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Volumn 46, Issue D1, 2018, Pages D677-D683

PULDB: The expanded database of Polysaccharide Utilization Loci

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; EPIMERASE; POLYSACCHARIDE; PROTEINASE; SULFATASE; BACTERIAL PROTEIN; BACTERIAL RNA; CARRIER PROTEIN; ENZYME;

EID: 85040905968     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkx1022     Document Type: Article
Times cited : (188)

References (47)
  • 1
    • 55249108031 scopus 로고    scopus 로고
    • Mucosal glycan foraging enhances fitness and transmission of a saccharolytic human gut bacterial symbiont
    • Martens, E.C., Chiang, H.C., Gordon, J.I. (2008) Mucosal glycan foraging enhances fitness and transmission of a saccharolytic human gut bacterial symbiont. Cell Host Microbe, 4, 447-457.
    • (2008) Cell Host Microbe , vol.4 , pp. 447-457
    • Martens, E.C.1    Chiang, H.C.2    Gordon, J.I.3
  • 2
    • 84879411201 scopus 로고    scopus 로고
    • The abundance and variety of carbohydrate-active enzymes in the human gut microbiota
    • El Kaoutari, A., Armougom, F., Gordon, J.I., Raoult, D., Henrissat, B. (2013) The abundance and variety of carbohydrate-active enzymes in the human gut microbiota. Nat. Rev. Microbiol., 11, 497-504.
    • (2013) Nat. Rev. Microbiol , vol.11 , pp. 497-504
    • El Kaoutari, A.1    Armougom, F.2    Gordon, J.I.3    Raoult, D.4    Henrissat, B.5
  • 3
    • 84928985213 scopus 로고    scopus 로고
    • Automatic prediction of polysaccharide utilization loci in Bacteroidetes species
    • Terrapon, N., Lombard, V., Gilbert, H.J., Henrissat, B. (2015) Automatic prediction of polysaccharide utilization loci in Bacteroidetes species. Bioinformatics, 31, 647-655.
    • (2015) Bioinformatics , vol.31 , pp. 647-655
    • Terrapon, N.1    Lombard, V.2    Gilbert, H.J.3    Henrissat, B.4
  • 6
    • 80053366291 scopus 로고    scopus 로고
    • Interactive metagenomic visualization in a Web browser
    • Ondov, B.D., Bergman, N.H., Phillippy, A.M. (2011) Interactive metagenomic visualization in a Web browser. BMC Bioinformatics, 12, 385.
    • (2011) BMC Bioinformatics , vol.12 , pp. 385
    • Ondov, B.D.1    Bergman, N.H.2    Phillippy, A.M.3
  • 7
    • 84883154681 scopus 로고    scopus 로고
    • Effects of diet on resource utilization by a model human gut microbiota containing Bacteroides cellulosilyticus WH2, a symbiont with an extensive glycobiome
    • McNulty, N.P., Wu, M., Erickson, A.R., Pan, C., Erickson, B.K., Martens, E.C., Pudlo, N.A., Muegge, B.D., Henrissat, B., Hettich, R.L., et al. (2013) Effects of diet on resource utilization by a model human gut microbiota containing Bacteroides cellulosilyticus WH2, a symbiont with an extensive glycobiome. PLoS Biol., 11, e1001637.
    • (2013) PLoS Biol , vol.11 , pp. e1001637
    • McNulty, N.P.1    Wu, M.2    Erickson, A.R.3    Pan, C.4    Erickson, B.K.5    Martens, E.C.6    Pudlo, N.A.7    Muegge, B.D.8    Henrissat, B.9    Hettich, R.L.10
  • 9
    • 84995600712 scopus 로고    scopus 로고
    • Habitat and taxon as driving forces of carbohydrate catabolism in marine heterotrophic bacteria: Example of the model algae-associated bacterium Zobellia galactanivorans DsijT
    • Barbeyron, T., Thomas, F., Barbe, V., Teeling, H., Schenowitz, C., Dossat, C., Goesmann, A., Leblanc, C., Oliver Glockner, F., Czjzek, M., et al. (2016) Habitat and taxon as driving forces of carbohydrate catabolism in marine heterotrophic bacteria: Example of the model algae-associated bacterium Zobellia galactanivorans DsijT. Environ. Microbiol., 18, 4610-4627.
