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FEBS Lett. 2016 Aug;590(16):2538-48. doi: 10.1002/1873-3468.12249. Epub 2016 Jun 29.

Mycofactocin biosynthesis: modification of the peptide MftA by the radical S-adenosylmethionine protein MftC.

Author information

1
Department of Chemistry and Biochemistry, University of Denver, CO, USA.

Abstract

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.

KEYWORDS:

mycofactocin; peptide interaction; radical S-adenosylmethionine

PMID:
27312813
DOI:
10.1002/1873-3468.12249
[Indexed for MEDLINE]
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