메뉴 건너뛰기




Volumn 193, Issue 19, 2011, Pages 5252-5259

UDP-glucuronic acid decarboxylases of Bacteroides fragilis and their prevalence in bacteria

Author keywords

[No Author keywords available]

Indexed keywords

GLUCURONIC ACID; POLYSACCHARIDE; URIDINE DIPHOSPHATE; XYLOSE;

EID: 80053614489     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.05337-11     Document Type: Article
Times cited : (19)

References (44)
  • 1
    • 17844392864 scopus 로고    scopus 로고
    • Combining prediction of secondary structure and solvent accessibility in proteins
    • Adamczak, R., A. Porollo, and J. Meller. 2005. Combining prediction of secondary structure and solvent accessibility in proteins. Proteins 59:467-475.
    • (2005) Proteins , vol.59 , pp. 467-475
    • Adamczak, R.1    Porollo, A.2    Meller, J.3
  • 2
    • 0036151285 scopus 로고    scopus 로고
    • Toward a structural understanding of the dehydratase mechanism
    • Allard, S. T., et al. 2002. Toward a structural understanding of the dehydratase mechanism. Structure 10:81-92.
    • (2002) Structure , vol.10 , pp. 81-92
    • Allard, S.T.1
  • 4
    • 0030801002 scopus 로고    scopus 로고
    • Gapped BLAST and PSI-BLAST: a new generation of protein database search programs
    • Altschul, S. F., et al. 1997. Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res. 25:3389-3402.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 3389-3402
    • Altschul, S.F.1
  • 5
    • 0013874808 scopus 로고
    • Biosynthesis of UDP D-xylose. II. UDP D-glucuronate carboxy-lyase of Cryptococcus laurentii
    • Ankel, H., and D. S. Feingold. 1966. Biosynthesis of UDP D-xylose. II. UDP D-glucuronate carboxy-lyase of Cryptococcus laurentii. Biochemistry 5:182- 189.
    • (1966) Biochemistry , vol.5 , pp. 182-189
    • Ankel, H.1    Feingold, D.S.2
  • 6
    • 0035834048 scopus 로고    scopus 로고
    • Functional cloning and characterization of a UDP-glucuronic acid decarboxylase: the pathogenic fungus Cryptococcus neoformans elucidates UDP-xylose synthesis
    • Bar-Peled, M., C. L. Griffith, and T. L. Doering. 2001. Functional cloning and characterization of a UDP-glucuronic acid decarboxylase: the pathogenic fungus Cryptococcus neoformans elucidates UDP-xylose synthesis. Proc. Natl. Acad. Sci. U. S. A. 98:12003-12008.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 12003-12008
    • Bar-Peled, M.1    Griffith, C.L.2    Doering, T.L.3
  • 7
    • 0037169485 scopus 로고    scopus 로고
    • Oxidative decarboxylation of UDP-glucuronic acid in extracts of polymyxin-resistant Escherichia coli. Origin of lipid A species modified with 4-amino-4-deoxy-L-arabinose
    • Breazeale, S. D., A. A. Ribeiro, and C. R. Raetz. 2002. Oxidative decarboxylation of UDP-glucuronic acid in extracts of polymyxin-resistant Escherichia coli. Origin of lipid A species modified with 4-amino-4-deoxy-L-arabinose. J. Biol. Chem. 277:2886-2896.
    • (2002) J. Biol. Chem. , vol.277 , pp. 2886-2896
    • Breazeale, S.D.1    Ribeiro, A.A.2    Raetz, C.R.3
  • 8
    • 0037329646 scopus 로고    scopus 로고
    • The biosynthesis of L-arabinose in plants: molecular cloning and characterization of a Golgi-localized UDP-D-xylose 4-epimerase encoded by the MUR4 gene of Arabidopsis
    • Burget, E. G., R. Verma, M. Molhoj, and W. D. Reiter. 2003. The biosynthesis of L-arabinose in plants: molecular cloning and characterization of a Golgi-localized UDP-D-xylose 4-epimerase encoded by the MUR4 gene of Arabidopsis. Plant Cell 15:523-531.
    • (2003) Plant Cell , vol.15 , pp. 523-531
    • Burget, E.G.1    Verma, R.2    Molhoj, M.3    Reiter, W.D.4
  • 9
    • 0029833779 scopus 로고    scopus 로고
    • Molecular characterization of the Pseudomonas aeruginosa serotype O5 (PAO1) B-band lipopolysaccharide gene cluster
    • Burrows, L. L., D. F. Charter, and J. S. Lam. 1996. Molecular characterization of the Pseudomonas aeruginosa serotype O5 (PAO1) B-band lipopolysaccharide gene cluster. Mol. Microbiol. 22:481-495.
