메뉴 건너뛰기




Volumn 76, Issue 6, 2007, Pages 1319-1327

Biochemical characterization and phylogenetic analysis of UDP-glucose dehydrogenase from the gellan gum producer Sphingomonas elodea ATCC 31461

Author keywords

Gelling agents; Gellun gum; Sphingomonas elodea; UDP glucosedehydrogenase; ugdG gene

Indexed keywords

CLONING; DNA SEQUENCES; ENZYME ACTIVITY; ESCHERICHIA COLI; GLUCOSE; PH EFFECTS;

EID: 34648816177     PISSN: 01757598     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00253-007-1112-8     Document Type: Article
Times cited : (20)

References (35)
  • 1
    • 3142667508 scopus 로고    scopus 로고
    • Biosynthesis of UDP-GlcA, a key metabolite for capsular polysaccharide synthesis in the pathogenic fungus Cryptococcus neoformans
    • Bar-Peled M, Griffith CL, Ory JJ, Doering TL (2004) Biosynthesis of UDP-GlcA, a key metabolite for capsular polysaccharide synthesis in the pathogenic fungus Cryptococcus neoformans. Biochem J 381:131-136
    • (2004) Biochem J , vol.381 , pp. 131-136
    • Bar-Peled, M.1    Griffith, C.L.2    Ory, J.J.3    Doering, T.L.4
  • 2
    • 0036707995 scopus 로고    scopus 로고
    • A structurally conserved water molecule in Rossmann dinucleotide-binding domains
    • Bottoms CA, Smith PE, Tanner JJ (2002) A structurally conserved water molecule in Rossmann dinucleotide-binding domains. Protein Sci 11:2125-2137
    • (2002) Protein Sci , vol.11 , pp. 2125-2137
    • Bottoms, C.A.1    Smith, P.E.2    Tanner, J.J.3
  • 3
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM (1976) A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248-254
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 4
    • 0031013279 scopus 로고    scopus 로고
    • Properties and kinetics analysis of UDP-glucose dehydrogenase from group a streptococci. Irreversible inhibition by UDP-chloroacetol
    • Campbell RE, Sala RF, van de Rijn I, Tanner ME (1997) Properties and kinetics analysis of UDP-glucose dehydrogenase from group A streptococci. Irreversible inhibition by UDP-chloroacetol. J Biol Chem 272:3416-3422
    • (1997) J Biol Chem , vol.272 , pp. 3416-3422
    • Campbell, R.E.1    Sala, R.F.2    Van De Rijn, I.3    Tanner, M.E.4
  • 5
    • 0034643813 scopus 로고    scopus 로고
    • The first structure of UDP-glucose dehydrogenase reveals the catalytic residues necessary for the two-fold oxidation
    • Campbell RE, Mosimann SC, van de Rijn I, Tanner ME, Strynadka CJ (2000) The first structure of UDP-glucose dehydrogenase reveals the catalytic residues necessary for the two-fold oxidation. Biochemistry 39:7012-7023
    • (2000) Biochemistry , vol.39 , pp. 7012-7023
    • Campbell, R.E.1    Mosimann, S.C.2    Van De Rijn, I.3    Tanner, M.E.4    Strynadka, C.J.5
  • 6
    • 0000461280 scopus 로고
    • Confidence limits on phylogenies: An approach using the bootstrap
    • Felsenstein J (1985) Confidence limits on phylogenies: an approach using the bootstrap. Evolution 39:783-791
    • (1985) Evolution , vol.39 , pp. 783-791
    • Felsenstein, J.1
  • 7
    • 0032978642 scopus 로고    scopus 로고
    • Structures and properties of gellan polymers produced by Sphingomonas paucimobilis ATCC 31461 from lactose compared with those produced from glucose and from cheese whey