    • (2016) Environ. Microbiol , vol.18 , pp. 4610-4627
    • Barbeyron, T.1    Thomas, F.2    Barbe, V.3    Teeling, H.4    Schenowitz, C.5    Dossat, C.6    Goesmann, A.7    Leblanc, C.8    Oliver Glockner, F.9    Czjzek, M.10
  • 10
    • 80051555789 scopus 로고    scopus 로고
    • The genome and surface proteome of Capnocytophaga canimorsus reveal a key role of glycan foraging systems in host glycoproteins deglycosylation
    • Manfredi, P., Renzi, F., Mally, M., Sauteur, L., Schmaler, M., Moes, S., Jeno, P., Cornelis, G.R. (2011) The genome and surface proteome of Capnocytophaga canimorsus reveal a key role of glycan foraging systems in host glycoproteins deglycosylation. Mol. Microbiol., 81, 1050-1060.
    • (2011) Mol. Microbiol , vol.81 , pp. 1050-1060
    • Manfredi, P.1    Renzi, F.2    Mally, M.3    Sauteur, L.4    Schmaler, M.5    Moes, S.6    Jeno, P.7    Cornelis, G.R.8
  • 11
    • 77953901767 scopus 로고    scopus 로고
    • Specificity of polysaccharide use in intestinal bacteroides species determines diet-induced microbiota alterations
    • Sonnenburg, E.D., Zheng, H., Joglekar, P., Higginbottom, S.K., Firbank, S.J., Bolam, D.N., Sonnenburg, J.L. (2010) Specificity of polysaccharide use in intestinal bacteroides species determines diet-induced microbiota alterations. Cell, 141, 1241-1252.
    • (2010) Cell , vol.141 , pp. 1241-1252
    • Sonnenburg, E.D.1    Zheng, H.2    Joglekar, P.3    Higginbottom, S.K.4    Firbank, S.J.5    Bolam, D.N.6    Sonnenburg, J.L.7
  • 18
    • 85009281007 scopus 로고    scopus 로고
    • Galactomannan catabolism conferred by a polysaccharide utilization locus of Bacteroides ovatus: ENZYME SYNERGY and CRYSTAL STRUCTURE of A beta-MANNANASE
    • Bagenholm, V., Reddy, S.K., Bouraoui, H., Morrill, J., Kulcinskaja, E., Bahr, C.M., Aurelius, O., Rogers, T., Xiao, Y., Logan, D.T., et al. (2017) Galactomannan catabolism conferred by a polysaccharide utilization locus of Bacteroides ovatus: ENZYME SYNERGY AND CRYSTAL STRUCTURE OF A beta-MANNANASE. J. Biol. Chem., 292, 229-243.
    • (2017) J. Biol. Chem , vol.292 , pp. 229-243
    • Bagenholm, V.1    Reddy, S.K.2    Bouraoui, H.3    Morrill, J.4    Kulcinskaja, E.5    Bahr, C.M.6    Aurelius, O.7    Rogers, T.8    Xiao, Y.9    Logan, D.T.10
  • 19
    • 85021683225 scopus 로고    scopus 로고
    • A Bacteroidetes locus dedicated to fungal 1, 6-beta-glucan degradation: Unique substrate conformation drives specificity of the key endo-1, 6-beta-glucanase
    • Temple, M.J., Cuskin, F., Basle, A., Hickey, N., Speciale, G., Williams, S.J., Gilbert, H.J., Lowe, E.C. (2017) A Bacteroidetes locus dedicated to fungal 1, 6-beta-glucan degradation: Unique substrate conformation drives specificity of the key endo-1, 6-beta-glucanase. J. Biol. Chem., 292, 10639-10650.
    • (2017) J. Biol. Chem , vol.292 , pp. 10639-10650
    • Temple, M.J.1    Cuskin, F.2    Basle, A.3    Hickey, N.4    Speciale, G.5    Williams, S.J.6    Gilbert, H.J.7    Lowe, E.C.8
  • 20
    • 84929484307 scopus 로고    scopus 로고
    • Glycan-foraging systems reveal the adaptation of Capnocytophaga canimorsus to the dog mouth
    • Renzi, F., Manfredi, P., Dol, M., Fu, J., Vincent, S., Cornelis, G.R. (2015) Glycan-foraging systems reveal the adaptation of Capnocytophaga canimorsus to the dog mouth. Mbio, 6, e02507.
