PMID:10375542
| Citation |
Shaw-Reid, CA, Kelleher, NL, Losey, HC, Gehring, AM, Berg, C and Walsh, CT (1999) Assembly line enzymology by multimodular nonribosomal peptide synthetases: the thioesterase domain of E. coli EntF catalyzes both elongation and cyclolactonization. Chem. Biol. 6:385-400 |
|---|---|
| Abstract |
EntF is a 142 kDa four domain (condensation-adenylation-peptidyl carrier protein-thioesterase) nonribosomal peptide synthetase (NRPS) enzyme that assembles the Escherichia coli N-acyl-serine trilactone siderophore enterobactin from serine, dihydroxybenzoate (DHB) and ATP with three other enzymes (EntB, EntD and EntE). To assess how EntF forms three ester linkages and cyclotrimerizes the covalent acyl enzyme DHB-Ser-S-PCP (peptidyl carrier protein) intermediate, we mutated residues of the proposed catalytic Ser-His-Asp triad of the thioesterase (TE) domain. |
| Links |
PubMed Online version:10.1016/S1074-5521(99)80050-7 |
| Keywords |
Amino Acid Sequence; Catalytic Domain/genetics; Enterobactin/metabolism; Escherichia coli/enzymology; Escherichia coli/genetics; Models, Biological; Mutagenesis, Site-Directed; Peptide Chain Elongation, Translational; Peptide Synthases/chemistry; Peptide Synthases/genetics; Peptide Synthases/metabolism; Substrate Specificity |
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