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Volumn 67, Issue 3-12, 2001, Pages 5197-5203

Purification and Properties of a Glucuronan Lyase from Sinorhizobium meliloti M5N1CS (NCIMB 40472)

Author keywords

[No Author keywords available]

Indexed keywords

SINORHIZOBIUM MELILOTI;

EID: 0035515303     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/aem.67.11.5197-5203.2001     Document Type: Article
Times cited : (24)

References (45)
  • 1
    • 2242469285 scopus 로고
    • Preparative scale depolymerisation of capsular polysaccharide from E. coli K28 using bacteriophage 28-1
    • Altman, E., G. G. S. Dutton, and A. M. Stephen. 1986. Preparative scale depolymerisation of capsular polysaccharide from E. coli K28 using bacteriophage 28-1. S. Afr. J. Sci. 82:45-46.
    • (1986) S. Afr. J. Sci. , vol.82 , pp. 45-46
    • Altman, E.1    Dutton, G.G.S.2    Stephen, A.M.3
  • 2
    • 0016231913 scopus 로고
    • R factor transfer ir. Rhizobium leguminosarum
    • Beringer, J. E. 1974. R factor transfer ir. Rhizobium leguminosarum. J. Gen. Microbiol. 84:188-198.
    • (1974) J. Gen. Microbiol. , vol.84 , pp. 188-198
    • Beringer, J.E.1
  • 3
    • 0026413086 scopus 로고
    • I -Guluronan-specific alginate lyase from a marine bacterium associated with Sargassum
    • Brown, B. J., and J. K. Preston. 1991. I -Guluronan-specific alginate lyase from a marine bacterium associated with Sargassum. Carhohydr. Res. 211: 91-102.
    • (1991) Carhohydr. Res. , vol.211 , pp. 91-102
    • Brown, B.J.1    Preston, J.K.2
  • 4
    • 0034123367 scopus 로고    scopus 로고
    • Cloning, expression, and purification of the K5 capsular pulysaccharide lyase (KflA) from coliphage K5A: Evidence for two distinct K5 lyase enzymes
    • Clarke, B. R., F. Esumeh, and I. S. Roberts. 2000. Cloning, expression, and purification of the K5 capsular pulysaccharide lyase (KflA) from coliphage K5A: evidence for two distinct K5 lyase enzymes. J. Bacteriol. 182:3761-3766.
    • (2000) J. Bacteriol. , vol.182 , pp. 3761-3766
    • Clarke, B.R.1    Esumeh, F.2    Roberts, I.S.3
  • 5
    • 0020527462 scopus 로고
    • Mise en evidence d'une propriété métabolique de Rhizobium meliloti utilisable pour sa classification
    • Courtois, B., J. P. Hornez, J. Courtois, and J. C. Derieux. 1983. Mise en evidence d'une propriété métabolique de Rhizobium meliloti utilisable pour sa classification. Ann. Microbiol. 134:141-147.
    • (1983) Ann. Microbiol. , vol.134 , pp. 141-147
    • Courtois, B.1    Hornez, J.P.2    Courtois, J.3    Derieux, J.C.4
  • 8
    • 0028712914 scopus 로고
    • Exopolysaccharide production by the Rhizobum meliton M5NICS strain. Location and quantification of the sites of O-acetylation
    • Courtois, J., J. P. Seguin, C. Roblot, A. Heyraud, C. Gey, L. Dantas, J. N. Barbotia, and B. Courtois. 1994. Exopolysaccharide production by the Rhizobum meliton M5NICS strain. Location and quantification of the sites of O-acetylation. Carhohydr. Polym. 25:7-12.
    • (1994) Carhohydr. Polym. , vol.25 , pp. 7-12
    • Courtois, J.1    Seguin, J.P.2    Roblot, C.3    Heyraud, A.4    Gey, C.5    Dantas, L.6    Barbotia, J.N.7    Courtois, B.8
  • 9
    • 0028665496 scopus 로고
    • NMR spectroscopic investigation of oligoglucuronates prepared by enzymic hydrolysis of a (1→4)-β-D-glacuronan
    • Dantas, L., J. Courtois, B. Courtois, J. P. Seguin, C. dey, and A. Heyraud. 1994. NMR spectroscopic investigation of oligoglucuronates prepared by enzymic hydrolysis of a (1→4)-β-D-glacuronan. Carbohydr. Res. 265:303-310.