    • (2015) Mbio , vol.6 , pp. e02507
    • Renzi, F.1    Manfredi, P.2    Dol, M.3    Fu, J.4    Vincent, S.5    Cornelis, G.R.6
  • 21
    • 84857676701 scopus 로고    scopus 로고
    • Characterization of a gene cluster for sialoglycoconjugate utilization in Bacteroides fragilis
    • Nakayama-Imaohji, H., Ichimura, M., Iwasa, T., Okada, N., Ohnishi, Y., Kuwahara, T. (2012) Characterization of a gene cluster for sialoglycoconjugate utilization in Bacteroides fragilis. J. Med. Invest., 59, 79-94.
    • (2012) J. Med. Invest , vol.59 , pp. 79-94
    • Nakayama-Imaohji, H.1    Ichimura, M.2    Iwasa, T.3    Okada, N.4    Ohnishi, Y.5    Kuwahara, T.6
  • 22
    • 79959826593 scopus 로고    scopus 로고
    • The N-glycan glycoprotein deglycosylation complex (Gpd) from Capnocytophaga canimorsus deglycosylates human IgG
    • Renzi, F., Manfredi, P., Mally, M., Moes, S., Jeno, P., Cornelis, G.R. (2011) The N-glycan glycoprotein deglycosylation complex (Gpd) from Capnocytophaga canimorsus deglycosylates human IgG. PLoS Pathog., 7, e1002118.
    • (2011) PLoS Pathog , vol.7 , pp. e1002118
    • Renzi, F.1    Manfredi, P.2    Mally, M.3    Moes, S.4    Jeno, P.5    Cornelis, G.R.6
  • 23
    • 84907228243 scopus 로고    scopus 로고
    • Efficient utilization of complex N-linked glycans is a selective advantage for Bacteroides fragilis in extraintestinal infections
    • Cao, Y., Rocha, E.R., Smith, C.J. (2014) Efficient utilization of complex N-linked glycans is a selective advantage for Bacteroides fragilis in extraintestinal infections. Proc. Natl. Acad. Sci. U.S.A., 111, 12901-12906.
    • (2014) Proc. Natl. Acad. Sci. U.S.A , vol.111 , pp. 12901-12906
    • Cao, Y.1    Rocha, E.R.2    Smith, C.J.3
  • 24
    • 84884411052 scopus 로고    scopus 로고
    • Bacterial colonization factors control specificity and stability of the gut microbiota
    • Lee, S.M., Donaldson, G.P., Mikulski, Z., Boyajian, S., Ley, K., Mazmanian, S.K. (2013) Bacterial colonization factors control specificity and stability of the gut microbiota. Nature, 501, 426-429.
    • (2013) Nature , vol.501 , pp. 426-429
    • Lee, S.M.1    Donaldson, G.P.2    Mikulski, Z.3    Boyajian, S.4    Ley, K.5    Mazmanian, S.K.6
  • 27
    • 84903381348 scopus 로고    scopus 로고
    • Functional characterization of polysaccharide utilization loci in the marine Bacteroidetes 'Gramella forsetii' KT0803
    • Kabisch, A., Otto, A., Konig, S., Becher, D., Albrecht, D., Schuler, M., Teeling, H., Amann, R.I., Schweder, T. (2014) Functional characterization of polysaccharide utilization loci in the marine Bacteroidetes 'Gramella forsetii' KT0803. ISME J., 8, 1492-1502.
    • (2014) ISME J , vol.8 , pp. 1492-1502
    • Kabisch, A.1    Otto, A.2    Konig, S.3    Becher, D.4    Albrecht, D.5    Schuler, M.6    Teeling, H.7    Amann, R.I.8    Schweder, T.9
  • 28
    • 84883435173 scopus 로고    scopus 로고
    • Lacto-N-biosidase encoded by a novel gene of Bifidobacterium longum subspecies longum shows unique substrate specificity and requires a designated chaperone for its active expression
    • Sakurama, H., Kiyohara, M., Wada, J., Honda, Y., Yamaguchi, M., Fukiya, S., Yokota, A., Ashida, H., Kumagai, H., Kitaoka, M., et al. (2013) Lacto-N-biosidase encoded by a novel gene of Bifidobacterium longum subspecies longum shows unique substrate specificity and requires a designated chaperone for its active expression. J. Biol. Chem., 288, 25194-25206.
