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Volumn 48, Issue 23, 2009, Pages 5246-5253

Two site-directed mutations are required for the conversion of a sugar dehydratase into an aminotransferase

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE ARCHITECTURE; AMINATION REACTION; AMINOTRANSFERASE; ASPARTATE AMINOTRANSFERASE; BIOSYNTHETIC PATHWAY; COLITOSE; E. COLI; GRAM-NEGATIVE BACTERIA; HYDROXYL GROUPS; MUTANT PROTEINS; SALMONELLA ENTERICA; SITE-DIRECTED MUTATION; SYNTHASE; THREE-DIMENSIONAL STRUCTURE; VIBRIO CHOLERAE;

EID: 67049119446     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi9005545     Document Type: Article
Times cited : (11)

References (21)
  • 2
    • 0021082768 scopus 로고
    • Role of the capsule and the O antigen in resistance of O18:K1 Escherichia coli to complement-mediated killing
    • Pluschke, G., Mayden, J., Achtman, M., and Levine, R. P. (1983) Role of the capsule and the O antigen in resistance of O18:K1 Escherichia coli to complement-mediated killing. Infect. Immun. 42, 907-913.
    • (1983) Infect. Immun. , vol.42 , pp. 907-913
    • Pluschke, G.1    Mayden, J.2    Achtman, M.3    Levine, R.P.4
  • 3
    • 0022484842 scopus 로고
    • Clonal analysis of descent and virulence among selected Escherichia coli
    • Achtman, M., and Pluschke, G. (1986) Clonal analysis of descent and virulence among selected Escherichia coli. Annu. Rev. Microbiol.40, 185-210.
    • (1986) Annu. Rev. Microbiol. , vol.40 , pp. 185-210
    • Achtman, M.1    Pluschke, G.2
  • 4
    • 0013852426 scopus 로고
    • Isolation of colitosec-ontaining oligosaccharides from the cell wall lipopolysaccharide of Escherichia coli
    • Edstrom, R. D., and Heath, E. C. (1965) Isolation of colitosec-ontaining oligosaccharides from the cell wall lipopolysaccharide of Escherichia coli. Biochem. Biophys. Res. Commun. 21, 638-643.
    • (1965) Biochem. Biophys. Res. Commun. , vol.21 , pp. 638-643
    • Edstrom, R.D.1    Heath, E.C.2
  • 5
    • 0033134851 scopus 로고    scopus 로고
    • Analysis of the genes responsible for the O-antigen synthesis in enterohaemorrhagic Escherichia coli O157
    • Shimizu, T., Yamasaki, S., Tsukamoto, T., and Takeda, Y. (1999) Analysis of the genes responsible for the O-antigen synthesis in enterohaemorrhagic Escherichia coli O157. Microb. Pathog. 26, 235-247.
    • (1999) Microb. Pathog. , vol.26 , pp. 235-247
    • Shimizu, T.1    Yamasaki, S.2    Tsukamoto, T.3    Takeda, Y.4
  • 6
    • 0034869490 scopus 로고    scopus 로고
    • Expression and identification of the RfbE protein Vibrio cholerae O1 and its use for the enzymatic synthesis of GDP-D-perosamine
    • Albermann, C., and Piepersberg, W. (2001) Expression and identification of the RfbE protein from Vibrio cholerae O1 and its use for the enzymatic synthesis of GDP-D-perosamine. Glycobiology11, 655-661. (Pubitemid 32782683)
    • (2001) Glycobiology , vol.11 , Issue.8 , pp. 655-661
    • Albermann, C.1    Piepersberg, W.2
  • 7
    • 0027497227 scopus 로고
    • O-antigenic lipopolysaccharide of Vibrio cholerae O139 Bengal, a new epidemic strain for recent cholera in the Indian subcontinent
    • Hisatsune, K., Kondo, S., Isshiki, Y., Iguchi, T., Kawamata, Y., and Shimada, T. (1993) O-antigenic lipopolysaccharide of Vibrio cholerae O139 Bengal, a new epidemic strain for recent cholera in the Indian subcontinent. Biochem. Biophys. Res. Commun.196, 1309-1315.
    • (1993) Biochem. Biophys. Res. Commun. , vol.196 , pp. 1309-1315
    • Hisatsune, K.1    Kondo, S.2    Isshiki, Y.3    Iguchi, T.4    Kawamata, Y.5    Shimada, T.6
  • 8
    • 0027250349 scopus 로고
    • Variation of the rfb gene clusters in Salmonella enterica
    • Xiang, S. H., Haase, A. M., and Reeves, P. R. (1993) Variation of the rfb gene clusters in Salmonella enterica. J. Bacteriol.175, 4877-4884. (Pubitemid 23220271)
    • (1993) Journal of Bacteriology , vol.175 , Issue.15 , pp. 4877-4884
    • Xiang, S.-H.1    Haase, A.M.2    Reeves, P.R.3
  • 9
    • 33748199595 scopus 로고    scopus 로고
    • 6-dependent enzyme
    • DOI 10.1110/ps.062328306
    • Cook, P. D., Thoden, J. B., and Holden, H. M. (2006) The structure of GDP-4-keto-6-deoxy-D-mannose-3-dehydratase: a unique coenzyme B6-dependent enzyme. Protein Sci.15, 2093-2106. (Pubitemid 44316012)
    • (2006) Protein Science , vol.15 , Issue.9 , pp. 2093-2106
    • Cook, P.D.1    Thoden, J.B.2    Holden, H.M.3
  • 10
    • 40149092973 scopus 로고    scopus 로고
    • GDP-perosamine synthase: Structural analysis and production of a novel trideoxysugar