    • (1994) Carbohydr. Res. , vol.265 , pp. 303-310
    • Dantas, L.1    Courtois, J.2    Courtois, B.3    Seguin, J.P.4    Dey, C.5    Heyraud, A.6
  • 10
    • 0014064044 scopus 로고
    • A protein sequenator
    • Edman, P., and G. Begg. 1967. A protein sequenator. Eur. J. Biochem. 1:80-91.
    • (1967) Eur. J. Biochem. , vol.1 , pp. 80-91
    • Edman, P.1    Begg, G.2
  • 11
    • 0031830749 scopus 로고    scopus 로고
    • Biochemical properties and substrate specificities of a recombinantly produced Azotobacter vinelandii alginate lyase
    • Ertesvag, H., F. Erlien, G. Skjak-Braek, B. H. A. Rehm, and S. Valla. 1998. Biochemical properties and substrate specificities of a recombinantly produced Azotobacter vinelandii alginate lyase. J. Bacleriol. 180:3779-3784.
    • (1998) J. Bacleriol. , vol.180 , pp. 3779-3784
    • Ertesvag, H.1    Erlien, F.2    Skjak-Braek, G.3    Rehm, B.H.A.4    Valla, S.5
  • 12
    • 0029946972 scopus 로고    scopus 로고
    • Selection of a succinoglycan deficient Rhuzobium meliloli mutant producing a partially acetylaled (l-4)-β-D-glucuronan: Symbiotic properties analysis
    • Gonzales, M. L., J. Courtois, A. Heyraud, P. Colin-Morel, P. Michaud, J. N. Barbolin, and B. Courtois. 1996. Selection of a succinoglycan deficient Rhuzobium meliloli mutant producing a partially acetylaled (l-4)-β-D-glucuronan: symbiotic properties analysis. Ann. N. Y. Acad. Sci. 782:53-61.
    • (1996) Ann. N. Y. Acad. Sci. , vol.782 , pp. 53-61
    • Gonzales, M.L.1    Courtois, J.2    Heyraud, A.3    Colin-Morel, P.4    Michaud, P.5    Barbolin, J.N.6    Courtois, B.7
  • 13
    • 0034641185 scopus 로고    scopus 로고
    • Production of a glucoglucuronan by a rhizobia strain infecting alfalfa. Structure of the repeating unit
    • Guentas. L., P. Pheulpin, A. Heyraud, C. Gey, B. Courtois, and J. Courtois. 2000. Production of a glucoglucuronan by a rhizobia strain infecting alfalfa. Structure of the repeating unit. Int. J. Biol. Macromol. 27:269-277
    • (2000) Int. J. Biol. Macromol. , vol.27 , pp. 269-277
    • Guentas, L.1    Pheulpin, P.2    Heyraud, A.3    Gey, C.4    Courtois, B.5    Courtois, J.6
  • 15
    • 0031664395 scopus 로고    scopus 로고
    • Xanthan lyase of Bacillus sp. strain GL1 liberates pyruvylated mannose from xanthan side chains
    • Hashimoto, W., H. Miki, N. Tsuchiya, H. Nankai, and K. Murala. 1998. Xanthan lyase of Bacillus sp. strain GL1 liberates pyruvylated mannose from xanthan side chains. Appl. Environ. Microbiol. 64:3765-3768.
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 3765-3768
    • Hashimoto, W.1    Miki, H.2    Tsuchiya, N.3    Nankai, H.4    Murala, K.5
  • 17
    • 0031956869 scopus 로고    scopus 로고
    • Alginate lyase promotes diffusion of aminoglycosides through the extracellular polysaccharide of mucoid Pseudomonas aeruginosa
    • Hatch, R. A., and N. L. Schiller. 1998. Alginate lyase promotes diffusion of aminoglycosides through the extracellular polysaccharide of mucoid Pseudomonas aeruginosa. Antimicrob. Agents Chemother. 42:974-977.
