4    Bork, P.5
  • 57
    • 78149351036 scopus 로고    scopus 로고
    • Structural and mechanistic classification of uronic acid-containing polysaccharide lyases
    • Garron, M. L., and Cygler, M. (2010) Structural and mechanistic classification of uronic acid-containing polysaccharide lyases. Glycobiology 20, 1547-1573
    • (2010) Glycobiology , vol.20 , pp. 1547-1573
    • Garron, M.L.1    Cygler, M.2
  • 59
    • 0031594282 scopus 로고    scopus 로고
    • The three-dimensional structure of Aspergillus niger pectin lyase b at 1.7-Å resolution
    • Vitali, J., Schick, B., Kester, H. C., Visser, J., and Jurnak, F. (1998) The tree-dimensional structure of Aspergillus niger pectin lyase B at 1.7-Å resolution. Plant Physiol. 116, 69-80 (Pubitemid 28503842)
    • (1998) Plant Physiology , vol.116 , Issue.1 , pp. 69-80
    • Vitali, J.1    Schick, B.2    Kester, H.C.M.3    Visser, J.4    Jurnak, F.5
  • 60
    • 0031570284 scopus 로고    scopus 로고
    • Two crystal structures of pectin lyase A from Aspergillus reveal a pH driven conformational change and striking divergence in the substrate-binding clefts of pectin and pectate lyases
    • Mayans, O., Scott, M., Connerton, I., Gravesen, T., Benen, J., Visser, J., Pickersgill, R., and Jenkins, J. (1997) Two crystal structures of pectin lyase A from Aspergillus reveal a pH driven conformational change and striking divergence in the substrate-binding clefts of pectin and pectate lyases. Structure 5, 677-689 (Pubitemid 27236266)
    • (1997) Structure , vol.5 , Issue.5 , pp. 677-689
    • Mayans, O.1    Scott, M.2    Connerton, I.3    Gravesen, T.4    Benen, J.5    Visser, J.6    Pickersgill, R.7    Jenkins, J.8
  • 61
    • 79951476387 scopus 로고    scopus 로고
    • PROPKA3: Consistent treatment of internal and surface residues in empirical pKa predictions
    • Olsson, M. H. M., Søndergaard, C. R., Rostkowski, M., and Jensen, J. H. (2011) PROPKA3: consistent treatment of internal and surface residues in empirical pKa predictions. J. Chem. Theory Comput. 7, 525-537
    • (2011) J. Chem. Theory Comput. , vol.7 , pp. 525-537
    • Olsson, M.H.M.1    Søndergaard, C.R.2    Rostkowski, M.3    Jensen, J.H.4
  • 62
    • 0037610166 scopus 로고    scopus 로고
    • The Pseudomonas fluorescens AlgG protein, but not its mannuronan C-5-epimerase activity, is needed for alginate polymer formation
    • DOI 10.1128/JB.185.12.3515-3523.2003
    • Gimmestad, M., Sletta, H., Ertesvåg, H., Bakkevig, K., Jain, S., Suh, S. J., Skjåk-Braek, G., Ellingsen, T. E., Ohman, D. E., and Valla, S. (2003) The Pseudomonas fluorescens AlgG protein, but not its mannuronan C-5-epimerase activity, is needed for alginate polymer formation. J. Bacteriol. 185, 3515-3523 (Pubitemid 36676417)
    • (2003) Journal of Bacteriology , vol.185 , Issue.12 , pp. 3515-3523
    • Gimmestad, M.1    Sletta, H.2    Ertesvag, H.3    Bakkevig, K.4    Jain, S.5    Suh, S.-J.6    Skjak-Braek, G.7    Ellingsen, T.E.8    Ohman, D.E.9    Valla, S.10
  • 64
    • 59449098994 scopus 로고    scopus 로고
    • Identification of the active site of DS-epimerase 1 and requirement of N-glycosylation for enzyme function
    • Pacheco, B., Maccarana, M., Goodlett, D. R., Malmström, A., and Malmström, L. (2009) Identification of the active site of DS-epimerase 1 and requirement of N-glycosylation for enzyme function. J. Biol. Chem. 284, 1741-1747
    • (2009) J. Biol. Chem. , vol.284 , pp. 1741-1747
    • Pacheco, B.1    Maccarana, M.2    Goodlett, D.R.3    Malmström, A.4    Malmström, L.5
  • 65
    • 63849246525 scopus 로고    scopus 로고
    • Protein structure prediction on the web: A case study using the Phyre server
    • Kelley, L. A., and Sternberg, M. J. (2009) Protein structure prediction on the web: a case study using the Phyre server. Nat. Protoc. 4, 363-371
    • (2009) Nat. Protoc. , vol.4 , pp. 363-371
    • Kelley, L.A.1    Sternberg, M.J.2
  • 66
    • 0033617262 scopus 로고    scopus 로고
    • The recombinant Azotobacter vinelandii mannuronan C-5-epimerase AlgE4 epimerizes alginate by a nonrandom attack mechanism