    • (1996) Mol. Microbiol. , vol.22 , pp. 481-495
    • Burrows, L.L.1    Charter, D.F.2    Lam, J.S.3
  • 10
    • 33645086858 scopus 로고    scopus 로고
    • Structures of the core oligosaccharide and O-units in the R- and SR-type lipopolysaccharides of reference strains of Pseudomonas aeruginosa O-serogroups
    • Bystrova, O. V., et al. 2006. Structures of the core oligosaccharide and O-units in the R- and SR-type lipopolysaccharides of reference strains of Pseudomonas aeruginosa O-serogroups. FEMS Immunol. Med. Microbiol. 46:85-99.
    • (2006) FEMS Immunol. Med. Microbiol. , vol.46 , pp. 85-99
    • Bystrova, O.V.1
  • 11
    • 38649103144 scopus 로고    scopus 로고
    • Expression of a uniquely regulated extracellular polysaccharide confers a large-capsule phenotype to Bacteroides fragilis
    • Chatzidaki-Livanis, M., M. J. Coyne, H. Roche-Hakansson, and L. E. Comstock. 2008. Expression of a uniquely regulated extracellular polysaccharide confers a large-capsule phenotype to Bacteroides fragilis. J. Bacteriol. 190: 1020-1026.
    • (2008) J. Bacteriol , vol.190 , pp. 1020-1026
    • Chatzidaki-Livanis, M.1    Coyne, M.J.2    Roche-Hakansson, H.3    Comstock, L.E.4
  • 12
    • 51349110626 scopus 로고    scopus 로고
    • Role of glycan synthesis in colonization of the mammalian gut by the bacterial symbiont Bacteroides fragilis
    • Coyne, M. J., M. Chatzidaki-Livanis, L. C. Paoletti, and L. E. Comstock. 2008. Role of glycan synthesis in colonization of the mammalian gut by the bacterial symbiont Bacteroides fragilis. Proc. Natl. Acad. Sci. U. S. A. 105: 13099-13104.
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 13099-13104
    • Coyne, M.J.1    Chatzidaki-Livanis, M.2    Paoletti, L.C.3    Comstock, L.E.4
  • 13
    • 15244340417 scopus 로고    scopus 로고
    • Human symbionts use a host-like pathway for surface fucosylation
    • Coyne, M. J., B. Reinap, M. M. Lee, and L. E. Comstock. 2005. Human symbionts use a host-like pathway for surface fucosylation. Science 307: 1778-1781.
    • (2005) Science , vol.307 , pp. 1778-1781
    • Coyne, M.J.1    Reinap, B.2    Lee, M.M.3    Comstock, L.E.4
  • 14
    • 0037067783 scopus 로고    scopus 로고
    • Critical residues for structure and catalysis in shortchain dehydrogenases/reductases
    • Filling, C., et al. 2002. Critical residues for structure and catalysis in shortchain dehydrogenases/reductases. J. Biol. Chem. 277:25677-25684.
    • (2002) J. Biol. Chem. , vol.277 , pp. 25677-25684
    • Filling, C.1
  • 15
    • 33847779192 scopus 로고    scopus 로고
    • Phase-variable expression of a family of glycoproteins imparts a dynamic surface to a symbiont in its human intestinal ecosystem
    • Fletcher, C. M., M. J. Coyne, D. L. Bentley, O. F. Villa, and L. E. Comstock. 2007. Phase-variable expression of a family of glycoproteins imparts a dynamic surface to a symbiont in its human intestinal ecosystem. Proc. Natl. Acad. Sci. U. S. A. 104:2413-2418.
    • (2007) Proc. Natl. Acad. Sci. U. S. A , vol.104 , pp. 2413-2418
    • Fletcher, C.M.1    Coyne, M.J.2    Bentley, D.L.3    Villa, O.F.4    Comstock, L.E.5
  • 16
    • 79952797070 scopus 로고    scopus 로고
    • Theoretical and experimental characterization of the scope of protein O-glycosylation in Bacteroides fragilis
    • Fletcher, C. M., M. J. Coyne, and L. E. Comstock. 2011. Theoretical and experimental characterization of the scope of protein O-glycosylation in Bacteroides fragilis. J. Biol. Chem. 286:3219-3226.
