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Volumn 50, Issue 9, 2011, Pages 1483-1491

Biochemical and structural Characterization of WlbA from Bordetella pertussis and Chromobacterium violaceum: Enzymes required for the biosynthesis of 2,3-diacetamido-2,3-dideoxy- d -mannuronic acid

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; ACTIVE SITE ARCHITECTURE; AMINO ACID SEQUENCE; CHROMOBACTERIUM VIOLACEUM; GLYCOSYLTRANSFERASES; GRAM-NEGATIVE BACTERIA; HYDROXYL GROUPS; KETOGLUTARATE; KINETIC MECHANISM; KINETIC STUDY; LIPOPOLYSACCHARIDES; MANNURONIC ACIDS; N-ACETYLGLUCOSAMINE; OCTAMERS; PING-PONG MECHANISM; PSEUDOMONAS AERUGINOSA; QUATERNARY STRUCTURE; REACTION MECHANISM; SHARP CONTRAST; STRUCTURAL CHARACTERIZATION; TERNARY STRUCTURE; TETRAMERS; THERMUS THERMOPHILUS;

EID: 79952172915     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi101871f     Document Type: Article
Times cited : (15)

References (18)
  • 1
    • 0028710287 scopus 로고
    • Structure of lipopolysaccharides from Gram-negative bacteria. III. Structure of O -specific polysaccharides
    • Knirel, Y. A. and Kochetkov, N. K. (1994) Structure of lipopolysaccharides from Gram-negative bacteria. III. Structure of O -specific polysaccharides Biokhimiya 59, 1784-1851
    • (1994) Biokhimiya , vol.59 , pp. 1784-1851
    • Knirel, Y.A.1    Kochetkov, N.K.2
  • 2
    • 0034443262 scopus 로고    scopus 로고
    • Multiple roles for Bordetella lipopolysaccharide molecules during respiratory tract infection
    • DOI 10.1128/IAI.68.12.6720-6728.2000
    • Harvill, E. T., Preston, A., Cotter, P. A., Allen, A. G., Maskell, D. J., and Miller, J. F. (2000) Multiple roles for Bordetella lipopolysaccharide molecules during respiratory tract infection Infect. Immun. 68, 6720-6728 (Pubitemid 32463376)
    • (2000) Infection and Immunity , vol.68 , Issue.12 , pp. 6720-6728
    • Harvill, E.T.1    Preston, A.2    Cotter, P.A.3    Allen, A.G.4    Maskell, D.J.5    Miller, J.F.6
  • 3
    • 3242755677 scopus 로고    scopus 로고
    • Bordetella pertussis lipopolysaccharide resists the bactericidal effects of pulmonary surfactant protein A
    • Schaeffer, L. M., McCormack, F. X., Wu, H., and Weiss, A. A. (2004) Bordetella pertussis lipopolysaccharide resists the bactericidal effects of pulmonary surfactant protein A J. Immunol. 173, 1959-1965 (Pubitemid 38971632)
    • (2004) Journal of Immunology , vol.173 , Issue.3 , pp. 1959-1965
    • Schaeffer, L.M.1    McCormack, F.X.2    Wu, H.3    Weiss, A.A.4
  • 4
    • 51549111375 scopus 로고    scopus 로고
    • Biosynthesis of a rare di- N -acetylated sugar in the lipopolysaccharides of both Pseudomonas aeruginosa and Bordetella pertussis occurs via an identical scheme despite different gene clusters
    • Westman, E. L., Preston, A., Field, R. A., and Lam, J. S. (2008) Biosynthesis of a rare di- N -acetylated sugar in the lipopolysaccharides of both Pseudomonas aeruginosa and Bordetella pertussis occurs via an identical scheme despite different gene clusters J. Bacteriol. 190, 6060-6069
    • (2008) J. Bacteriol. , vol.190 , pp. 6060-6069
    • Westman, E.L.1    Preston, A.2    Field, R.A.3    Lam, J.S.4
  • 5
    • 66449116171 scopus 로고    scopus 로고
    • Characterization of WbpB, WbpE, and WbpD and reconstitution of a pathway for the biosynthesis of UDP-2,3-diacetamido-2,3-dideoxy- d -mannuronic acid in Pseudomonas aeruginosa
    • Westman, E. L., McNally, D. J., Charchoglyan, A., Brewer, D., Field, R. A., and Lam, J. S. (2009) Characterization of WbpB, WbpE, and WbpD and reconstitution of a pathway for the biosynthesis of UDP-2,3-diacetamido-2,3- dideoxy- d -mannuronic acid in Pseudomonas aeruginosa J. Biol. Chem. 284, 11854-11862
    • (2009) J. Biol. Chem. , vol.284 , pp. 11854-11862
    • Westman, E.L.1    McNally, D.J.2    Charchoglyan, A.3    Brewer, D.4    Field, R.A.5    Lam, J.S.6
