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

Nathan A. Bruender, Vahe Bandarian

Research output: Contribution to journalArticle

25 Citations (Scopus)

Abstract

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.

Original languageEnglish (US)
Pages (from-to)2813-2816
Number of pages4
JournalBiochemistry
Volume55
Issue number20
DOIs
StatePublished - May 24 2016
Externally publishedYes

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Decarboxylation
Methionine
Peptides
Enzymes
Accessories
Microorganisms
Open Reading Frames
Genes
Genome
Proteins

ASJC Scopus subject areas

  • Biochemistry

Cite this

The Radical S-Adenosyl- l -methionine Enzyme MftC Catalyzes an Oxidative Decarboxylation of the C-Terminus of the MftA Peptide. / Bruender, Nathan A.; Bandarian, Vahe.

In: Biochemistry, Vol. 55, No. 20, 24.05.2016, p. 2813-2816.

Research output: Contribution to journalArticle

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