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Mycofactocin biosynthesis: modification of the peptide MftA by the radical S‐adenosylmethionine protein MftC
Author(s) -
Khaliullin Bulat,
Aggarwal Priyanka,
Bubas Michael,
Eaton Gareth R.,
Eaton Sandra S.,
Latham John A.
Publication year - 2016
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.12249
Subject(s) - biosynthesis , chemistry , peptide , biochemistry , protein biosynthesis , peptide synthesis , stereochemistry , enzyme
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 K D (~ 100 n m ) and MftC with a low micromolar K D (~ 2 μ m ). 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.