The Radical S-Adenosyl-l-methionine Enzyme MftC Catalyzes an Oxidative Decarboxylation of the C-Terminus of the MftA Peptide

Biochemistry. 2016 May 24;55(20):2813-6. doi: 10.1021/acs.biochem.6b00355. Epub 2016 May 13.


Ribosomally synthesized post-translationally modified peptides (RiPPs) are encoded in the genomes of a wide variety of microorganisms, in the proximity of open reading frames that encode enzymes that conduct extensive modifications, many of which are novel. Recently, members of the radical S-adenosyl-l-methionine (SAM) superfamily have been identified in these biosynthetic clusters. Herein, we demonstrate the putative radical SAM enzyme, MftC, oxidatively decarboxylates the C-terminus of the MftA peptide in the presence of the accessory protein MftB. The reaction catalyzed by MftC expands the repertoire of peptide-based radical SAM chemistry beyond the intramolecular cross-links.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Adenosylmethionine Decarboxylase / chemistry*
  • Adenosylmethionine Decarboxylase / genetics
  • Adenosylmethionine Decarboxylase / metabolism
  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism
  • Mycobacterium smegmatis / chemistry*
  • Mycobacterium smegmatis / genetics
  • Mycobacterium smegmatis / metabolism
  • Oxidation-Reduction
  • Peptides / chemistry*
  • Peptides / genetics
  • Peptides / metabolism


  • Bacterial Proteins
  • Peptides
  • Adenosylmethionine Decarboxylase