    • (2013) J. Biol. Chem , vol.288 , pp. 25194-25206
    • Sakurama, H.1    Kiyohara, M.2    Wada, J.3    Honda, Y.4    Yamaguchi, M.5    Fukiya, S.6    Yokota, A.7    Ashida, H.8    Kumagai, H.9    Kitaoka, M.10
  • 31
    • 85019167008 scopus 로고    scopus 로고
    • New ulvan-degrading polysaccharide lyase family: Structure and catalytic mechanism suggests convergent evolution of active site architecture
    • Ulaganathan, T., Boniecki, M.T., Foran, E., Buravenkov, V., Mizrachi, N., Banin, E., Helbert, W., Cygler, M. (2017) New ulvan-degrading polysaccharide lyase family: Structure and catalytic mechanism suggests convergent evolution of active site architecture. ACS Chem. Biol., 12, 1269-1280.
    • (2017) ACS Chem. Biol , vol.12 , pp. 1269-1280
    • Ulaganathan, T.1    Boniecki, M.T.2    Foran, E.3    Buravenkov, V.4    Mizrachi, N.5    Banin, E.6    Helbert, W.7    Cygler, M.8
  • 32
    • 84973345254 scopus 로고    scopus 로고
    • New family of ulvan lyases identified in three isolates from the alteromonadales order
    • Kopel, M., Helbert, W., Belnik, Y., Buravenkov, V., Herman, A., Banin, E. (2016) New family of ulvan lyases identified in three isolates from the alteromonadales order. J. Biol. Chem., 291, 5871-5878.
    • (2016) J. Biol. Chem , vol.291 , pp. 5871-5878
    • Kopel, M.1    Helbert, W.2    Belnik, Y.3    Buravenkov, V.4    Herman, A.5    Banin, E.6
  • 33
    • 84941994584 scopus 로고    scopus 로고
    • Molecular characterization of a Penicillium chrysogenum exo-rhamnogalacturonan lyase that is structurally distinct from other polysaccharide lyase family proteins
    • Iwai, M., Kawakami, T., Ikemoto, T., Fujiwara, D., Takenaka, S., Nakazawa, M., Ueda, M., Sakamoto, T. (2015) Molecular characterization of a Penicillium chrysogenum exo-rhamnogalacturonan lyase that is structurally distinct from other polysaccharide lyase family proteins. Appl. Microbiol. Biotechnol., 99, 8515-8525.
    • (2015) Appl. Microbiol. Biotechnol , vol.99 , pp. 8515-8525
    • Iwai, M.1    Kawakami, T.2    Ikemoto, T.3    Fujiwara, D.4    Takenaka, S.5    Nakazawa, M.6    Ueda, M.7    Sakamoto, T.8
  • 34
    • 85027394586 scopus 로고    scopus 로고
    • An evolutionarily distinct family of polysaccharide lyases removes rhamnose capping of complex arabinogalactan proteins
    • Munoz-Munoz, J., Cartmell, A., Terrapon, N., Basle, A., Henrissat, B., Gilbert, H.J. (2017) An evolutionarily distinct family of polysaccharide lyases removes rhamnose capping of complex arabinogalactan proteins. J. Biol. Chem., 292, 13271-13283.
    • (2017) J. Biol. Chem , vol.292 , pp. 13271-13283
    • Munoz-Munoz, J.1    Cartmell, A.2    Terrapon, N.3    Basle, A.4    Henrissat, B.5    Gilbert, H.J.6
  • 37
    • 85017203954 scopus 로고    scopus 로고
    • Marine polysaccharide sulfatases
    • Helbert, W. (2017) Marine polysaccharide sulfatases. Front. Mar. Sci., 4, 6.
    • (2017) Front. Mar. Sci , vol.4 , pp. 6
    • Helbert, W.1
  • 38
    • 79960418118 scopus 로고    scopus 로고
    • Sulfatases and a radical S-adenosyl-L-methionine (AdoMet) enzyme are key for mucosal foraging and fitness of the prominent human gut symbiont, Bacteroides thetaiotaomicron
    • Benjdia, A., Martens, E.C., Gordon, J.I., Berteau, O. (2011) Sulfatases and a radical S-adenosyl-L-methionine (AdoMet) enzyme are key for mucosal foraging and fitness of the prominent human gut symbiont, Bacteroides thetaiotaomicron. J. Biol. Chem., 286, 25973-25982.