    • Fialho AM, Martins LO, Donval ML, Leitão JH, Ridout MJ, Jay AJ, Morris VJ, Sá-Correia I (1999) Structures and properties of gellan polymers produced by Sphingomonas paucimobilis ATCC 31461 from lactose compared with those produced from glucose and from cheese whey. Appl Environ Microbiol 65:2485-2491
    • (1999) Appl Environ Microbiol , vol.65 , pp. 2485-2491
    • Fialho, A.M.1    Martins, L.O.2    Donval, M.L.3    Leitão, J.H.4    Ridout, M.J.5    Jay, A.J.6    Morris, V.J.7    Sá-Correia, I.8
  • 8
    • 0022870839 scopus 로고
    • Molecular cloning of the plasmid RP4 primase region in multi-host-range tacP expression vector
    • Fürste JP, Pansegran W, Frank R, Blöcker H, Sholz P, Bagdasarian M, Lanka E (1986) Molecular cloning of the plasmid RP4 primase region in multi-host-range tacP expression vector. Gene 48:119-131
    • (1986) Gene , vol.48 , pp. 119-131
    • Fürste, J.P.1    Pansegran, W.2    Frank, R.3    Blöcker, H.4    Sholz, P.5    Bagdasarian, M.6    Lanka, E.7
  • 9
    • 1642580528 scopus 로고    scopus 로고
    • Active sites residues and mechanism of UDP-glucose dehydrogenase
    • Ge X, Penney LC, van de Rijn I, Tanner ME (2004) Active sites residues and mechanism of UDP-glucose dehydrogenase. Eur J Biochem 271:14-22
    • (2004) Eur J Biochem , vol.271 , pp. 14-22
    • Ge, X.1    Penney, L.C.2    Van De Rijn, I.3    Tanner, M.E.4
  • 10
    • 1842607480 scopus 로고    scopus 로고
    • Organization of genes required for gellan polysaccharide biosynthesis in Sphingomonas elodea ATCC 31461
    • Harding NE, Patel YN, Coleman RJ (2004) Organization of genes required for gellan polysaccharide biosynthesis in Sphingomonas elodea ATCC 31461. J Ind Microbiol Biotechnol 31:70-82
    • (2004) J Ind Microbiol Biotechnol , vol.31 , pp. 70-82
    • Harding, N.E.1    Patel, Y.N.2    Coleman, R.J.3
  • 11
    • 0024234855 scopus 로고
    • CLUSTAL: A package for performing multiple sequence alignment on a microcomputer
    • Higgins DG, Sharp PM (1988) CLUSTAL: a package for performing multiple sequence alignment on a microcomputer. Gene 73:237-244
    • (1988) Gene , vol.73 , pp. 237-244
    • Higgins, D.G.1    Sharp, P.M.2
  • 12
    • 34547096749 scopus 로고    scopus 로고
    • Comparative analysis of two UDP-glucose dehydrogenases in Pseudomonas aeruginosa PAO1
    • (in press). DOI 10.1074/jbc.M701824200
    • Hung RJ, Chien HS, Lin RZ, Lin CT, Vatsyayan J, Peng HL, Chang HY (2007) Comparative analysis of two UDP-glucose dehydrogenases in Pseudomonas aeruginosa PAO1. J Biol Chem (in press). DOI 10.1074/jbc.M701824200
    • (2007) J Biol Chem
    • Hung, R.J.1    Chien, H.S.2    Lin, R.Z.3    Lin, C.T.4    Vatsyayan, J.5    Peng, H.L.6    Chang, H.Y.7
  • 13
    • 14844336384 scopus 로고    scopus 로고
    • The influence of gellan gum on the transfer of fluorescein dextran across rat nasal epithelium in vivo
    • Jansson B, Hagerstrom H, Fransen N, Edsman K, Bjork E (2005) The influence of gellan gum on the transfer of fluorescein dextran across rat nasal epithelium in vivo. Eur J Pharm Biopharm 59:557-564
    • (2005) Eur J Pharm Biopharm , vol.59 , pp. 557-564
    • Jansson, B.1    Hagerstrom, H.2    Fransen, N.3    Edsman, K.4    Bjork, E.5
  • 15
    • 33846631847 scopus 로고    scopus 로고
    • Regulation of Vibrio polysaccharide synthesis and virulence factor production by CdgC, a GGDEF-EAL domain protein, in Vibrio cholerae
