title: A natural prodrug activation mechanism in nonribosomal peptide synthesis.
abstract: We have identified a new mechanism for the cleavage and activation of nonribosomally made peptides and peptide-polyketide hybrids that are apparently operational in several different bacteria. This process includes the cleavage of a precursor molecule by a membrane-bound and D-asparagine-specific peptidase, as shown here in the biosynthesis of the antibiotic xenocoumacin from Xenorhabdus nematophila.
authors.affiliation: Molecular Biotechnology, Institute for Molecular Biosciences, Goethe University Frankfurt, Frankfurt, Germany.
authors.forename: Daniela
authors.initials: D
authors.lastname: Reimer
authors.forename: Klaas M
authors.initials: KM
authors.lastname: Pos
authors.forename: Marco
authors.initials: M
authors.lastname: Thines
authors.forename: Peter
authors.initials: P
authors.lastname: Grün
authors.forename: Helge B
authors.initials: HB
authors.lastname: Bode
mesh_terms: D000900:Anti-Bacterial Agents / Q000096:biosynthesis* / Q000737:chemistry; D001578:Benzopyrans / Q000737:chemistry / Q000378:metabolism; D008968:Molecular Conformation; D010452:Peptide Biosynthesis; D011355:Prodrugs / Q000737:chemistry / Q000378:metabolism*; D013237:Stereoisomerism; D020593:Xenorhabdus / Q000737:chemistry*
chemical_list: D000900:Anti-Bacterial Agents; D001578:Benzopyrans; D011355:Prodrugs