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Volumn 49, Issue 36, 2010, Pages 7939-7948

Structural and functional studies of WlbA: A dehydrogenase involved in the biosynthesis of 2,3-diacetamido-2,3-dideoxy- D -mannuronic acid

Author keywords

[No Author keywords available]

Indexed keywords

ACIDS; AMIDES; BIOCHEMISTRY; BIOSYNTHESIS; CATALYSIS; INTERNET PROTOCOLS; SUGAR (SUCROSE);

EID: 77956418190     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi101103s     Document Type: Article
Times cited : (16)

References (23)
  • 3
    • 70349972115 scopus 로고    scopus 로고
    • Review: Lipopolysaccharide biosynthesis in Pseudomonas aeruginosa
    • King, J. D., Kocincova, D., Westman, E. L., and Lam, J. S. (2009) Review: Lipopolysaccharide biosynthesis in Pseudomonas aeruginosa Innate Immun. 15, 261-312
    • (2009) Innate Immun. , vol.15 , pp. 261-312
    • King, J.D.1    Kocincova, D.2    Westman, E.L.3    Lam, J.S.4
  • 4
    • 76549128410 scopus 로고    scopus 로고
    • Lipopolysaccharide: Biosynthetic pathway and structure modification
    • Wang, X. and Quinn, P. J. (2010) Lipopolysaccharide: Biosynthetic pathway and structure modification Prog. Lipid Res. 49, 97-107
    • (2010) Prog. Lipid Res. , vol.49 , pp. 97-107
    • Wang, X.1    Quinn, P.J.2
  • 5
    • 0042970055 scopus 로고
    • 2,3-Diacetamido-2,3-dideoxy- d -mannuronic acid and its 2-imidazoline derivative: New acidic amino sugars from Pseudomonas aeruginosa O:3a,d lipopolysaccharide
    • Knirel, Y. A., Vinogradov, E. V., Shashkov, A. S., Dmitriev, B. A., and Kochetkov, N. K. (1982) 2,3-Diacetamido-2,3-dideoxy- d -mannuronic acid and its 2-imidazoline derivative: New acidic amino sugars from Pseudomonas aeruginosa O:3a,d lipopolysaccharide Carbohydr. Res. 104, C4-C7
    • (1982) Carbohydr. Res. , vol.104
    • Knirel, Y.A.1    Vinogradov, E.V.2    Shashkov, A.S.3    Dmitriev, B.A.4    Kochetkov, N.K.5
  • 6
    • 0023656274 scopus 로고
    • Somatic antigens of Pseudomonas aeruginosa. The structure of O-specific polysaccharide chains of lipopolysaccharides of P. aeruginosa O3 (Lanyi), O25 (Wokatsch) and Fisher immunotypes 3 and 7
    • Knirel, Y. A., Paramonov, N. A., Vinogradov, E. V., Shashkov, A. S., Dmitriev, B. A., Kochetkov, N. K., Kholodkova, E. V., and Stanislavsky, E. S. (1987) Somatic antigens of Pseudomonas aeruginosa. The structure of O-specific polysaccharide chains of lipopolysaccharides of P. aeruginosa O3 (Lanyi), O25 (Wokatsch) and Fisher immunotypes 3 and 7 Eur. J. Biochem. 167, 549-561
    • (1987) Eur. J. Biochem. , vol.167 , pp. 549-561
    • Knirel, Y.A.1    Paramonov, N.A.2    Vinogradov, E.V.3    Shashkov, A.S.4    Dmitriev, B.A.5    Kochetkov, N.K.6    Kholodkova, E.V.7    Stanislavsky, E.S.8
  • 7
    • 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
  • 8
    • 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
  • 9
    • 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
  • 10
    • 77953097504 scopus 로고    scopus 로고
    • Molecular structure of WlbB, a bacterial N -acetyltransferase involved in the biosynthesis of 2,3-diacetamido-2,3-dideoxy- d -mannuronic acid
    • Thoden, J. B. and Holden, H. M. (2010) Molecular structure of WlbB, a bacterial N -acetyltransferase involved in the biosynthesis of 2,3-diacetamido-2,3-dideoxy- d -mannuronic acid Biochemistry 49, 4644-4653
    • (2010) Biochemistry , vol.49 , pp. 4644-4653
    • Thoden, J.B.1    Holden, H.M.2
  • 11
    • 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
    • (1996) Structure , vol.4 , pp. 1413-1428
    • Kingston, R.L.1    Scopes, R.K.2    Baker, E.N.3
  • 12
    • 15744370513 scopus 로고    scopus 로고
    • Molecular structure of human galactokinase: Implications for Type II galactosemia
    • 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
    • (2005) J. Biol. Chem. , vol.280 , pp. 9662-9670
    • Thoden, J.B.1    Timson, D.J.2    Reece, R.J.3    Holden, H.M.4
  • 13
    • 33745933955 scopus 로고    scopus 로고
    • HKL-3000: The integration of data reduction and structure solution - From diffraction images to an initial model in minutes
    • 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. D62, 859-866
    • (2006) Acta Crystallogr. , vol.62 , pp. 859-866
    • Minor, W.1    Cymborowski, M.2    Otwinowski, Z.3    Chruszcz, M.4
  • 14
    • 0033119895 scopus 로고    scopus 로고
    • Automated MAD and MIR structure solution
    • Terwilliger, T. C. and Berendzen, J. (1999) Automated MAD and MIR structure solution Acta Crystallogr. D55 (Part 4) 849-861
    • (1999) Acta Crystallogr. , vol.55 , Issue.PART 4 , pp. 849-861
    • Terwilliger, T.C.1    Berendzen, J.2
  • 15
    • 0033896691 scopus 로고    scopus 로고
    • Maximum-likelihood density modification
    • Terwilliger, T. C. (2000) Maximum-likelihood density modification Acta Crystallogr. D56 (Part 8) 965-972
    • (2000) Acta Crystallogr. , vol.56 , Issue.PART 8 , pp. 965-972
    • Terwilliger, T.C.1
  • 16
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Emsley, P. and Cowtan, K. (2004) Coot: Model-building tools for molecular graphics Acta Crystallogr. D60, 2126-2132
    • (2004) Acta Crystallogr. , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 18
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov, G. N., Vagin, A. A., and Dodson, E. J. (1997) Refinement of macromolecular structures by the maximum-likelihood method Acta Crystallogr. D53, 240-255
    • (1997) Acta Crystallogr. , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 20
    • 0024278356 scopus 로고
    • The kinetics of glucose-fructose oxidoreductase from Zymomonas mobilis
    • Hardman, M. J. and Scopes, R. K. (1988) The kinetics of glucose-fructose oxidoreductase from Zymomonas mobilis Eur. J. Biochem. 173, 203-209
    • (1988) Eur. J. Biochem. , vol.173 , pp. 203-209
    • Hardman, M.J.1    Scopes, R.K.2
  • 21
    • 0015955554 scopus 로고
    • Description of Thermus thermophilus (Yoshida and Oshima) comb. nov., a Nonsporulating Thermophilic Bacterium from a Japanese Thermal Spa
    • Oshima, T. and Imahori, K. (1974) Description of Thermus thermophilus (Yoshida and Oshima) comb. nov., a Nonsporulating Thermophilic Bacterium from a Japanese Thermal Spa Int. J. Syst. Bacteriol. 24, 102-112
    • (1974) Int. J. Syst. Bacteriol. , vol.24 , pp. 102-112
    • Oshima, T.1    Imahori, K.2
  • 22
    • 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.