메뉴 건너뛰기




Volumn 51, Issue 51, 2012, Pages 10259-10266

Functional characterization of AlgL, an alginate lyase from pseudomonas aeruginosa

Author keywords

[No Author keywords available]

Indexed keywords

ALGINATE LYASE; ELIMINATION REACTION; EPIMERS; EXOPOLYSACCHARIDES; FUNCTIONAL CHARACTERIZATION; PERIPLASMIC SPACE; PSEUDOMONAS AERUGINOSA; STEADY-STATE KINETICS; STEREOSPECIFICITY; SUBSTRATE SIZES; SUBSTRATE SPECIFICITY;

EID: 84871545622     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi301425r     Document Type: Article
Times cited : (44)

References (24)
  • 1
    • 0036482281 scopus 로고    scopus 로고
    • Persistent infections and immunity in cystic fibrosis
    • Yu, H. and Head, N. E. (2002) Persistent infections and immunity in cystic fibrosis Front. Biosci. 7, 442-457
    • (2002) Front. Biosci. , vol.7 , pp. 442-457
    • Yu, H.1    Head, N.E.2
  • 2
    • 0141650541 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa alginate is refractory to Th1 immune response and impedes host immune clearance in a mouse model of acute lung infection
    • Song, Z., Wu, H., Ciofu, O., Kong, K.-F., Hoiby, N., Rygaard, J. R., Kharazmi, A., and Mathee, K. (2003) Pseudomonas aeruginosa alginate is refractory to Th1 immune response and impedes host immune clearance in a mouse model of acute lung infection J. Med. Microbiol. 52, 731-740
    • (2003) J. Med. Microbiol. , vol.52 , pp. 731-740
    • Song, Z.1    Wu, H.2    Ciofu, O.3    Kong, K.-F.4    Hoiby, N.5    Rygaard, J.R.6    Kharazmi, A.7    Mathee, K.8
  • 3
    • 0037199430 scopus 로고    scopus 로고
    • Allosterism and cooperativity in Pseudomonas aeruginosa GDP-mannose dehydrogenase
    • Naught, L. E., Gilbert, S., Imhoff, R., Snook, C., Beamer, L., and Tipton, P. (2002) Allosterism and cooperativity in Pseudomonas aeruginosa GDP-mannose dehydrogenase Biochemistry 41, 9637-9645
    • (2002) Biochemistry , vol.41 , pp. 9637-9645
    • Naught, L.E.1    Gilbert, S.2    Imhoff, R.3    Snook, C.4    Beamer, L.5    Tipton, P.6
  • 4
    • 0042974219 scopus 로고    scopus 로고
    • Roles of active site residues in Pseudomonas aeruginosa phosphomannomutase/phosphoglucomutase
    • Naught, L. E., Regni, C., Beamer, L. J., and Tipton, P. A. (2003) Roles of active site residues in Pseudomonas aeruginosa phosphomannomutase/ phosphoglucomutase Biochemistry 42, 9946-9951
    • (2003) Biochemistry , vol.42 , pp. 9946-9951
    • Naught, L.E.1    Regni, C.2    Beamer, L.J.3    Tipton, P.A.4
  • 5
    • 0025871067 scopus 로고
    • Purification and characterization of phosphomannose isomerase-guanosine diphospho-d -mannose pyrophosphorylase. A bifunctional enzyme in the alginate biosynthetic pathway of Pseudomonas aeruginosa
    • Shinabarger, D., Berry, A., May, T. B., Rothmel, R., Fialho, A., and Chakrabarty, A. M. (1991) Purification and characterization of phosphomannose isomerase-guanosine diphospho-d -mannose pyrophosphorylase. A bifunctional enzyme in the alginate biosynthetic pathway of Pseudomonas aeruginosa J. Biol. Chem. 266, 2080-2088
    • (1991) J. Biol. Chem. , vol.266 , pp. 2080-2088
    • Shinabarger, D.1    Berry, A.2    May, T.B.3    Rothmel, R.4    Fialho, A.5    Chakrabarty, A.M.6
  • 6
    • 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, 1-16
    • (2011) Front. Microbiol. , vol.2 , pp. 1-16
    • Franklin, M.J.1    Nivens, D.E.2    Weadge, J.T.3    Howell, P.L.4
  • 7
    • 25444481824 scopus 로고    scopus 로고
    • Role of an alginate lyase for alginate transport in mucoid Pseudomonas aeruginosa
    • Jain, S. and Ohman, D. E. (2005) Role of an alginate lyase for alginate transport in mucoid Pseudomonas aeruginosa Infect. Immun. 73, 6429-6436
    • (2005) Infect. Immun. , vol.73 , pp. 6429-6436
    • Jain, S.1    Ohman, D.E.2
  • 8
    • 0021216094 scopus 로고
    • Isolation and characterization of an alginase from mucoid strains of Pseudomonas aeruginosa
    • Linker, A. and Evans, L. R. (1984) Isolation and characterization of an alginase from mucoid strains of Pseudomonas aeruginosa J. Bacteriol. 159, 958-964
    • (1984) J. Bacteriol. , vol.159 , pp. 958-964
    • Linker, A.1    Evans, L.R.2
  • 9
    • 84862518550 scopus 로고    scopus 로고
    • Expression, purification, crystallization and preliminary X-ray analysis of Pseudomonas aeruginosa AlgL
    • Wolfram, F., Arora, K., Robinson, H., Neculai, A. M., Yip, P., and Howell, P. L. (2012) Expression, purification, crystallization and preliminary X-ray analysis of Pseudomonas aeruginosa AlgL Acta Crystallogr. F68, 584-587
    • (2012) Acta Crystallogr. , vol.68 , pp. 584-587