    • Lim B, Beyhan S, Yildiz FH (2007) Regulation of Vibrio polysaccharide synthesis and virulence factor production by CdgC, a GGDEF-EAL domain protein, in Vibrio cholerae. J Bacteriol 189:717-729
    • (2007) J Bacteriol , vol.189 , pp. 717-729
    • Lim, B.1    Beyhan, S.2    Yildiz, F.H.3
  • 16
    • 0037363278 scopus 로고    scopus 로고
    • Characterization of the ugpG gene encoding a UDP-glucose pyrophosphorylase from the gellan gum producer Sphingomonas paucimobilis ATCC 31461
    • Marques AR, Ferreira PB, Sá-Correia I, Fialho AM (2003) Characterization of the ugpG gene encoding a UDP-glucose pyrophosphorylase from the gellan gum producer Sphingomonas paucimobilis ATCC 31461. Mol Genet Genomics 268:816-824
    • (2003) Mol Genet Genomics , vol.268 , pp. 816-824
    • Marques, A.R.1    Ferreira, P.B.2    Sá-Correia, I.3    Fialho, A.M.4
  • 17
    • 16344381001 scopus 로고    scopus 로고
    • The gellan gum biosynthetic genes gelC and gelE encode two separate polypeptides homologous to the activator and the kinase domains of tyrosine autokinases
    • Moreira LM, Hoffmann K, Albano H, Becker A, Niehaus K, Sá-Correia I (2004) The gellan gum biosynthetic genes gelC and gelE encode two separate polypeptides homologous to the activator and the kinase domains of tyrosine autokinases. J Mol Microbiol Biotechnol l8:43-57
    • (2004) J Mol Microbiol Biotechnol , vol.8 , pp. 43-57
    • Moreira, L.M.1    Hoffmann, K.2    Albano, H.3    Becker, A.4    Niehaus, K.5    Sá-Correia, I.6
  • 18
    • 77956924601 scopus 로고
    • Mechanism of NAD-dependent enzymes
    • Oppenheimer NJ, Handlon AL (1992) Mechanism of NAD-dependent enzymes. Enzymes 20:453-504
    • (1992) Enzymes , vol.20 , pp. 453-504
    • Oppenheimer, N.J.1    Handlon, A.L.2
  • 19
    • 0016719206 scopus 로고
    • Mechanism of action of uridine diphosphoglucose dehydrogenase. Evidence for a second reversible dehydrogenation step involving essential thiol group
    • Ridley WP, Houchins JP, Kirkwood S (1975) Mechanism of action of uridine diphosphoglucose dehydrogenase. Evidence for a second reversible dehydrogenation step involving essential thiol group. J Biol Chem 250:8761-8767
    • (1975) J Biol Chem , vol.250 , pp. 8761-8767
    • Ridley, W.P.1    Houchins, J.P.2    Kirkwood, S.3
  • 20
    • 0036801506 scopus 로고    scopus 로고
    • Gellan gum biosynthesis in Sphingomonas paucimobilis ATCC 31461: Genes, enzymes and exopolysaccharide production engineering
    • Sá-Correia I, Fialho AM, Videira P, Moreira LM, Marques AR, Albano H (2002) Gellan gum biosynthesis in Sphingomonas paucimobilis ATCC 31461: genes, enzymes and exopolysaccharide production engineering. J Ind Microbiol Biotechnol 29:170-176
    • (2002) J Ind Microbiol Biotechnol , vol.29 , pp. 170-176
    • Sá-Correia, I.1    Fialho, A.M.2    Videira, P.3    Moreira, L.M.4    Marques, A.R.5    Albano, H.6
  • 21
    • 0023375195 scopus 로고
    • The neighbor-joining method: A new method for reconstructing phylogenetic trees
    • Saitou N, Nei M (1987) The neighbor-joining method: a new method for reconstructing phylogenetic trees. Mol Biol Evol 4:406-425
    • (1987) Mol Biol Evol , vol.4 , pp. 406-425
    • Saitou, N.1    Nei, M.2
  • 22
    • 34648844741 scopus 로고
    • Partial purification and properties of UDPG dehydrogenase from Escherichia coli
