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Volumn 7, Issue 10, 2000, Pages 765-772

Aminoacyl-SNACs as small-molecule substrates for the condensation domains of nonribosomal peptide synthetases

Author keywords

Condensation domain; Nonribosomal peptide synthetase; Substrate specificity

Indexed keywords

DRUG DERIVATIVE; ENTEROBACTIN SYNTHETASE; ENTEROCHELIN; ESTER; LIGASE; MERCAPTAMINE; MULTIENZYME COMPLEX; NON RIBOSOMAL PEPTIDE SYNTHASE; NON-RIBOSOMAL PEPTIDE SYNTHASE; PEPTIDE SYNTHASE; PROTEIN SUBUNIT; TYROCIDINE SYNTHETASE;

EID: 0033782162     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1074-5521(00)00022-3     Document Type: Article
Times cited : (108)

References (26)
  • 5
    • 0344222177 scopus 로고    scopus 로고
    • Penicillin biosynthesis: Energy requirement for tripeptide precursor formation by delta-(L-α-aminoadipyl)-L-cysteinyl-D-valine synthetase from Acremonium chrysogenum
    • (1998) Biochemistry , vol.37 , pp. 5947-5952
    • Kallow, W.1    Von Dohren, H.2    Kleinkauf, H.3
  • 23
    • 0030738431 scopus 로고    scopus 로고
    • Enterobactin biosynthesis in Escherichia coli: Isochorismate lyase (EntB) is a bifunctional enzyme that is phosphopantetheinylated by EntD and then acylated by EntE using ATP and 2, 3-dihydroxybenzoate
    • (1997) Biochemistry , vol.36 , pp. 8495-8503
    • Gehring, A.M.1    Bradley, K.A.2    Walsh, C.T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.