    • (2011) J. Biol. Chem. , vol.286 , pp. 3219-3226
    • Fletcher, C.M.1    Coyne, M.J.2    Comstock, L.E.3
  • 17
    • 64249095086 scopus 로고    scopus 로고
    • A general O-glycosylation system important to the physiology of a major human intestinal symbiont
    • Fletcher, C. M., M. J. Coyne, O. F. Villa, M. Chatzidaki-Livanis, and L. E. Comstock. 2009. A general O-glycosylation system important to the physiology of a major human intestinal symbiont. Cell 137:321-331.
    • (2009) Cell , vol.137 , pp. 321-331
    • Fletcher, C.M.1    Coyne, M.J.2    Villa, O.F.3    Chatzidaki-Livanis, M.4    Comstock, L.E.5
  • 19
    • 77950571350 scopus 로고    scopus 로고
    • Identification of a bifunctional UDP-4-keto-pentose/UDP-xylose synthase in the plant pathogenic bacterium Ralstonia solanacearum strain GMI1000, a distinct member of the 4 6-dehydratase and decarboxylase family
    • Gu, X., et al. 2010. Identification of a bifunctional UDP-4-keto-pentose/UDP-xylose synthase in the plant pathogenic bacterium Ralstonia solanacearum strain GMI1000, a distinct member of the 4,6-dehydratase and decarboxylase family. J. Biol. Chem. 285:9030-9040.
    • (2010) J. Biol. Chem , vol.285 , pp. 9030-9040
    • Gu, X.1
  • 20
    • 78650752821 scopus 로고    scopus 로고
    • Biosynthesis of UDP-xylose and UDP-arabinose in Sinorhizobium meliloti first 1021 characterization of a bacterial UDP-xylose synthase, and UDP-xylose 4-epimerase
    • Gu, X., S. G. Lee, and M. Bar-Peled. 2011. Biosynthesis of UDP-xylose and UDP-arabinose in Sinorhizobium meliloti 1021: first characterization of a bacterial UDP-xylose synthase, and UDP-xylose 4-epimerase. Microbiology 157:260-269.
    • (2011) Microbiology , vol.157 , pp. 260-269
    • Gu, X.1    Lee, S.G.2    Bar-Peled, M.3
  • 21
    • 65649152950 scopus 로고    scopus 로고
    • Real-time NMR monitoring of intermediates and labile products of the bifunctional enzyme UDP-apiose/UDP-xylose synthase
    • Guyett, P., J. Glushka, X. Gu, and M. Bar-Peled. 2009. Real-time NMR monitoring of intermediates and labile products of the bifunctional enzyme UDP-apiose/UDP-xylose synthase. Carbohydr. Res. 344:1072-1078.
    • (2009) Carbohydr. Res. , vol.344 , pp. 1072-1078
    • Guyett, P.1    Glushka, J.2    Gu, X.3    Bar-Peled, M.4
  • 22
    • 0036918914 scopus 로고    scopus 로고
    • Biosynthesis of UDP-xylose. Cloning and characterization of a novel Arabidopsis gene family, UXS, encoding soluble and putative membrane-bound UDP-glucuronic acid decarboxylase isoforms
    • Harper, A. D., and M. Bar-Peled. 2002. Biosynthesis of UDP-xylose. Cloning and characterization of a novel Arabidopsis gene family, UXS, encoding soluble and putative membrane-bound UDP-glucuronic acid decarboxylase isoforms. Plant Physiol. 130:2188-2198.
    • (2002) Plant Physiol. , vol.130 , pp. 2188-2198
    • Harper, A.D.1    Bar-Peled, M.2
  • 24
    • 58149133711 scopus 로고    scopus 로고
    • The SDR superfamily: functional and structural diversity within a family of metabolic and regulatory enzymes
    • Kavanagh, K. L., H. Jornvall, B. Persson, and U. Oppermann. 2008. The SDR superfamily: functional and structural diversity within a family of metabolic and regulatory enzymes. Cell. Mol. Life Sci. 65:3895-3906.
    • (2008) Cell. Mol. Life Sci. , vol.65 , pp. 3895-3906
    • Kavanagh, K.L.1    Jornvall, H.2    Persson, B.3    Oppermann, U.4
  • 25
    • 0025078706 scopus 로고
    • Polysaccharide antigens of Pseudomonas aeruginosa
    • Knirel, Y. A. 1990. Polysaccharide antigens of Pseudomonas aeruginosa. Crit. Rev. Microbiol. 17:273-304.
    • (1990) Crit. Rev. Microbiol. , vol.17 , pp. 273-304
    • Knirel, Y.A.1
  • 26
    • 0016904277 scopus 로고
    • Comparative aspects of glycoprotein structure
    • Kornfeld, R., and S. Kornfeld. 1976. Comparative aspects of glycoprotein structure. Annu. Rev. Biochem. 45:217-237.