    • Schiller JG, Lamy F, Frazier R, Feingold DS (1973) Partial purification and properties of UDPG dehydrogenase from Escherichia coli. Biochim Biophys Acta 453:418-425
    • (1973) Biochim Biophys Acta , vol.453 , pp. 418-425
    • Schiller, J.G.1    Lamy, F.2    Frazier, R.3    Feingold, D.S.4
  • 23
    • 0031039255 scopus 로고    scopus 로고
    • Expression, inducer spectrum, domain structure, and function of MopR, the regulator of phenol degradation in Acinetobacter calcoaceticus NCIB8250
    • Schirmer F, Ehrt S, Hillen W (1997) Expression, inducer spectrum, domain structure, and function of MopR, the regulator of phenol degradation in Acinetobacter calcoaceticus NCIB8250. J Bacteriol 179:1329-1336
    • (1997) J Bacteriol , vol.179 , pp. 1329-1336
    • Schirmer, F.1    Ehrt, S.2    Hillen, W.3
  • 24
    • 0036205377 scopus 로고    scopus 로고
    • TREE-PUZZLE: Maximum likelihood phylogenetic analysis using quartets and parallel computing
    • Schmidt HA, Strimmer K, Vingron M, von Haeseler A (2002) TREE-PUZZLE: maximum likelihood phylogenetic analysis using quartets and parallel computing. Bioinformatics 18:502-504
    • (2002) Bioinformatics , vol.18 , pp. 502-504
    • Schmidt, H.A.1    Strimmer, K.2    Vingron, M.3    Von Haeseler, A.4
  • 25
    • 23744492608 scopus 로고    scopus 로고
    • Proteins encoded by Sphingomonas elodea ATCC 31461 rmlA and ugpG genes, involved in gellan gum biosynthesis, exhibit both dTDP- and UDP-glucose pyrophosphorylase activities
    • Silva E, Marques AR, Fialho AM, Granja AT, Sá-Correia I (2005) Proteins encoded by Sphingomonas elodea ATCC 31461 rmlA and ugpG genes, involved in gellan gum biosynthesis, exhibit both dTDP- and UDP-glucose pyrophosphorylase activities. Appl Environ Microbiol 71:4703-4712
    • (2005) Appl Environ Microbiol , vol.71 , pp. 4703-4712
    • Silva, E.1    Marques, A.R.2    Fialho, A.M.3    Granja, A.T.4    Sá-Correia, I.5
  • 26
    • 34648849748 scopus 로고    scopus 로고
    • An initial evaluation of gellan gum as a material for tissue engineering applications
    • (in press). DOI 10.1177/0885328207076522
    • Smith AM, Shelton R, Perrie Y, Manis JJ (2007) An initial evaluation of gellan gum as a material for tissue engineering applications. J Biomater Appl (in press). DOI 10.1177/0885328207076522
    • (2007) J Biomater Appl
    • Smith, A.M.1    Shelton, R.2    Perrie, Y.3    Manis, J.J.4
  • 27
    • 0037391289 scopus 로고    scopus 로고
    • Identification of a third sulfate activation system in Sinorhizobium sp. strain BR816: The CysDN sulfate activation complex
    • Snoeck C, Verreth C, Hernandez-Lucas I, Martinez-Romero E, Vanderleyden J (2003) Identification of a third sulfate activation system in Sinorhizobium sp. strain BR816: the CysDN sulfate activation complex. Appl Environ Microbiol 69:2006-2014
    • (2003) Appl Environ Microbiol , vol.69 , pp. 2006-2014
    • Snoeck, C.1    Verreth, C.2    Hernandez-Lucas, I.3    Martinez-Romero, E.4    Vanderleyden, J.5
  • 28
    • 0037472127 scopus 로고    scopus 로고
    • Crystal structure of GDP-mannose dehydrogenase: A key enzyme of alginate biosynthesis in P. aeruginosa
    • Snook CF, Tipton PA, Beamer LJ (2003) Crystal structure of GDP-mannose dehydrogenase: a key enzyme of alginate biosynthesis in P. aeruginosa. Biochemistry 42:4658-4668
    • (2003) Biochemistry , vol.42 , pp. 4658-4668
    • Snook, C.F.1    Tipton, P.A.2    Beamer, L.J.3