    • (2011) J. Biol. Chem , vol.286 , pp. 25973-25982
    • Benjdia, A.1    Martens, E.C.2    Gordon, J.I.3    Berteau, O.4
  • 39
    • 84992391383 scopus 로고    scopus 로고
    • Matching the diversity of sulfated biomolecules: Creation of a classification database for sulfatases reflecting their substrate specificity
    • Barbeyron, T., Brillet-Gueguen, L., Carre, W., Carriere, C., Caron, C., Czjzek, M., Hoebeke, M., Michel, G. (2016) Matching the diversity of sulfated biomolecules: Creation of a classification database for sulfatases reflecting their substrate specificity. PLoS One, 11, e0164846.
    • (2016) PLoS One , vol.11 , pp. e0164846
    • Barbeyron, T.1    Brillet-Gueguen, L.2    Carre, W.3    Carriere, C.4    Caron, C.5    Czjzek, M.6    Hoebeke, M.7    Michel, G.8
  • 40
    • 84937391752 scopus 로고    scopus 로고
    • Structural biology of the major facilitator superfamily transporters
    • Yan, N. (2015) Structural biology of the major facilitator superfamily transporters. Annu. Rev. Biophys., 44, 257-283.
    • (2015) Annu. Rev. Biophys , vol.44 , pp. 257-283
    • Yan, N.1
  • 42
    • 84863406922 scopus 로고    scopus 로고
    • Sialic acid, periodontal pathogens and Tannerella forsythia: Stick around and enjoy the feast! Mol
    • Stafford, G., Roy, S., Honma, K., Sharma, A. (2012) Sialic acid, periodontal pathogens and Tannerella forsythia: Stick around and enjoy the feast! Mol. Oral Microbiol., 27, 11-22.
    • (2012) Oral Microbiol , vol.27 , pp. 11-22
    • Stafford, G.1    Roy, S.2    Honma, K.3    Sharma, A.4
  • 43
    • 66149087332 scopus 로고    scopus 로고
    • Sialic acid (N-acetyl neuraminic acid) utilization by Bacteroides fragilis requires a novel N-acetyl mannosamine epimerase
    • Brigham, C., Caughlan, R., Gallegos, R., Dallas, M.B., Godoy, V.G., Malamy, M.H. (2009) Sialic acid (N-acetyl neuraminic acid) utilization by Bacteroides fragilis requires a novel N-acetyl mannosamine epimerase. J. Bacteriol., 191, 3629-3638.
    • (2009) J. Bacteriol , vol.191 , pp. 3629-3638
    • Brigham, C.1    Caughlan, R.2    Gallegos, R.3    Dallas, M.B.4    Godoy, V.G.5    Malamy, M.H.6
  • 44
    • 84976878698 scopus 로고    scopus 로고
    • Twenty years of the MEROPS database of proteolytic enzymes, their substrates and inhibitors
    • Rawlings, N.D., Barrett, A.J., Finn, R. (2016) Twenty years of the MEROPS database of proteolytic enzymes, their substrates and inhibitors. Nucleic Acids Res., 44, D343-D350.
    • (2016) Nucleic Acids Res , vol.44 , pp. D343-D350
    • Rawlings, N.D.1    Barrett, A.J.2    Finn, R.3
  • 46
    • 84892694478 scopus 로고    scopus 로고
    • Rapid similarity search of proteins using alignments of domain arrangements
    • Terrapon, N., Weiner, J., Grath, S., Moore, A.D., Bornberg-Bauer, E. (2014) Rapid similarity search of proteins using alignments of domain arrangements. Bioinformatics, 30, 274-281.
    • (2014) Bioinformatics , vol.30 , pp. 274-281
    • Terrapon, N.1    Weiner, J.2    Grath, S.3    Moore, A.D.4    Bornberg-Bauer, E.5
  • 47
    • 0014757386 scopus 로고
    • A general method applicable to the search for similarities in the amino acid sequence of two proteins
    • Needleman, S.B., Wunsch, C.D. (1970) A general method applicable to the search for similarities in the amino acid sequence of two proteins. J. Mol. Biol., 48, 443-453.
    • (1970) J. Mol. Biol , vol.48 , pp. 443-453
    • Needleman, S.B.1    Wunsch, C.D.2


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