    • Wolfram, F.1    Arora, K.2    Robinson, H.3    Neculai, A.M.4    Yip, P.5    Howell, P.L.6
  • 11
    • 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
    • (1990) J. Bacteriol. , vol.172 , pp. 2894-2900
    • Chitnis, C.E.1    Ohman, D.E.2
  • 12
    • 0028224854 scopus 로고
    • Isolation and assay of Pseudomonas aeruginosa alginate
    • May, T. B. and Chakrabarty, A. M. (1994) Isolation and assay of Pseudomonas aeruginosa alginate Methods Enzymol. 235, 295-304
    • (1994) Methods Enzymol. , vol.235 , pp. 295-304
    • May, T.B.1    Chakrabarty, A.M.2
  • 13
    • 0037096082 scopus 로고    scopus 로고
    • Determination of reducing sugars with 3-methyl-2- benzothiazolinonehydrazone
    • Anthon, G. E. and Barrett, D. M. (2002) Determination of reducing sugars with 3-methyl-2-benzothiazolinonehydrazone Anal. Biochem. 305, 287-289
    • (2002) Anal. Biochem. , vol.305 , pp. 287-289
    • Anthon, G.E.1    Barrett, D.M.2
  • 14
    • 0013185850 scopus 로고    scopus 로고
    • Modification of alginate using mannuronan C-5-epimerases
    • In (Bucke, C. Ed.) pp. Humana Press, Totowa, NJ. -78
    • Ertesvag, H. and Skjak-Braek, G. (1999) Modification of alginate using mannuronan C-5-epimerases. In Carbohydrate Biotechnology Protocols (Bucke, C., Ed.) pp 71-78., Humana Press, Totowa, NJ.
    • (1999) Carbohydrate Biotechnology Protocols , pp. 71
    • Ertesvag, H.1    Skjak-Braek, G.2
  • 15
    • 0035234566 scopus 로고    scopus 로고
    • Purification and characterization of bifunctional alginate lyase from Alteromonas sp. strain no. 272 and its action on saturated oligomeric substrates
    • Iwamoto, Y., Araki, R., Iriyama, K., Oda, T., Fukuda, H., Hayashida, S., and Muramatsu, T. (2001) Purification and characterization of bifunctional alginate lyase from Alteromonas sp. strain no. 272 and its action on saturated oligomeric substrates Biosci., Biotechnol., Biochem. 65, 133-142
    • (2001) Biosci., Biotechnol., Biochem. , vol.65 , pp. 133-142
    • Iwamoto, Y.1    Araki, R.2    Iriyama, K.3    Oda, T.4    Fukuda, H.5    Hayashida, S.6    Muramatsu, T.7
  • 16
    • 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 of the substrate specificity of Haliotis tuberculate alginate lyase
    • Heyraud, A., Gey, C., Leonard, C., Rochas, C., Girond, S., and Kloareg, B. (1996) NMR spectroscopy analysis of oligoguluronates and oligomannuronates prepared by acid or enzymatic hydrolysis of homopolymeric blocks of alginic acid. Application to the determination of the substrate specificity of Haliotis tuberculate alginate lyase Carbohydr. Res. 289, 11-23
    • (1996) Carbohydr. Res. , vol.289 , pp. 11-23
    • Heyraud, A.1    Gey, C.2    Leonard, C.3    Rochas, C.4    Girond, S.5    Kloareg, B.6
  • 17
    • 0141439132 scopus 로고
    • 1H n.m.r. spectroscopy of alginate: Sequential structure and linkage conformations
    • 1H n.m.r. spectroscopy of alginate: Sequential structure and linkage conformations Carbohydr. Res. 118, 255-260
    • (1983) Carbohydr. Res. , vol.118 , pp. 255-260
    • Grasdalen, H.1
  • 19
    • 0001963343 scopus 로고
    • A p.m.r. study of the composition and sequence of uronate residues in alginate
    • Grasdalen, H., Larsen, B., and Smidsrod, O. (1979) A p.m.r. study of the composition and sequence of uronate residues in alginate Carbohydr. Res. 68, 23-31
    • (1979) Carbohydr. Res. , vol.68 , pp. 23-31
    • Grasdalen, H.1    Larsen, B.2    Smidsrod, O.3
  • 20
    • 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
  • 21
    • 1842800737 scopus 로고
    • Understanding enzyme-catalyzed proton abstraction from carbon acids: Details of stepwise mechanisms for β-elimination reactions
    • Gerlt, J. A. and Gassman, P. G. (1992) Understanding enzyme-catalyzed proton abstraction from carbon acids: Details of stepwise mechanisms for β-elimination reactions J. Am. Chem. Soc. 114, 5928-5934
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 5928-5934
    • Gerlt, J.A.1    Gassman, P.G.2
  • 24
    • 77953734606 scopus 로고    scopus 로고
    • Catalytic Mechanism of Heparinase II Investigated by Site-directed Mutagenesis and the Crystal Structure with Its Substrate
    • Shaya, D., Zhao, W., Garron, M.-L., Xiao, Z., Cui, Q., Zhang, Z., Sulea, T., Linhardt, R. J., and Cygler, M. (2010) Catalytic Mechanism of Heparinase II Investigated by Site-directed Mutagenesis and the Crystal Structure with Its Substrate J. Biol. Chem. 285, 20051-20061
    • (2010) J. Biol. Chem. , vol.285 , pp. 20051-20061
    • Shaya, D.1    Zhao, W.2    Garron, M.-L.3    Xiao, Z.4    Cui, Q.5    Zhang, Z.6    Sulea, T.7    Linhardt, R.J.8    Cygler, M.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.