  • 29
    • 33645284156 scopus 로고    scopus 로고
    • Ion-activated, gelrite-based in situ ophthalmic gels of pefloxacin mesylate: Comparison with conventional eye drops
    • Sultana Y, Aqil M, Ali A (2006) Ion-activated, gelrite-based in situ ophthalmic gels of pefloxacin mesylate: comparison with conventional eye drops. Drug Deliv 13:215-219
    • (2006) Drug Deliv , vol.13 , pp. 215-219
    • Sultana, Y.1    Aqil, M.2    Ali, A.3
  • 30
    • 33845417500 scopus 로고    scopus 로고
    • Mesorhizobium loti produces nodPQ-dependent sulfated cell surface polysaccharides
    • Townsend GE, Forsberg LS, Keating DH (2006) Mesorhizobium loti produces nodPQ-dependent sulfated cell surface polysaccharides. J Bacteriol 188:8560-8672
    • (2006) J Bacteriol , vol.188 , pp. 8560-8672
    • Townsend, G.E.1    Forsberg, L.S.2    Keating, D.H.3
  • 31
    • 0034016761 scopus 로고    scopus 로고
    • Identification of the pgmG gene, encoding a bifuncional protein with phosphoglucomutase and phosphomannomutase activities, in the gellan gum-producing strain Sphingomonas paucimobilis ATCC 31461
    • Videira PA, Cortes LL, Fialho AM, Sá-Correia I (2000) Identification of the pgmG gene, encoding a bifuncional protein with phosphoglucomutase and phosphomannomutase activities, in the gellan gum-producing strain Sphingomonas paucimobilis ATCC 31461. Appl Environ Microbiol 66:2252-2258
    • (2000) Appl Environ Microbiol , vol.66 , pp. 2252-2258
    • Videira, P.A.1    Cortes, L.L.2    Fialho, A.M.3    Sá-Correia, I.4
  • 32
    • 0035446965 scopus 로고    scopus 로고
    • Biochemical characterization of the β-1,4-glucuronosyltransferase GelK in gellan gum producing strain Sphingomonas paucimobilis ATCC 31461
    • Videira PA, Fialho AM, Geremia RA, Breton C, Sá-Correia I (2001) Biochemical characterization of the β-1,4-glucuronosyltransferase GelK in gellan gum producing strain Sphingomonas paucimobilis ATCC 31461. Biochem J 358:457-464
    • (2001) Biochem J , vol.358 , pp. 457-464
    • Videira, P.A.1    Fialho, A.M.2    Geremia, R.A.3    Breton, C.4    Sá-Correia, I.5
  • 33
    • 0037381267 scopus 로고    scopus 로고
    • Isolation and sequencing of glycosyltransferase gene and UDP-glucose dehydrogenase gene that are located on a gene cluster involved in a new exopolysaccharide biosynthesis in Streptomyces
    • Wang L, Li S, Li Y (2003) Isolation and sequencing of glycosyltransferase gene and UDP-glucose dehydrogenase gene that are located on a gene cluster involved in a new exopolysaccharide biosynthesis in Streptomyces. DNA Seq 14:141-145
    • (2003) DNA Seq , vol.14 , pp. 141-145
    • Wang, L.1    Li, S.2    Li, Y.3
  • 34
    • 34247574796 scopus 로고    scopus 로고
    • Mutations blocking side chain assembly, polymerization, or transport of a Wzy-dependent Streptococcus pneumoniae capsule are lethal in the absence of suppressor mutations and can affect polymer transfer to the cell wall
    • Xayarath B, Yother J (2007) Mutations blocking side chain assembly, polymerization, or transport of a Wzy-dependent Streptococcus pneumoniae capsule are lethal in the absence of suppressor mutations and can affect polymer transfer to the cell wall. J Bacteriol 189:3369-3381
    • (2007) J Bacteriol , vol.189 , pp. 3369-3381
    • Xayarath, B.1    Yother, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.