title: Promiscuous hydroxylases for the functionalization of polycyclic tetramate macrolactams--conversion of ikarugamycin to butremycin.
abstract: Polycyclic tetramate macrolactams (PTMs) are a structurally, biomedically and biosynthetically intriguing class of bacterial metabolites. By combining parts of the machineries of different PTM biosynthetic pathways, we demonstrate for the first time the substrate promiscuity of a class of PTM tailoring enzymes, thereby facilitating the (bio)synthesis of butremycin.
authors.affiliation: Biosystems Chemistry, Department of Chemistry and Center for Integrated Protein Science Munich (CIPSM), Technische Universität München, Lichtenbergstraße 4, 85747 Garching, Germany. tobias.gulder@ch.tum.de.
authors.forename: Christian
authors.initials: C
authors.lastname: Greunke
authors.forename: Janine
authors.initials: J
authors.lastname: Antosch
authors.forename: Tobias A M
authors.initials: TA
authors.lastname: Gulder
mesh_terms: D007769:Lactams / Q000737:chemistry / Q000378:metabolism*; D047029:Lactams, Macrocyclic / Q000737:chemistry / Q000378:metabolism*; D006899:Mixed Function Oxygenases / Q000737:chemistry / Q000378:metabolism*; D008968:Molecular Conformation; D011084:Polycyclic Aromatic Hydrocarbons / Q000737:chemistry / Q000378:metabolism*
chemical_list: D007769:Lactams; D047029:Lactams, Macrocyclic; D011084:Polycyclic Aromatic Hydrocarbons; C000591703:butremycin; C074292:ikarugamycin; D006899:Mixed Function Oxygenases