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Volumn 48, Issue 12, 2009, Pages 2699-2709

Structural and functional studies of QdtC: An N-acetyltransferase required for the biosynthesis of dTDP-3-acetamido-3,6-dideoxy-R-D-glucose

Author keywords

[No Author keywords available]

Indexed keywords

ACETAMIDO; ACETYL-COA; ACTIVE SITES; AMINO ACID RESIDUES; AMINO GROUPS; BIOSYNTHETIC PATHWAYS; CATALYTIC BASE; CATALYTIC MECHANISMS; D GALACTOSE; D GLUCOSE; GLYCANS; GRAM-NEGATIVE BACTERIA; GRAM-POSITIVE BACTERIA; MUTANT PROTEINS; N-ACETYLTRANSFERASE; PROTON ACCEPTORS; S LAYERS; SUBUNIT INTERFACES; TERNARY COMPLEXES; TRIMERIC ENZYMES; WILD-TYPE ENZYMES;

EID: 65249154793     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi802313n     Document Type: Article
Times cited : (24)

References (23)
  • 1
    • 3843086796 scopus 로고    scopus 로고
    • Genes and enzymes involved in deoxysugar biosynthesis in bacteria
    • Trefzer, A., Salas, J. A., and Bechthold, A. (1999) Genes and enzymes involved in deoxysugar biosynthesis in bacteria. Nat. Prod. Rep. 16, 283-299.
    • (1999) Nat. Prod. Rep , vol.16 , pp. 283-299
    • Trefzer, A.1    Salas, J.A.2    Bechthold, A.3
  • 3
    • 38449105655 scopus 로고    scopus 로고
    • Antifungal agents
    • Chen, S. C., and Sorrell, T. C. (2007) Antifungal agents. Med. J. Aust. 187, 404-409.
    • (2007) Med. J. Aust , vol.187 , pp. 404-409
    • Chen, S.C.1    Sorrell, T.C.2
  • 4
    • 1542269182 scopus 로고    scopus 로고
    • Avermectin: Biochemical and molecular basis of its biosynthesis and regulation
    • Yoon, Y. J., Kim, E. S., Hwang, Y. S., and Choi, C. Y. (2004) Avermectin: Biochemical and molecular basis of its biosynthesis and regulation. Appl. Microbiol. Biotechnol. 63, 626-634.
    • (2004) Appl. Microbiol. Biotechnol , vol.63 , pp. 626-634
    • Yoon, Y.J.1    Kim, E.S.2    Hwang, Y.S.3    Choi, C.Y.4
  • 5
    • 2642566088 scopus 로고    scopus 로고
    • Anthracyclines: Molecular advances and pharmacologic developments in antitumor activity and cardiotoxicity
    • Minotti, G., Menna, P., Salvatorelli, E., Cairo, G., and Gianni, L. (2004) Anthracyclines: Molecular advances and pharmacologic developments in antitumor activity and cardiotoxicity. Pharmacol. Rev. 56, 185-229.
    • (2004) Pharmacol. Rev , vol.56 , pp. 185-229
    • Minotti, G.1    Menna, P.2    Salvatorelli, E.3    Cairo, G.4    Gianni, L.5
  • 6
    • 3843111246 scopus 로고    scopus 로고
    • Identification of Escherichia coli O114 O-antigen gene cluster and development of an O114 serogroup-specific PCR assay
    • Feng, L., Wang, W., Tao, J., Guo, H., Krause, G., Beutin, L., and Wang, L. (2004) Identification of Escherichia coli O114 O-antigen gene cluster and development of an O114 serogroup-specific PCR assay. J. Clin. Microbiol. 42, 3799-3804.
    • (2004) J. Clin. Microbiol , vol.42 , pp. 3799-3804
    • Feng, L.1    Wang, W.2    Tao, J.3    Guo, H.4    Krause, G.5    Beutin, L.6    Wang, L.7
  • 9
    • 15844409901 scopus 로고    scopus 로고
    • Genetic organization of chromosomal S-layer glycan biosynthesis loci of Bacillaceae
    • Novotny, R., Pfoestl, A., Messner, P., and Schaffer, C. (2004) Genetic organization of chromosomal S-layer glycan biosynthesis loci of Bacillaceae. Glycoconjugate J. 20, 435-447.
    • (2004) Glycoconjugate J , vol.20 , pp. 435-447
    • Novotny, R.1    Pfoestl, A.2    Messner, P.3    Schaffer, C.4
  • 10
    • 34547095033 scopus 로고    scopus 로고
    • The X-ray structure of dTDP-4-keto-6-deoxy-D-glucose-3,4-ketoisomerase
    • Davis, M. L., Thoden, J. B., and Holden, H. M. (2007) The X-ray structure of dTDP-4-keto-6-deoxy-D-glucose-3,4-ketoisomerase. J. Biol. Chem. 282, 19227-19236.
    • (2007) J. Biol. Chem , vol.282 , pp. 19227-19236
    • Davis, M.L.1    Thoden, J.B.2    Holden, H.M.3
