Introduction of a Non‐Natural Amino Acid into a Nonribosomal Peptide Antibiotic by Modification of Adenylation Domain Specificity

Introduction of a Non‐Natural Amino Acid into a Nonribosomal Peptide Antibiotic by Modification of Adenylation Domain Specificity Structure, Biosynthetic Origin, and Engineered Biosynthesis of Calcium-Dependent Antibiotics from Streptomyces coelicolor Cadasides, Calcium-Dependent Acidic Lipopeptides from the Soil Metagenome That Are Active against Multidrug-Resistant Bacteria A stand-alone adenylation domain forms amide bonds in streptothricin biosynthesis CDA: Calcium‐Dependent Peptide Antibiotics from <i>Streptomyces coelicolor</i> A3(2) Containing Unusual Residues Active site modification of the β-ketoacyl-ACP synthase FabF3 of Streptomyces coelicolor affects the fatty acid chain length of the CDA lipopeptides Active site modification of the β-ketoacyl-ACP synthase FabF3 of Streptomyces coelicolor affects the fatty acid chain length of the CDA lipopeptides Chain Initiation in the Leinamycin-producing Hybrid Nonribosomal Peptide/Polyketide Synthetase from Streptomyces atroolivaceus S-140 A Trojan-Horse Peptide-Carboxymethyl-Cytidine Antibiotic from <i>Bacillus amyloliquefaciens</i> NRPS Substrate Promiscuity Diversifies the Xenematides