    • (1976) Annu. Rev. Biochem. , vol.45 , pp. 217-237
    • Kornfeld, R.1    Kornfeld, S.2
  • 27
    • 0035969489 scopus 로고    scopus 로고
    • Extensive surface diversity of a commensal microorganism by multiple DNA inversions
    • Krinos, C. M., et al. 2001. Extensive surface diversity of a commensal microorganism by multiple DNA inversions. Nature 414:555-558.
    • (2001) Nature , vol.414 , pp. 555-558
    • Krinos, C.M.1
  • 28
    • 36448991500 scopus 로고    scopus 로고
    • Clustal W and Clustal X version 2 0
    • Larkin, M. A., et al. 2007. Clustal W and Clustal X version 2.0. Bioinformatics 23:2947-2948.
    • (2007) Bioinformatics , vol.23 , pp. 2947-2948
    • Larkin, M.A.1
  • 29
    • 0029562477 scopus 로고
    • NAD- binding domains of dehydrogenases
    • Lesk, A. M. 1995. NAD-binding domains of dehydrogenases. Curr. Opin. Struct. Biol. 5:775-783.
    • (1995) Curr. Opin. Struct. Biol. , vol.5 , pp. 775-783
    • Lesk, A.M.1
  • 30
    • 44449106055 scopus 로고    scopus 로고
    • A microbial symbiosis factor prevents intestinal inflammatory disease
    • Mazmanian, S. K., J. L. Round, and D. L. Kasper. 2008. A microbial symbiosis factor prevents intestinal inflammatory disease. Nature 453:620- 625.
    • (2008) Nature , vol.453 , pp. 620-625
    • Mazmanian, S.K.1    Round, J.L.2    Kasper, D.L.3
  • 31
    • 0037053343 scopus 로고    scopus 로고
    • UDP- glucuronate decarboxylase, a key enzyme in proteoglycan synthesis: cloning, characterization, and localization
    • Moriarity, J. L., et al. 2002. UDP-glucuronate decarboxylase, a key enzyme in proteoglycan synthesis: cloning, characterization, and localization. J. Biol. Chem. 277:16968-16975.
    • (2002) J. Biol. Chem. , vol.277 , pp. 16968-16975
    • Moriarity, J.L.1
  • 32
    • 0025891060 scopus 로고
    • Immunochemical characterization of two surface polysaccharides of Bacteroides fragilis
    • Pantosti, A., A. O. Tzianabos, A. B. Onderdonk, and D. L. Kasper. 1991. Immunochemical characterization of two surface polysaccharides of Bacteroides fragilis. Infect. Immun. 59:2075-2082.
    • (1991) Infect. Immun , vol.59 , pp. 2075-2082
    • Pantosti, A.1    Tzianabos, A.O.2    Onderdonk, A.B.3    Kasper, D.L.4
  • 33
    • 0022167021 scopus 로고
    • Characterization of protein and mannan polysaccharide antigens of yeasts, moulds, and actinomycetes
    • Reiss, E., M. Huppert, and R. Cherniak. 1985. Characterization of protein and mannan polysaccharide antigens of yeasts, moulds, and actinomycetes. Curr. Top. Med. Mycol. 1:172-207.
    • (1985) Curr. Top. Med. Mycol. , vol.1 , pp. 172-207
    • Reiss, E.1    Huppert, M.2    Cherniak, R.3
  • 34
    • 78651345652 scopus 로고    scopus 로고
    • The RCSB Protein Data Bank: redesigned web site and web services
    • Rose, P. W., et al. 2011. The RCSB Protein Data Bank: redesigned web site and web services. Nucleic Acids Res. 39:D392-D401.
    • (2011) Nucleic Acids Res. , vol.39
    • Rose, P.W.1
  • 35
    • 0023243453 scopus 로고
    • Chemical properties of lipopolysaccharide-like substance (LLS) extracted from Leptospira interrogans serovar canicola strain Moulton
    • Shimizu, T., et al. 1987. Chemical properties of lipopolysaccharide-like substance (LLS) extracted from Leptospira interrogans serovar canicola strain Moulton. Microbiol. Immunol. 31:717-725.
    • (1987) Microbiol. Immunol. , vol.31 , pp. 717-725
    • Shimizu, T.1
  • 36
    • 15544376418 scopus 로고    scopus 로고
    • Glycan foraging in vivo by an intestineadapted bacterial symbiont
    • Sonnenburg, J. L., et al. 2005. Glycan foraging in vivo by an intestineadapted bacterial symbiont. Science 307:1955-1959.