  • 11
    • 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.D55 , Issue.PART 4 , pp. 849-861
    • Terwilliger, T.C.1    Berendzen, J.2
  • 12
    • 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.D56 , Issue.PART 8 , pp. 965-972
    • Terwilliger, T.C.1
  • 13
    • 0037237545 scopus 로고    scopus 로고
    • Automated main-chain model building by template matching and iterative fragment extension
    • Terwilliger, T. C. (2003) Automated main-chain model building by template matching and iterative fragment extension. Acta Crystallogr. D59, 38-44.
    • (2003) Acta Crystallogr , vol.D59 , pp. 38-44
    • Terwilliger, T.C.1
  • 14
    • 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.D60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 15
    • 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. A43, 489-501.
    • (1987) Acta Crystallogr , vol.A43 , pp. 489-501
    • Tronrud, D.E.1    Ten Eyck, L.F.2    Matthews, B.W.3
  • 17
    • 0002936576 scopus 로고
    • A spectrophotometric assay for thiogalactoside transacetylase
    • Alpers, D. H., Appel, S. H., and Tomkins, G. M. (1965) A spectrophotometric assay for thiogalactoside transacetylase. J. Biol. Chem. 240, 10-13.
    • (1965) J. Biol. Chem , vol.240 , pp. 10-13
    • Alpers, D.H.1    Appel, S.H.2    Tomkins, G.M.3
  • 18
    • 28944432885 scopus 로고    scopus 로고
    • The kinetic mechanism of AAC3-IV aminoglycoside acetyltransferase from Escherichia coli
    • Magalhaes, M. L., and Blanchard, J. S. (2005) The kinetic mechanism of AAC3-IV aminoglycoside acetyltransferase from Escherichia coli. Biochemistry 44, 16275-16283.
    • (2005) Biochemistry , vol.44 , pp. 16275-16283
    • Magalhaes, M.L.1    Blanchard, J.S.2
  • 19
    • 0028844306 scopus 로고
    • A left-handed parallel β helix in the structure of UDP-N-acetylglucosamine acyltransferase
    • Raetz, C. R., and Roderick, S. L. (1995) A left-handed parallel β helix in the structure of UDP-N-acetylglucosamine acyltransferase. Science 270, 997-1000.
    • (1995) Science , vol.270 , pp. 997-1000
    • Raetz, C.R.1    Roderick, S.L.2
  • 20
    • 39649117771 scopus 로고    scopus 로고
    • Structure and active site residues of PglD, an N-acetyltransferase from the bacillosamine synthetic pathway required for N-glycan synthesis in Campylobacter jejuni
    • Rangarajan, E. S., Ruane, K M., Sulea, T., Watson, D. C., Proteau, A., Leclerc, S., Cygler, M., Matte, A., and Young, N. M. (2008) Structure and active site residues of PglD, an N-acetyltransferase from the bacillosamine synthetic pathway required for N-glycan synthesis in Campylobacter jejuni. Biochemistry 47, 1827-1836.
    • (2008) Biochemistry , vol.47 , pp. 1827-1836
    • Rangarajan, E.S.1    Ruane, K.M.2    Sulea, T.3    Watson, D.C.4    Proteau, A.5    Leclerc, S.6    Cygler, M.7    Matte, A.8    Young, N.M.9
  • 21
    • 55549145055 scopus 로고    scopus 로고
    • Crystal structure and catalytic mechanism of PglD from Campylobacter jejuni
    • Olivier, N. B., and Imperiali, B. (2008) Crystal structure and catalytic mechanism of PglD from Campylobacter jejuni. J. Biol. Chem. 283, 27937-27946.
    • (2008) J. Biol. Chem , vol.283 , pp. 27937-27946
    • Olivier, N.B.1    Imperiali, B.2
  • 22
    • 0034476899 scopus 로고    scopus 로고
    • Structure and mechanism of homoserine kinase: Prototype for the GHMP kinase superfamily
    • Zhou, T., Daugherty, M., Grishin, N. V., Osterman, A. L., and Zhang, H. (2000) Structure and mechanism of homoserine kinase: Prototype for the GHMP kinase superfamily. Struct. Folding Des. 8, 1247-1257.
    • (2000) Struct. Folding Des , vol.8 , pp. 1247-1257
    • Zhou, T.1    Daugherty, M.2    Grishin, N.V.3    Osterman, A.L.4    Zhang, H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.