Promiscuous hydroxylases for the functionalization of polycyclic tetramate macrolactams--conversion of ikarugamycin to butremycin

Christian Greunke; Janine Antosch; Tobias A M Gulder

doi:10.1039/c5cc00843c

Promiscuous hydroxylases for the functionalization of polycyclic tetramate macrolactams--conversion of ikarugamycin to butremycin

Chem Commun (Camb). 2015 Mar 28;51(25):5334-6. doi: 10.1039/c5cc00843c.

Authors

Christian Greunke¹, Janine Antosch, Tobias A M Gulder

Affiliation

¹ 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.

PMID: 25711294
DOI: 10.1039/c5cc00843c

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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Lactams / chemistry
Lactams / metabolism*
Lactams, Macrocyclic / chemistry
Lactams, Macrocyclic / metabolism*
Mixed Function Oxygenases / chemistry
Mixed Function Oxygenases / metabolism*
Molecular Conformation
Polycyclic Aromatic Hydrocarbons / chemistry
Polycyclic Aromatic Hydrocarbons / metabolism*

Substances

Lactams
Lactams, Macrocyclic
Polycyclic Aromatic Hydrocarbons
butremycin
ikarugamycin
Mixed Function Oxygenases