    • Høidal, H. K., Ertesvåg, H., Skjåk-Braek, G., Stokke, B. T., and Valla, S. (1999) The recombinant Azotobacter vinelandii mannuronan C-5-epimerase AlgE4 epimerizes alginate by a nonrandom attack mechanism. J. Biol. Chem. 274, 12316-12322
    • (1999) J. Biol. Chem. , vol.274 , pp. 12316-12322
    • Høidal, H.K.1    Ertesvåg, H.2    Skjåk-Braek, G.3    Stokke, B.T.4    Valla, S.5
  • 67
    • 6344275008 scopus 로고    scopus 로고
    • Calcium signalling in bacteria
    • Dominguez, D. C. (2004) Calcium signalling in bacteria. Mol. Microbiol. 54, 291-297
    • (2004) Mol. Microbiol. , vol.54 , pp. 291-297
    • Dominguez, D.C.1
  • 68
    • 84866334596 scopus 로고    scopus 로고
    • LapG, required for modulating biofilm formation by Pseudomonas fluorescens Pf0-1, is a calcium-dependent protease
    • Boyd, C. D., Chatterjee, D., Sondermann, H., and O'Toole, G. A. (2012) LapG, required for modulating biofilm formation by Pseudomonas fluorescens Pf0-1, is a calcium-dependent protease. J. Bacteriol. 194, 4406-4414
    • (2012) J. Bacteriol. , vol.194 , pp. 4406-4414
    • Boyd, C.D.1    Chatterjee, D.2    Sondermann, H.3    O'Toole, G.A.4
  • 69
    • 0015197907 scopus 로고
    • Biosynthesis of alginate. 3. Tritium incorporation with polymannuronic acid 5-epimerase from Azotobacter vinelandii
    • Larsen, B., and Haug, A. (1971) Biosynthesis of alginate. 3. Tritium incorporation with polymannuronic acid 5-epimerase from Azotobacter vinelandii. Carbohydr. Res. 20, 225-232
    • (1971) Carbohydr. Res. , vol.20 , pp. 225-232
    • Larsen, B.1    Haug, A.2
  • 71
    • 49649090029 scopus 로고    scopus 로고
    • The crystal structure of pectate lyase peli from soft rot pathogen Erwinia chrysanthemi in complex with its substrate
    • Creze, C., Castang, S., Derivery, E., Haser, R., Hugouvieux-Cotte-Pattat, N., Shevchik, V. E., and Gouet, P. (2008) The crystal structure of pectate lyase peli from soft rot pathogen Erwinia chrysanthemi in complex with its substrate. J. Biol. Chem. 283, 18260-18268
    • (2008) J. Biol. Chem. , vol.283 , pp. 18260-18268
    • Creze, C.1    Castang, S.2    Derivery, E.3    Haser, R.4    Hugouvieux-Cotte-Pattat, N.5    Shevchik, V.E.6    Gouet, P.7
  • 73
    • 0032553312 scopus 로고    scopus 로고
    • The azotobacter vinelandii mannuronan C-5-epimerase AlgE1 consists of two separate catalytic domains
    • DOI 10.1074/jbc.273.47.30927
    • Ertesvåg, H., Høidal, H. K., Skjåk-Braek, G., and Valla, S. (1998) The Azotobacter vinelandii mannuronan C-5-epimerase AlgE1 consists of two separate catalytic domains. J. Biol. Chem. 273, 30927-30932 (Pubitemid 28533095)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.47 , pp. 30927-30932
    • Ertesvag, H.1    Hoidal, H.K.2    Skjak-Braek, G.3    Valla, S.4
  • 74
    • 0035793153 scopus 로고    scopus 로고
    • Influence of environmental conditions on the activity of the recombinant mannuronan C-5-epimerase AlgE2
    • Ramstadab, M. V., Markussen, S., Ellingsen, T. E., Skjåk-Braek, G., and Levine, D. W. (2001) Influence of environmental conditions on the activity of the recombinant mannuronan C-5-epimerase AlgE2. Enzyme Microb. Technol. 28, 57-69
    • (2001) Enzyme Microb. Technol. , vol.28 , pp. 57-69
    • Ramstadab, M.V.1    Markussen, S.2    Ellingsen, T.E.3    Skjåk-Braek, G.4    Levine, D.W.5
  • 75
    • 0035943715 scopus 로고    scopus 로고
    • The catalytic activities of the bifunctional Azotobacter vinelandii mannuronan C-5-epimerase and alginate lyase AlgE7 probably originate from the same active site in the enzyme
    • Svanem, B. I., Strand, W. I., Ertesvag, H., Skjåk-Braek, G., Hartmann, M., Barbeyron, T., and Valla, S. (2001) The catalytic activities of the bifunctional Azotobacter vinelandii mannuronan C-5-epimerase and alginate lyase AlgE7 probably originate from the same active site in the enzyme. J. Biol. Chem. 276, 31542-31550
    • (2001) J. Biol. Chem. , vol.276 , pp. 31542-31550
    • Svanem, B.I.1    Strand, W.I.2    Ertesvag, H.3    Skjåk-Braek, G.4    Hartmann, M.5    Barbeyron, T.6    Valla, S.7
