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Volumn 48, Issue 3, 2009, Pages 511-513

In vitro kinetic analysis of substrate specificity in enterobactin biosynthetic lower pathway enzymes provides insight into the biochemical function of the hot dog-fold thioesterase EntH

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMICAL FUNCTIONS; DIHYDROXYBENZOATE; ENTEROBACTIN; IN-VITRO; KINETIC ANALYSIS; L SERINES; NONRIBOSOMAL PEPTIDE SYNTHETASES; SIDEROPHORE; SUBSTRATE SPECIFICITIES; THIOESTERASE;

EID: 59249107241     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi802207t     Document Type: Article
Times cited : (22)

References (9)
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  • 2
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    • Payne, S.M.1
  • 3
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    • (2002) Microbiol. Mol. Biol. Rev , vol.66 , pp. 223-249
    • Crossa, J.A.1    Walsh, C.T.2
  • 4
    • 13244267005 scopus 로고    scopus 로고
    • The hotdog fold: Wrapping up a superfamily of thioesterases and dehydratases
    • Dillon, S. C., and Bateman, A. (2004) The hotdog fold: Wrapping up a superfamily of thioesterases and dehydratases. BMC Bioinf. 5, 109.
    • (2004) BMC Bioinf , vol.5 , pp. 109
    • Dillon, S.C.1    Bateman, A.2
  • 5
    • 4544326782 scopus 로고    scopus 로고
    • PchC thioesterase optimizes nonribosomal biosynthesis of the peptide siderophore pyochelin in Pseudomonas aeruginosa
    • Reimmann, C., Patel, H. M., Walsh, C. T., and Haas, D. (2004) PchC thioesterase optimizes nonribosomal biosynthesis of the peptide siderophore pyochelin in Pseudomonas aeruginosa. J. Bacteriol. 186, 6367-6373.
    • (2004) J. Bacteriol , vol.186 , pp. 6367-6373
    • Reimmann, C.1    Patel, H.M.2    Walsh, C.T.3    Haas, D.4
  • 6
    • 4644278719 scopus 로고    scopus 로고
    • Type II thioesterase restores activity of a NRPS module stalled with an aminoacyl-S-enzyme that cannot be elongated
    • Yeh, E., Kohli, R. M., Bruner, S. D., and Walsh, C. T. (2004) Type II thioesterase restores activity of a NRPS module stalled with an aminoacyl-S-enzyme that cannot be elongated. ChemBioChem 5, 1290-1293.
    • (2004) ChemBioChem , vol.5 , pp. 1290-1293
    • Yeh, E.1    Kohli, R.M.2    Bruner, S.D.3    Walsh, C.T.4
  • 7
    • 0037195068 scopus 로고    scopus 로고
    • Regeneration of misprimed nonribosomal peptide synthetases by type II thioesterases
    • Schwarzer, D., Mootz, H. D., Linne, U., and Marahiel, M. A. (2002) Regeneration of misprimed nonribosomal peptide synthetases by type II thioesterases. Proc. Natl. Acad. Sci. U.S.A. 99, 14083-14088.
    • (2002) Proc. Natl. Acad. Sci. U.S.A , vol.99 , pp. 14083-14088
    • Schwarzer, D.1    Mootz, H.D.2    Linne, U.3    Marahiel, M.A.4
  • 8
    • 34948820655 scopus 로고    scopus 로고
    • The hotdog thioesterase EntH (YbdB) plays a role in vivo in optimal enterobactin biosynthesis by interacting with the ArCP domain of EntB
    • Leduc, D., Battesti, A., and Bouveret, E. (2007) The hotdog thioesterase EntH (YbdB) plays a role in vivo in optimal enterobactin biosynthesis by interacting with the ArCP domain of EntB. J Bacteriol. 189, 7112-7126.
    • (2007) J Bacteriol , vol.189 , pp. 7112-7126
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  • 9
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    • Gerhing, A. M., Bradely, K. A., and Walsh, C. T. (1997) Enterobactin biosynthesis in E. coli: Isochorismate lyase (EntB) is a bifunctional enzyme that is phosphopantetheinylated by EntD and then acylated by EntE using ATP and 2,3-dihydroxybenzoate. Biochemistry 36, 8495-8503.
    • (1997) Biochemistry , vol.36 , pp. 8495-8503
    • Gerhing, A.M.1    Bradely, K.A.2    Walsh, C.T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.