title: Protein templates for the biosynthesis of peptide antibiotics.
abstract: Peptide synthetases of microbial origin can act as protein templates for the biosynthesis of unusual, often pharmacologically active, peptides of diverse structure and biological activity. Specific repeated modules in the synthetases each contain at least two distinct domains, required for substrate adenylation and thiolation, that define the sequence and length of the peptide product. The first crystal structure of an adenylation domain has provided insights into the mechanism of substrate recognition and activation.
authors.affiliation: Biochemie/Fachbereich Chemie, Hans-Meerwein-Strasse, Philipps-Universität Marburg, 35032, Marburg, Germany. marahiel@ps1515.chemie.uni-marburg.de
authors.forename: M A
authors.initials: MA
authors.lastname: Marahiel
mesh_terms: D000249:Adenosine Monophosphate / Q000378:metabolism; D000900:Anti-Bacterial Agents / Q000096:biosynthesis*; D005798:Genes, Bacterial; D005800:Genes, Fungal; D008958:Models, Molecular; D015394:Molecular Structure; D010453:Peptide Synthases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D010455:Peptides; D011487:Protein Conformation; D011499:Protein Processing, Post-Translational; D011506:Proteins / Q000378:metabolism*; D013698:Templates, Genetic
chemical_list: D000900:Anti-Bacterial Agents; D010455:Peptides; D011506:Proteins; D000249:Adenosine Monophosphate; D010453:Peptide Synthases