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Literature summary for 1.3.98.7 extracted from

  • Bruender, N.A.; Bandarian, V.
    The radical S-adenosyl-L-methionine enzyme MftC catalyzes an oxidative decarboxylation of the C-terminus of the MftA peptide (2016), Biochemistry, 55, 2813-2816 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.3.98.7

Cloned(Commentary)

Cloned (Comment) Organism
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 Mycolicibacterium smegmatis

Metals/Ions

Metals/Ions Comment Organism Structure
Iron purified and reconstituted protein contains 10.8 mol of iron and 7.4 mol of sulfide per mol of MftC Mycolicibacterium smegmatis

Organism

Organism UniProt Comment Textmining
Mycolicibacterium smegmatis A0QSB8 cf. EC 4.1.99.26
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Mycolicibacterium smegmatis ATCC 700084 A0QSB8 cf. EC 4.1.99.26
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Purification (Commentary)

Purification (Comment) Organism
recombinant protein, anaerobically purified using a N-terminal His6-tag. Enzyme is brown in color Mycolicibacterium smegmatis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
C-terminal [mycofactocin precursor peptide]-glycyl-L-valyl-L-tyrosine + S-adenosyl-L-methionine
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 Mycolicibacterium smegmatis C-terminal [mycofactocin precursor peptide]-glycyl-L-valyl-4-[2-aminoethenyl]phenol + CO2 + 5'-deoxyadenosine + L-methionine
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 ?
C-terminal [mycofactocin precursor peptide]-glycyl-L-valyl-L-tyrosine + S-adenosyl-L-methionine
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 Mycolicibacterium smegmatis ATCC 700084 C-terminal [mycofactocin precursor peptide]-glycyl-L-valyl-4-[2-aminoethenyl]phenol + CO2 + 5'-deoxyadenosine + L-methionine
-
 ?

Synonyms

Synonyms Comment Organism
MtfC
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 Mycolicibacterium smegmatis

General Information

General Information Comment Organism
physiological function MtfC is a radical SAM enzyme and oxidatively decarboxylates the C-terminus of the MftA peptide in the presence of the accessory protein MftB. MftC abstracts a hydrogen atom from the beta-carbon of the C-terminal Tyr residue. The resulting radical species is stabilized by the adjacent phenol ring. Decarboxylation occurs either via transfer of the unpaired spin from the radical intermediate to a [4Fe-4S] cluster concomitant with decarboxylation to form the final product. Alternatively, the Calpha-COOH bond can be homolytically cleaved resulting in the formation of a COOH radical species that can either be quenched to formate or CO2 Mycolicibacterium smegmatis