    • (1998) Antimicrob. Agents Chemother. , vol.42 , pp. 974-977
    • Hatch, R.A.1    Schiller, N.L.2
  • 18
    • 0027551659 scopus 로고
    • Structural characterization and Theological properties of an extracellular glucuronan produced by a Rhizobium meliloti M5N1 mutant strain
    • Heyraud, A., J. Courtois, L. Dantas, P. Colin-Morel, and B. Courtois. 1993. Structural characterization and Theological properties of an extracellular glucuronan produced by a Rhizobium meliloti M5N1 mutant strain Carbohydr. Res. 240:71-78.
    • (1993) Carbohydr. Res. , vol.240 , pp. 71-78
    • Heyraud, A.1    Courtois, J.2    Dantas, L.3    Colin-Morel, P.4    Courtois, B.5
  • 19
    • 0029813385 scopus 로고    scopus 로고
    • NMR spectroscopy analysis of oligoguluronates and oligomannuronates prepared by acid or enzymatic hydrolysis of homopolymeric blocks of alginic acid. Application to the determination ol the substrate specificity of Halions tuberculata alginate lyase
    • Heyraud, A., C. Cry, C. Leonard, C. Rochas, S. Girond, and B. Kloareg. 1996. NMR spectroscopy analysis of oligoguluronates and oligomannuronates prepared by acid or enzymatic hydrolysis of homopolymeric blocks of alginic acid. Application to the determination ol the substrate specificity of Halions tuberculata alginate lyase. Carbohydr. Res. 289:11-23
    • (1996) Carbohydr. Res. , vol.289 , pp. 11-23
    • Heyraud, A.1    Cry, C.2    Leonard, C.3    Rochas, C.4    Girond, S.5    Kloareg, B.6
  • 20
    • 0029778944 scopus 로고    scopus 로고
    • Substrate depolymerization pattern of Pseudomonas vindiflava SF-312 pectate lyase
    • Hotchkiss, A. T., Jr., L. G. Revear, and K. B. Hicks. 1996. Substrate depolymerization pattern of Pseudomonas vindiflava SF-312 pectate lyase. Physiol. Mol. Plant Pathol. 48:1-9.
    • (1996) Physiol. Mol. Plant Pathol. , vol.48 , pp. 1-9
    • Hotchkiss Jr., A.T.1    Revear, L.G.2    Hicks, K.B.3
  • 21
    • 0034180742 scopus 로고    scopus 로고
    • Purification of alginate oligosaccharides with root growth-promoting activity toward lettuce
    • Iwasaki, K., and Y. Matsubara. 2000. Purification of alginate oligosaccharides with root growth-promoting activity toward lettuce. Biosci. Biotechnol. Biochem. 64:1067-1070.
    • (2000) Biosci. Biotechnol. Biochem. , vol.64 , pp. 1067-1070
    • Iwasaki, K.1    Matsubara, Y.2
  • 23
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 25
    • 0031589723 scopus 로고    scopus 로고
    • Fine chemical structure analysis of oligosaccharides produced by an ulvan-lyase degradation of the water-soluble cell-wall polysaccharides from Uilva sp. (Ulvales, Chlorophyta)
    • Lahaye, M., M. Brunel, and E. Bonnin. 1997. Fine chemical structure analysis of oligosaccharides produced by an ulvan-lyase degradation of the water-soluble cell-wall polysaccharides from Uilva sp. (Ulvales, Chlorophyta). Carbohydr. Res. 304:325-333.
    • (1997) Carbohydr. Res. , vol.304 , pp. 325-333
    • Lahaye, M.1    Brunel, M.2    Bonnin, E.3
  • 26
    • 0007384811 scopus 로고
    • Kinetics and specificity of alginate lyases
    • Larsen, B., K. Hooen, and K. Oslgaard. 1993. Kinetics and specificity of alginate lyases. Hydrobiologia 260/261:557-561.
    • (1993) Hydrobiologia , vol.260-261 , pp. 557-561
    • Larsen, B.1    Hooen, K.2    Oslgaard, K.3
  • 27
    • 0031886487 scopus 로고    scopus 로고
    • Exopolysaccharide II production is regulated by salt in the halotolerant strain Rhizohium meliloti EFBI
    • Lloret, J., B. B. H. Wulf, J. M. Rubio, J. A. Downie, I. Bonilla, and R. Rivilla. 1998. Exopolysaccharide II production is regulated by salt in the halotolerant strain Rhizohium meliloti EFBI. Appl. Environ Microbiol 64:1024-1028.