  • 76
    • 0030071225 scopus 로고    scopus 로고
    • Biosynthesis of dermatan sulphate. Defructosylated Escherichia coli K4 capsular polysaccharide as a substrate for the D-glucuronyl C-5 epimerase, and an indication of a two-base reaction mechanism
    • Hannesson, H. H., Hagner-McWhirter, A., Tiedemann, K., Lindahl, U., and Malmström, A. (1996) Biosynthesis of dermatan sulphate. Defructosylated Escherichia coli K4 capsular polysaccharide as a substrate for the D-glucuronyl C-5 epimerase, and an indication of a two-base reaction mechanism. Biochem. J. 313, 589-596
    • (1996) Biochem. J. , vol.313 , pp. 589-596
    • Hannesson, H.H.1    Hagner-McWhirter, A.2    Tiedemann, K.3    Lindahl, U.4    Malmström, A.5
  • 77
    • 0034177670 scopus 로고    scopus 로고
    • Biosynthesis of heparin/heparan sulphate: Mechanism of epimerization of glucuronyl C-5
    • DOI 10.1042/0264-6021:3470069
    • Hagner-Mcwhirter, A., Lindahl, U., and Li, J. (2000) Biosynthesis of heparin/heparan sulphate: mechanism of epimerization of glucuronyl C-5. Biochem. J. 347, 69-75 (Pubitemid 30199042)
    • (2000) Biochemical Journal , vol.347 , Issue.1 , pp. 69-75
    • Hagner-McWhirter, A.1    Lindahl, U.2    Li, J.-P.3
  • 78
    • 84873107819 scopus 로고    scopus 로고
    • Synthase-dependent exopolysaccharide secretion in Gram-negative bacteria
    • Whitney, J. C., and Howell, P. L. (2013) Synthase-dependent exopolysaccharide secretion in Gram-negative bacteria. Trends Microbiol. 21, 63-72
    • (2013) Trends Microbiol. , vol.21 , pp. 63-72
    • Whitney, J.C.1    Howell, P.L.2
  • 79
    • 84872141928 scopus 로고    scopus 로고
    • Crystallographic snapshot of cellulose synthesis and membrane translocation
    • Morgan, J. L., Strumillo, J., and Zimmer, J. (2013) Crystallographic snapshot of cellulose synthesis and membrane translocation. Nature 493, 181-186
    • (2013) Nature , vol.493 , pp. 181-186
    • Morgan, J.L.1    Strumillo, J.2    Zimmer, J.3
  • 81
    • 0034850147 scopus 로고    scopus 로고
    • A structural basis for processivity
    • DOI 10.1110/ps.10301
    • Breyer, W. A., and Matthews, B. W. (2001) A structural basis for processivity. Protein Sci. 10, 1699-1711 (Pubitemid 32851041)
    • (2001) Protein Science , vol.10 , Issue.9 , pp. 1699-1711
    • Breyer, W.A.1    Matthews, B.W.2
  • 82
    • 3142782823 scopus 로고    scopus 로고
    • Biochemical analysis of the processive mechanism for epimerization of alginate by mannuronan C-5 epimerase AlgE4
    • DOI 10.1042/BJ20031265
    • Campa, C., Holtan, S., Nilsen, N., Bjerkan, T. M., Stokke, B. T., and Skjåk-Braek, G. (2004) Biochemical analysis of the processive mechanism for epimerization of alginate by mannuronan C-5 epimerase AlgE4. Biochem. J. 381, 155-164 (Pubitemid 38937048)
    • (2004) Biochemical Journal , vol.381 , Issue.1 , pp. 155-164
    • Campa, C.1    Holtan, S.2    Nilsen, N.3    Bjerkan, T.M.4    Stokke, B.T.5    Skjak-Braek, G.6
  • 83
    • 33645756079 scopus 로고    scopus 로고
    • Mode of action and subsite studies of the guluronan block-forming mannuronan C-5 epimerases AlgE1 and AlgE6
    • Holtan, S., Bruheim, P., and Skjåk-Braek, G. (2006) Mode of action and subsite studies of the guluronan block-forming mannuronan C-5 epimerases AlgE1 and AlgE6. Biochem. J. 395, 319-329
    • (2006) Biochem. J. , vol.395 , pp. 319-329
    • Holtan, S.1    Bruheim, P.2    Skjåk-Braek, G.3
  • 84
    • 4143059011 scopus 로고    scopus 로고
    • Single-molecular pain unbinding studies of mannuronan C-5 epimerase AlgE4 and its polymer substrate
    • DOI 10.1021/bm0345211
    • Sletmoen, M., Skjåk-Braek, G., and Stokke, B. T. (2004) Single-molecular pair unbinding studies of mannuronan C-5 epimerase AlgE4 and its polymer substrate. Biomacromolecules 5, 1288-1295 (Pubitemid 39099115)
    • (2004) Biomacromolecules , vol.5 , Issue.4 , pp. 1288-1295
    • Sletmoen, M.1    Skjak-Braek, G.2    Stokke, B.T.3


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