  • 6
    • 67049154264 scopus 로고    scopus 로고
    • Biosynthesis of UDP-GlcNAc(3NAc)A by WbpB, WbpE, and WbpD: Enzymes in the Wbp pathway responsible for O -antigen assembly in Pseudomonas aeruginosa PAO1
    • Larkin, A. and Imperiali, B. (2009) Biosynthesis of UDP-GlcNAc(3NAc)A by WbpB, WbpE, and WbpD: enzymes in the Wbp pathway responsible for O -antigen assembly in Pseudomonas aeruginosa PAO1 Biochemistry 48, 5446-5455
    • (2009) Biochemistry , vol.48 , pp. 5446-5455
    • Larkin, A.1    Imperiali, B.2
  • 7
    • 77956418190 scopus 로고    scopus 로고
    • Structural and functional studies of WlbA: A dehydrogenase involved in the biosynthesis of 2,3-diacetamido-2,3-dideoxy- d -mannuronic acid
    • Thoden, J. B. and Holden, H. M. (2010) Structural and functional studies of WlbA: a dehydrogenase involved in the biosynthesis of 2,3-diacetamido-2,3- dideoxy- d -mannuronic acid Biochemistry 49, 7939-7948
    • (2010) Biochemistry , vol.49 , pp. 7939-7948
    • Thoden, J.B.1    Holden, H.M.2
  • 8
    • 0030589696 scopus 로고    scopus 로고
    • The structure of glucose-fructose oxidoreductase from Zymomonas mobilis: An osmoprotective periplasmic enzyme containing non-dissociable NADP
    • Kingston, R. L., Scopes, R. K., and Baker, E. N. (1996) The structure of glucose-fructose oxidoreductase from Zymomonas mobilis: an osmoprotective periplasmic enzyme containing non-dissociable NADP Structure 4, 1413-1428 (Pubitemid 27050275)
    • (1996) Structure , vol.4 , Issue.12 , pp. 1413-1428
    • Kingston, R.L.1    Scopes, R.K.2    Baker, E.N.3
  • 9
    • 0004997147 scopus 로고
    • The antibiotic activity of violacein, prodigiosin, and phthiocol
    • Lichstein, H. C. and Van De Sand, V. F. (1946) The antibiotic activity of violacein, prodigiosin, and phthiocol J. Bacteriol. 52, 145-146
    • (1946) J. Bacteriol. , vol.52 , pp. 145-146
    • Lichstein, H.C.1    Van De Sand, V.F.2
  • 10
    • 15744370513 scopus 로고    scopus 로고
    • Molecular structure of human galactokinase: Implications for type II galactosemia
    • DOI 10.1074/jbc.M412916200
    • Thoden, J. B., Timson, D. J., Reece, R. J., and Holden, H. M. (2005) Molecular structure of human galactokinase: implications for Type II galactosemia J. Biol. Chem. 280, 9662-9670 (Pubitemid 40409664)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.10 , pp. 9662-9670
    • Thoden, J.B.1    Timson, D.J.2    Reece, R.J.3    Holden, H.M.4
  • 11
    • 33745933955 scopus 로고    scopus 로고
    • HKL-3000: The integration of data reduction and structure solution - From diffraction images to an initial model in minutes
    • DOI 10.1107/S0907444906019949
    • Minor, W., Cymborowski, M., Otwinowski, Z., and Chruszcz, M. (2006) HKL-3000: the integration of data reduction and structure solution-from diffraction images to an initial model in minutes Acta Crystallogr., Sect. D: Biol. Crystallogr. 62, 859-866 (Pubitemid 44125661)
    • (2006) Acta Crystallographica Section D: Biological Crystallography , vol.62 , Issue.8 , pp. 859-866
    • Minor, W.1    Cymborowski, M.2    Otwinowski, Z.3    Chruszcz, M.4
  • 16
    • 0002583957 scopus 로고
    • "dM": An automated procedure for phase improvement by density modification
    • Cowtan, K. (1994) "DM": an automated procedure for phase improvement by density modification Joint CCP4 ESF-EACBM Newsl. Protein Crystallogr. 31, 34-38
    • (1994) Joint CCP4 ESF-EACBM Newsl. Protein Crystallogr. , vol.31 , pp. 34-38
    • Cowtan, K.1
  • 17
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R. A., MacArthur, M. W., Moss, D. S., and Thornton, J. M. (1993) PROCHECK: a program to check the stereochemical quality of protein structures J. Appl. Crystallogr. 26, 283-291
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4


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