    • (1998) Appl. Environ Microbiol , vol.64 , pp. 1024-1028
    • Lloret, J.1    Wulf, B.B.H.2    Rubio, J.M.3    Downie, J.A.4    Bonilla, I.5    Rivilla, R.6
  • 28
    • 0027312126 scopus 로고
    • Cloning, sequence analysis and expression in Escherichia coli of a gene encoding an alginate lyase from Pseudamonas sp OS-Alg-9
    • Maki, H., A. Mori, K. Fujiyama, S. Kinoshita, and T. Yoshida. 1993. Cloning, sequence analysis and expression in Escherichia coli of a gene encoding an alginate lyase from Pseudamonas sp OS-Alg-9. J. Ger. Microbiol. 139: 987-993.
    • (1993) J. Ger. Microbiol. , vol.139 , pp. 987-993
    • Maki, H.1    Mori, A.2    Fujiyama, K.3    Kinoshita, S.4    Yoshida, T.5
  • 31
    • 0031941054 scopus 로고    scopus 로고
    • An effective method for isolating alginate lyase-producing Bacillus sp. ATB-1015 strain and purification and characterisation of the lyase
    • Nakagawa, A., T. Ozaki, K. Chubachi, T. Hosoyama, T. Okubo, S. Iyobe, and T. Suzuki. 1998 An effective method for isolating alginate lyase-producing Bacillus sp. ATB-1015 strain and purification and characterisation of the lyase. J. Appl. Microbiol. 84:328-335.
    • (1998) J. Appl. Microbiol. , vol.84 , pp. 328-335
    • Nakagawa, A.1    Ozaki, T.2    Chubachi, K.3    Hosoyama, T.4    Okubo, T.5    Iyobe, S.6    Suzuki, T.7
  • 32
    • 0033018230 scopus 로고    scopus 로고
    • Cloning and expression of the algl. gene, encoding the Azotobacter chroococcum alginate lyase: Purification and characterization of the enzyme
    • Pecina, A., A. Pascual, and A. Paneque. 1999. Cloning and expression of the algl. gene, encoding the Azotobacter chroococcum alginate lyase: purification and characterization of the enzyme. J. Bacteriol. 181:1409-1414.
    • (1999) J. Bacteriol. , vol.181 , pp. 1409-1414
    • Pecina, A.1    Pascual, A.2    Paneque, A.3
  • 33
    • 0031754996 scopus 로고    scopus 로고
    • Separation of low-molecular-mass acetylated glucuronans on L-histidine immobilized onto poly(ethylene-vinyl alcohol) hollow-fiber membranes
    • Pirlet, A. S., O. Pitiot, L. Guentas, A. Heyraud, B. Courtois, J. Courtois, and M. A. Vijalayakshmi. 1998. Separation of low-molecular-mass acetylated glucuronans on L-histidine immobilized onto poly(ethylene-vinyl alcohol) hollow-fiber membranes. J. Chromatogr. 826:157-166.
    • (1998) J. Chromatogr. , vol.826 , pp. 157-166
    • Pirlet, A.S.1    Pitiot, O.2    Guentas, L.3    Heyraud, A.4    Courtois, B.5    Courtois, J.6    Vijalayakshmi, M.A.7
  • 34
    • 0033151658 scopus 로고    scopus 로고
    • Oligosaccharide recognition signals and defence reactions in marine plant-microbe interactions
    • Potin, P., K. Bouarab, K. Küpper, and B. Kloareg. 1999 Oligosaccharide recognition signals and defence reactions in marine plant-microbe interactions. Curr. Opin. Microbiol. 2:276-283.
    • (1999) Curr. Opin. Microbiol. , vol.2 , pp. 276-283
    • Potin, P.1    Bouarab, K.2    Küpper, K.3    Kloareg, B.4
  • 35
    • 0030827479 scopus 로고    scopus 로고
    • Novel alginate lyases from marine bacterium Alteromonas sp. strain H-4
    • Sawabe, T., M. Ohtsuka, and Y. Ezura. 1997. Novel alginate lyases from marine bacterium Alteromonas sp. strain H-4. Carhohydr. Res, 304:69-76.
