Mycofactocin Biosynthesis: Modification of the Peptide MftA by the Radical S-adenosylmethionine Protein MftC
Mycofactocin, Peptide interaction, Radical S‐adenosylmethionine
College of Natual Science and Mathematics, Chemistry and Biochemistry
Mycofactocin is a putative, peptide derived, cofactor that is associated primarily with the Mycobacterium genera including the pathogen M. tuberculosis. The pathway consists of the three genes mftA, mftB, and mftC that encode for the peptide substrate, peptide chaperone, and a radical S‐adenosylmethionine protein (RS), respectively. Here, we show that the MftB acts as a peptide chaperone, binding MftA with a submicromolar KD (~ 100 nm) and MftC with a low micromolar KD (~ 2 μm). Moreover, we demonstrate that MftC is a radical S‐adenosylmethionine (SAM) enzyme. Finally, we show that MftC catalyzes the oxidative decarboxylation of the peptide MftA.
Copyright held by author or publisher. User is responsible for all copyright compliance.
Khaliullin, B., Aggarwal, P., Bubas, M., Eaton, G. R., Eaton, S. S., & Latham, J. A. (2016). Mycofactocin biosynthesis: Modification of the peptide MftA by the radical S-adenosylmethionine protein MftC. FEBS Letters, 590(16), 2538-2548. DOI: 10.1002/1873-3468.12249.