Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 4.1.99.26 extracted from

  • Bruender, N.A.; Bandarian, V.
    The creatininase homolog MftE from Mycobacterium smegmatis catalyzes a peptide cleavage reaction in the biosynthesis of a novel ribosomally synthesized post-translationally modified peptide (RiPP) (2017), J. Biol. Chem., 292, 4371-4381 .
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
MftB the putative radical SAM enzyme, MftC, oxidatively decarboxylates the C-terminus of the MftA peptide in the presence of the accessory protein MftB. MftB may be playing a role analogous to PqqD by binding the peptide substrate to facilitate binding to the MftC for chemistry Mycolicibacterium smegmatis

Cloned(Commentary)

Cloned (Comment) Organism
gene mftC, recombinant expression of His-tagged enzyme in Escherichia coli strain Bl21(DE3) Mycolicibacterium smegmatis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
C-terminal [mycofactocin precursor peptide]-glycyl-L-valyl-4-[2-aminoethenyl]phenol + S-adenosyl-L-methionine + AH2 Mycolicibacterium smegmatis
-
C-terminal [mycofactocin precursor peptide]-glycyl-3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one + 5'-deoxyadenosine + L-methionine + A
-
?
C-terminal [mycofactocin precursor peptide]-glycyl-L-valyl-4-[2-aminoethenyl]phenol + S-adenosyl-L-methionine + AH2 Mycolicibacterium smegmatis ATCC 700084
-
C-terminal [mycofactocin precursor peptide]-glycyl-3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one + 5'-deoxyadenosine + L-methionine + A
-
?

Organism

Organism UniProt Comment Textmining
Mycolicibacterium smegmatis A0QSB8
-
-
Mycolicibacterium smegmatis ATCC 700084 A0QSB8
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme from Escherichia coli strain Bl21(DE3) by nickel affinity chromatography to near homogeneity/over 95% purity Mycolicibacterium smegmatis

Reaction

Reaction Comment Organism Reaction ID
C-terminal [mycofactocin precursor peptide]-glycyl-3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one + 5'-deoxyadenosine + L-methionine + A = C-terminal [mycofactocin precursor peptide]-glycyl-L-valyl-4-[2-aminoethenyl]phenol + S-adenosyl-L-methionine + AH2 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. One can envision at least two plausible routes both ending with the oxidative decarboxylation of the C-terminus. The top pathway shows 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 radical-COOH species that can either be quenched to formate or CO2 Mycolicibacterium smegmatis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
C-terminal [mycofactocin precursor peptide]-glycyl-L-valyl-4-[2-aminoethenyl]phenol + S-adenosyl-L-methionine + AH2
-
Mycolicibacterium smegmatis C-terminal [mycofactocin precursor peptide]-glycyl-3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one + 5'-deoxyadenosine + L-methionine + A
-
?
C-terminal [mycofactocin precursor peptide]-glycyl-L-valyl-4-[2-aminoethenyl]phenol + S-adenosyl-L-methionine + AH2 MftC catalyzes a radical-mediated oxidative decarboxylation of the C-terminal Tyr 30 in MftA and requires the presence of MftB Mycolicibacterium smegmatis C-terminal [mycofactocin precursor peptide]-glycyl-3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one + 5'-deoxyadenosine + L-methionine + A
-
?
C-terminal [mycofactocin precursor peptide]-glycyl-L-valyl-4-[2-aminoethenyl]phenol + S-adenosyl-L-methionine + AH2
-
Mycolicibacterium smegmatis ATCC 700084 C-terminal [mycofactocin precursor peptide]-glycyl-3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one + 5'-deoxyadenosine + L-methionine + A
-
?
C-terminal [mycofactocin precursor peptide]-glycyl-L-valyl-4-[2-aminoethenyl]phenol + S-adenosyl-L-methionine + AH2 MftC catalyzes a radical-mediated oxidative decarboxylation of the C-terminal Tyr 30 in MftA and requires the presence of MftB Mycolicibacterium smegmatis ATCC 700084 C-terminal [mycofactocin precursor peptide]-glycyl-3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one + 5'-deoxyadenosine + L-methionine + A
-
?

Synonyms

Synonyms Comment Organism
mftC
-
Mycolicibacterium smegmatis
mycofactocin maturase
-
Mycolicibacterium smegmatis

Cofactor

Cofactor Comment Organism Structure
Fe-S cluster the enzyme contains several iron-sulfur clusters. Iron and sulfide analyses show that purified and reconstituted protein contains 10.8 mol of iron and 7.4 mol of sulfide per mol of MftC Mycolicibacterium smegmatis
S-adenosyl-L-methionine
-
Mycolicibacterium smegmatis
[4Fe-4S] cluster
-
Mycolicibacterium smegmatis

General Information

General Information Comment Organism
evolution enzyme MftC is a member of the radical S-adenosyl-L-methionine (SAM) superfamily, based on the presence of the CxxxCxxC motif Mycolicibacterium smegmatis
metabolism the MftA peptide belongs to the ribosomally-synthesized post-translationally modified peptides, RiPPs, that are encoded in the genomes of a wide variety of microorganisms. The mature RiPPs are derived from a precursor peptide, which is encoded by an orf in the genome, that is often extensively modified post-translationally. Interestingly, the orfs encoding for the modification enzymes are often clustered near the orf encoding for the precursor peptide in the genome of many RiPP producing organisms. Bioinformatic analysis shows that three of the orfs (mftA, mftB, and mftC) are clustered in at least 336 genomes (based on the interpro family IPR023850 for the mftB gene product MftB) Mycolicibacterium smegmatis
physiological function the putative radical SAM enzyme, MftC, oxidatively decarboxylates the C-terminus of the MftA peptide in the presence of the accessory protein MftB. The MftA peptide belongs to the ribosomally-synthesized post-translationally modified peptides, RiPPs, that are encoded in the genomes of a wide variety of microorganisms, in close proximity to orfs that encode enzymes which carry out extensive modifications. Members of the radical S-adenosyl-L-methionine (SAM) superfamily have been identified in these biosynthetic clusters Mycolicibacterium smegmatis