    • (1997) Carhohydr. Res , vol.304 , pp. 69-76
    • Sawabe, T.1    Ohtsuka, M.2    Ezura, Y.3
  • 36
    • 0031126778 scopus 로고    scopus 로고
    • Purification and characterization of extracellular poly(β-D1,4-mannuronide) lyase from Dendryhiella salina IFO 32139
    • Shimokawa, T., S. Yoshida, T. Takeuchi, K. Murata, H. Kobayashi, and I. Kusakabe, 1997. Purification and characterization of extracellular poly(β-D1,4-mannuronide) lyase from Dendryhiella salina IFO 32139. Biosci. Biotech. Biochem. 61:636-640.
    • (1997) Biosci. Biotech. Biochem. , vol.61 , pp. 636-640
    • Shimokawa, T.1    Yoshida, S.2    Takeuchi, T.3    Murata, K.4    Kobayashi, H.5    Kusakabe, I.6
  • 37
    • 0023050603 scopus 로고
    • Monomer sequence and acetylation pattern in some bacterial alginates
    • Skjak-Braek. G., H. Grasdalen, and B. Larsen. 1986. Monomer sequence and acetylation pattern in some bacterial alginates. Carbohydr. Res. 154: 239-250.
    • (1986) Carbohydr. Res. , vol.154 , pp. 239-250
    • Skjak-Braek, G.1    Grasdalen, H.2    Larsen, B.3
  • 39
    • 0030911037 scopus 로고    scopus 로고
    • Cloning and sequencing of the hyaluronate lyase gene from Propionibacterium acnes
    • Steiner, B., S. Romero-Steiner, D. Cruce, and R. George. 1997. Cloning and sequencing of the hyaluronate lyase gene from Propionibacterium acnes. Can. J. Microbiol. 43:315-321.
    • (1997) Can. J. Microbiol. , vol.43 , pp. 315-321
    • Steiner, B.1    Romero-Steiner, S.2    Cruce, D.3    George, R.4
  • 41
    • 0029922414 scopus 로고    scopus 로고
    • Polysaccharide lyases from gellanproducing Sphingomonas spp
    • Sutherland, I. W., and L. Kennedy. 1996. Polysaccharide lyases from gellanproducing Sphingomonas spp Microbiology 142:867-872.
    • (1996) Microbiology , vol.142 , pp. 867-872
    • Sutherland, I.W.1    Kennedy, L.2
  • 42
    • 0033115002 scopus 로고    scopus 로고
    • Polysaccharases for microbial exopolysaccharides
    • Sutherland, I. W. 1999 Polysaccharases for microbial exopolysaccharides. Carhohydr Polym. 38:319-328.
    • (1999) Carhohydr Polym. , vol.38 , pp. 319-328
    • Sutherland, I.W.1
  • 43
    • 0023406022 scopus 로고
    • Assay of reducing sugars in the nanomolerange with 2.2 -bicinchoninate
    • Waffenschmidt, S., and L. Jaenicke. 1987. Assay of reducing sugars in the nanomolerange with 2.2 -bicinchoninate Anal. Biochem. 165:337-340.
    • (1987) Anal. Biochem. , vol.165 , pp. 337-340
    • Waffenschmidt, S.1    Jaenicke, L.2
  • 44
    • 78651113725 scopus 로고
    • The formation of 2-keto-3-deoxy heptonic acid in extracts of Escherichia coli B
    • Weissbach, A., and J. Hurwitz. 1958. The formation of 2-keto-3-deoxy heptonic acid in extracts of Escherichia coli B. J. Biol. Chem. 234:705-712.
    • (1958) J. Biol. Chem. , vol.234 , pp. 705-712
    • Weissbach, A.1    Hurwitz, J.2
  • 45
    • 0030965769 scopus 로고    scopus 로고
    • Efiicient purification, characterization and partial amino acid sequencing of two α-1,4-glucan lyases from fungi
    • Yu, S., T. M. I. E. Christensen, K. M. Kragh, K. Bojsen, and J. Marcussen. 1997. Efiicient purification, characterization and partial amino acid sequencing of two α-1,4-glucan lyases from fungi. Biochim. Biophys. Acta 1339:311-320.
    • (1997) Biochim. Biophys. Acta , vol.1339 , pp. 311-320
    • Yu, S.1    Christensen, T.M.I.E.2    Kragh, K.M.3    Bojsen, K.4    Marcussen, J.5


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