    • DOI 10.1021/bi702430d
    • Cook, P. D., and Holden, H. M. (2008) GDP-perosamine synthase: structural analysis and production of a novel trideoxysugar. Biochemistry47, 2833-2840. (Pubitemid 351328834)
    • (2008) Biochemistry , vol.47 , Issue.9 , pp. 2833-2840
    • Cook, P.D.1    Holden, H.M.2
  • 11
    • 11144320397 scopus 로고    scopus 로고
    • Biosynthesis of colitose: Expression, purification, and mechanistic characterization of GDP-4-keto-6-deoxy-D-mannose-3-dehydrase (ColD) and GDP-Lcolitose synthase (ColC)
    • Alam, J., Beyer, N., and Liu, H. W. (2004) Biosynthesis of colitose: expression, purification, and mechanistic characterization of GDP-4-keto-6-deoxy-D-mannose-3-dehydrase (ColD) and GDP-Lcolitose synthase (ColC). Biochemistry43, 16450-16460.
    • (2004) Biochemistry , vol.43 , pp. 16450-16460
    • Alam, J.1    Beyer, N.2    Liu, H.W.3
  • 12
    • 37049019111 scopus 로고    scopus 로고
    • A structural study of GDP-4-keto-6-deoxy-D-mannose-3-dehydratase: Caught in the act of geminal diamine formation
    • DOI 10.1021/bi701686s
    • Cook, P. D., and Holden, H. M. (2007) A structural study of GDP-4- keto-6-deoxy-D-mannose-3-dehydratase: caught in the act of geminal diamine formation. Biochemistry46, 14215-14224. (Pubitemid 350250315)
    • (2007) Biochemistry , vol.46 , Issue.49 , pp. 14215-14224
    • Cook, P.D.1    Holden, H.M.2
  • 13
    • 42949104259 scopus 로고    scopus 로고
    • GDP-4-keto-6-deoxy-D-mannose 3-dehydratase, accommodating a sugar substrate in the active site
    • Cook, P. D., and Holden, H. M. (2008) GDP-4-keto-6-deoxy-D-mannose 3-dehydratase, accommodating a sugar substrate in the active site. J. Biol. Chem.283, 4295-4303.
    • (2008) J. Biol. Chem. , vol.283 , pp. 4295-4303
    • Cook, P.D.1    Holden, H.M.2
  • 14
    • 53249103318 scopus 로고    scopus 로고
    • Accommodation of GDP-linked sugars in the active site of GDP-perosamine synthase
    • Cook, P. D., Carney, A. E., and Holden, H. M. (2008) Accommodation of GDP-linked sugars in the active site of GDP-perosamine synthase. Biochemistry 47, 10685-10693.
    • (2008) Biochemistry , vol.47 , pp. 10685-10693
    • Cook, P.D.1    Carney, A.E.2    Holden, H.M.3
  • 15
    • 0035788107 scopus 로고    scopus 로고
    • Pushing the boundaries of molecular replacement with maximum likelihood
    • Read, R. J. (2001) Pushing the boundaries of molecular replacement with maximum likelihood. Acta Crystallogr., Sect. D: Biol. Crystallogr. D57, 1373-1382.
    • (2001) Acta Crystallogr., Sect. D: Biol. Crystallogr. D , vol.57 , pp. 1373-1382
    • Read, R.J.1
  • 16
    • 3042613550 scopus 로고    scopus 로고
    • Likelihood-enhanced fast rotation functions
    • Storoni, L. C., McCoy, A. J., and Read, R. J. (2004) Likelihood-enhanced fast rotation functions. Acta Crystallogr. DD60, 432-438.
    • (2004) Acta Crystallogr. D , vol.D60 , pp. 432-438
    • Storoni, L.C.1    McCoy, A.J.2    Read, R.J.3
  • 18
    • 84913050729 scopus 로고
    • An efficient general-purpose least-squares refinement program for macromolecular structures
    • Tronrud, D. E., Ten Eyck, L. F., and Matthews, B. W. (1987) An efficient general-purpose least-squares refinement program for macromolecular structures. Acta Crystallogr., Sect. A43, 489-501.
    • (1987) Acta Crystallogr., Sect. A , vol.43 , pp. 489-501
    • Tronrud, D.E.1    Ten Eyck, L.F.2    Matthews, B.W.3
  • 20
    • 0242507490 scopus 로고    scopus 로고
    • Crystal Structure of Serine Dehydratase from Rat Liver
    • DOI 10.1021/bi035324p
    • Yamada, T., Komoto, J., Takata, Y., Ogawa, H., Pitot, H. C., and Takusagawa, F. (2003) Crystal structure of serine dehydratase from rat liver. Biochemistry42, 12854-12865. (Pubitemid 37385816)
    • (2003) Biochemistry , vol.42 , Issue.44 , pp. 12854-12865
    • Yamada, T.1    Komoto, J.2    Takata, Y.3    Ogawa, H.4    Pitot, H.C.5    Takusagawa, F.6
  • 21
    • 45749107783 scopus 로고    scopus 로고
    • 1 dehydrase: At the crossroads of dehydration, amino transfer, and epimerization
    • DOI 10.1021/bi702449p
    • Smith, P., Szu, P.H., Bui, C., Liu, H. W., and Tsai, S. C. (2008) Structure and mutagenic conversion of E1 dehydrase: at the crossroads of dehydration, amino transfer, and epimerization. Biochemistry47, 6329-6341. (Pubitemid 351874224)
    • (2008) Biochemistry , vol.47 , Issue.24 , pp. 6329-6341
    • Smith, P.1    Szu, P.-H.2    Bui, C.3    Liu, H.-W.4    Tsai, S.-C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.