    • (2005) Science , vol.307 , pp. 1955-1959
    • Sonnenburg, J.L.1
  • 37
    • 0023042283 scopus 로고
    • Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes
    • Studier, F. W., and B. A. Moffatt. 1986. Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes. J. Mol. Biol. 189:113-130.
    • (1986) J. Mol. Biol. , vol.189 , pp. 113-130
    • Studier, F.W.1    Moffatt, B.A.2
  • 38
    • 0037178867 scopus 로고    scopus 로고
    • Structural analysis of the Y299C mutant of Escherichia coli UDPgalactose 4-epimerase Teaching an old dog new tricks
    • Thoden, J. B., J. M. Henderson, J. L. Fridovich-Keil, and H. M. Holden. 2002. Structural analysis of the Y299C mutant of Escherichia coli UDPgalactose 4-epimerase. Teaching an old dog new tricks. J. Biol. Chem. 277: 27528-27534.
    • (2002) J. Biol. Chem. , vol.277 , pp. 27528-27534
    • Thoden, J.B.1    Henderson, J.M.2    Fridovich-Keil, J.L.3    Holden, H.M.4
  • 39
    • 0025305139 scopus 로고
    • Sequencing the gene for an imipenem-cefoxitin-hydrolyzing enzyme (CfiA) from Bacteroides fragilis TAL2480 reveals strong similarity between CfiA and Bacillus cereus betalactamase II
    • Thompson, J. S., and M. H. Malamy. 1990. Sequencing the gene for an imipenem-cefoxitin-hydrolyzing enzyme (CfiA) from Bacteroides fragilis TAL2480 reveals strong similarity between CfiA and Bacillus cereus betalactamase II. J. Bacteriol. 172:2584-2593.
    • (1990) J. Bacteriol. , vol.172 , pp. 2584-2593
    • Thompson, J.S.1    Malamy, M.H.2
  • 40
    • 0027366918 scopus 로고
    • Structural features of polysaccharides that induce intraabdominal abscesses
    • Tzianabos, A. O., A. B. Onderdonk, B. Rosner, R. L. Cisneros, and D. L. Kasper. 1993. Structural features of polysaccharides that induce intraabdominal abscesses. Science 262:416-419.
    • (1993) Science , vol.262 , pp. 416-419
    • Tzianabos, A.O.1    Onderdonk, A.B.2    Rosner, B.3    Cisneros, R.L.4    Kasper, D.L.5
  • 41
    • 20744455042 scopus 로고    scopus 로고
    • Structure and function of both domains of ArnA, a dual function decarboxylase and a formyltransferase, involved in 4-amino-4-deoxy-L-arabinose biosynthesis
    • Williams, G. J., S. D. Breazeale, C. R. Raetz, and J. H. Naismith. 2005. Structure and function of both domains of ArnA, a dual function decarboxylase and a formyltransferase, involved in 4-amino-4-deoxy-L-arabinose biosynthesis. J. Biol. Chem. 280:23000--23008.
    • (2005) J. Biol. Chem. , vol.280 , pp. 23000-23008
    • Williams, G.J.1    Breazeale, S.D.2    Raetz, C.R.3    Naismith, J.H.4
  • 42
    • 0037470975 scopus 로고    scopus 로고
    • A genomic view of the human-Bacteroides thetaiotaomicron symbiosis
    • Xu, J., et al. 2003. A genomic view of the human-Bacteroides thetaiotaomicron symbiosis. Science 299:2074-2076.
    • (2003) Science , vol.299 , pp. 2074-2076
    • Xu, J.1
  • 43
    • 43849087208 scopus 로고    scopus 로고
    • Biochemical control of xylan biosynthesis- which end is up?
    • York, W. S., and M. A. O'Neill. 2008. Biochemical control of xylan biosynthesis- which end is up? Curr. Opin. Plant Biol. 11:258-265.
    • (2008) Curr Opin. Plant Biol. , vol.11 , pp. 258-265
    • York, W.S.1    O'Neill, M.A.2
  • 44
    • 79955603120 scopus 로고    scopus 로고
    • Longitudinal analysis of the prevalence, maintenance, and IgA response to species of the order Bacteroidales in the human gut
    • Zitomersky, N., M. J. Coyne, and L. E. Comstock. 2011. Longitudinal analysis of the prevalence, maintenance, and IgA response to species of the order Bacteroidales in the human gut. Infect. Immun. 79:2012-2020.
    • (2011) Infect. Immun. , vol.79 , pp. 2012-2020
    • Zitomersky, N.1    Coyne, M.J.2    Comstock, L.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.