Biosynthetic systems for nonribosomal peptide antibiotic assembly.
Modular peptide synthetases, which act as the protein templates for the synthesis of a large number of peptide antibiotics and siderophores, hold great potential for the development of novel compounds. Recently, significant progress has been made towards understanding their molecular architecture and substrate specificity. The first crystal structure of a peptide synthetase has been solved, and the enzymes responsible for post-translational modification of peptide synthetases have recently been discovered. These will allow addressing important yet poorly understood mechanistic aspects.
Philipps-Universität Marburg, Fachbereich Chemie/Biochemie, Hans-Meerwein-Strasse 35032, Marburg, Germany.
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Mootz
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Marahiel
D000595:Amino Acid Sequence; D000900:Anti-Bacterial Agents / Q000096:biosynthesis* / Q000737:chemistry*; D006096:Gramicidin / Q000096:biosynthesis; D008956:Models, Chemical; D005810:Multigene Family; D010453:Peptide Synthases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D013379:Substrate Specificity
D000900:Anti-Bacterial Agents; D006096:Gramicidin; D010453:Peptide Synthases