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Literature summary 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

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.3.98.7
-
 Mycolicibacterium smegmatis
4.1.99.26
-
 Mycolicibacterium smegmatis

Metals/Ions

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

Organism

EC Number Organism UniProt Comment Textmining
1.3.98.7 Mycolicibacterium smegmatis A0QSB8 cf. EC 4.1.99.26
-
1.3.98.7 Mycolicibacterium smegmatis ATCC 700084 A0QSB8 cf. EC 4.1.99.26
-
4.1.99.26 Mycolicibacterium smegmatis A0QSB8 cf. EC 1.3.98.7
-
4.1.99.26 Mycolicibacterium smegmatis ATCC 700084 A0QSB8 cf. EC 1.3.98.7
-

Purification (Commentary)

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.3.98.7 C-terminal [mycofactocin precursor peptide]-glycyl-L-valyl-L-tyrosine + S-adenosyl-L-methionine
-
 Mycolicibacterium smegmatis C-terminal [mycofactocin precursor peptide]-glycyl-L-valyl-4-[2-aminoethenyl]phenol + CO2 + 5'-deoxyadenosine + L-methionine
-
 ?
1.3.98.7 C-terminal [mycofactocin precursor peptide]-glycyl-L-valyl-L-tyrosine + S-adenosyl-L-methionine
-
 Mycolicibacterium smegmatis ATCC 700084 C-terminal [mycofactocin precursor peptide]-glycyl-L-valyl-4-[2-aminoethenyl]phenol + CO2 + 5'-deoxyadenosine + L-methionine
-
 ?
4.1.99.26 additional information in the absence of chaperone MtfB, MftC catalyzes the reductive cleavage of SAM Mycolicibacterium smegmatis ?
-
-
4.1.99.26 additional information in the absence of chaperone MtfB, MftC catalyzes the reductive cleavage of SAM Mycolicibacterium smegmatis ATCC 700084 ?
-
-

Synonyms

EC Number Synonyms Comment Organism
1.3.98.7 MtfC
-
 Mycolicibacterium smegmatis
4.1.99.26 MtfC
-
 Mycolicibacterium smegmatis

General Information

EC Number General Information Comment Organism
1.3.98.7 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