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Information on EC 4.1.99.26 - 3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one synthase
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4.1.99.26 3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one synthaseIUBMB Comments
This is a bifunctional radical AdoMet (radical SAM) enzyme that catalyses the first two steps in the biosynthesis of the enzyme cofactor mycofactocin. Activity requires the presence of the MftB chaperone. The reaction occurs in the right-to-left direction. The other activity of the enzyme is EC 1.3.98.7, [mycofactocin precursor peptide]-tyrosine decarboxylase.
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The expected taxonomic range for this enzyme is: Mycobacteriaceae
Reaction Schemes
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C-terminal [mycofactocin precursor peptide]-glycyl-3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one
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C-terminal [mycofactocin precursor peptide]-glycyl-L-valyl-4-[2-aminoethenyl]phenol
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Synonyms
mftC, MtfC, mycofactocin biosynthetic protein, mycofactocin maturase, mycofactocin-biosynthetic radical S-adenosylmethionine protein, Rv0693, [mycofactocin precursor peptide]-pyrrolidinone derivative synthase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
mftC
MtfC
mycofactocin maturase
mycofactocin-biosynthetic radical S-adenosylmethionine protein
[mycofactocin precursor peptide]-pyrrolidinone derivative synthase
UniProt
mftC
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mycofactocin-biosynthetic radical S-adenosylmethionine protein
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mycofactocin-biosynthetic radical S-adenosylmethionine protein
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
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
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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
enzyme mechanism, detailed overview. MftC catalyzes the formation of two products from substrate MftA, 13C NMR and 1H NMR analysis of substrate, intermediates and products. The major product of the MftC reaction is a Val-Tyr* crosslinked peptide formed through two S-adenosylmethionine-dependent turnovers. The hydroxyl group on MftA Tyr30 is required for MftC catalysis
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
enzyme mechanism, overview
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
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
enzyme mechanism, overview
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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
enzyme mechanism, detailed overview. MftC catalyzes the formation of two products from substrate MftA, 13C NMR and 1H NMR analysis of substrate, intermediates and products. The major product of the MftC reaction is a Val-Tyr* crosslinked peptide formed through two S-adenosylmethionine-dependent turnovers. The hydroxyl group on MftA Tyr30 is required for MftC catalysis
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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
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C-C bond formation
oxidative decarboxylation
additional information
additional information
enzyme MftC catalyzes two distinct chemistries in the same active, an oxidative decarboxylation of the C-terminus and a subsequent redox neutral C-C bond formation
additional information
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enzyme MftC catalyzes two distinct chemistries in the same active, an oxidative decarboxylation of the C-terminus and a subsequent redox neutral C-C bond formation
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
C-terminal [mycofactocin precursor peptide]-glycyl-3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one lyase (C-terminal [mycofactocin precursor peptide]-glycyl-L-valyl-4-[2-aminoethenyl]phenol-forming)
This is a bifunctional radical AdoMet (radical SAM) enzyme that catalyses the first two steps in the biosynthesis of the enzyme cofactor mycofactocin. Activity requires the presence of the MftB chaperone. The reaction occurs in the right-to-left direction. The other activity of the enzyme is EC 1.3.98.7, [mycofactocin precursor peptide]-tyrosine decarboxylase.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
C-terminal [mycofactocin precursor peptide MftA]-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
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C-terminal [mycofactocin precursor peptide]-glycyl-L-valyl-4-[2-aminoethenyl]phenol + S-adenosyl-L-methionine + AH2
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
C-terminal [mycofactocin precursor peptide]-glycyl-3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one + 5'-deoxyadenosine + L-methionine + A
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C-terminal [mycofactocin precursor peptide]-glycyl-L-valyl-4-[2-aminoethenyl]phenol + S-adenosyl-L-methionine + AH2
C-terminal [mycofactocin precursor peptide]-glycyl-3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one + 5'-deoxyadenosine + L-methionine + A
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C-terminal [mycofactocin precursor peptide]-glycyl-L-valyl-4-[2-aminoethenyl]phenol + S-adenosyl-L-methionine + AH2
C-terminal [mycofactocin precursor peptide]-glycyl-3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one + 5'-deoxyadenosine + L-methionine + A
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C-terminal [mycofactocin precursor peptide]-glycyl-L-valyl-4-[2-aminoethenyl]phenol + S-adenosyl-L-methionine + AH2
C-terminal [mycofactocin precursor peptide]-glycyl-3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one + 5'-deoxyadenosine + L-methionine + A
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C-terminal [mycofactocin precursor peptide]-glycyl-L-valyl-4-[2-aminoethenyl]phenol + S-adenosyl-L-methionine + AH2
C-terminal [mycofactocin precursor peptide]-glycyl-3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one + 5'-deoxyadenosine + L-methionine + A
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C-terminal [mycofactocin precursor peptide]-glycyl-L-valyl-4-[2-aminoethenyl]phenol + S-adenosyl-L-methionine + AH2
C-terminal [mycofactocin precursor peptide]-glycyl-3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one + 5'-deoxyadenosine + L-methionine + A
enzyme MftC catalyzes the oxidative decarboxylation of the C-terminal tyrosine (Tyr30) on the mycofactocin precursor peptide MftA. MftC catalyzes the formation of two MftA products annotated as MftA* and MftA**. The MftAM1W variant is used to increase the spectroscopic handle at 280 nm. The major product, MftA*, is a tyramine-valine-cross-linked peptide formed by MftC through two S-adenosylmethionine-dependent turnovers. In case of the reaction containing MftA M1W/V29A, HPLC analysis shows a a minor peak for MftA M1W/V29A* (10%) and a major peak for MftA M1W/V29A**. Substitution in the penultimate MftA Val29 position causes the accumulation of an MftA** minor product. The 1H-NMR spectrum indicates that this minor product contains an alpha/beta-unsaturated bond that likely arises from an aborted intermediate of MftA* synthesis
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C-terminal [mycofactocin precursor peptide]-glycyl-L-valyl-4-[2-aminoethenyl]phenol + S-adenosyl-L-methionine + AH2
C-terminal [mycofactocin precursor peptide]-glycyl-3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one + 5'-deoxyadenosine + L-methionine + A
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?
C-terminal [mycofactocin precursor peptide]-glycyl-L-valyl-4-[2-aminoethenyl]phenol + S-adenosyl-L-methionine + AH2
C-terminal [mycofactocin precursor peptide]-glycyl-3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one + 5'-deoxyadenosine + L-methionine + A
enzyme MftC catalyzes the oxidative decarboxylation of the C-terminal tyrosine (Tyr30) on the mycofactocin precursor peptide MftA. MftC catalyzes the formation of two MftA products annotated as MftA* and MftA**. The MftAM1W variant is used to increase the spectroscopic handle at 280 nm. The major product, MftA*, is a tyramine-valine-cross-linked peptide formed by MftC through two S-adenosylmethionine-dependent turnovers. In case of the reaction containing MftA M1W/V29A, HPLC analysis shows a a minor peak for MftA M1W/V29A* (10%) and a major peak for MftA M1W/V29A**. Substitution in the penultimate MftA Val29 position causes the accumulation of an MftA** minor product. The 1H-NMR spectrum indicates that this minor product contains an alpha/beta-unsaturated bond that likely arises from an aborted intermediate of MftA* synthesis
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C-terminal [mycofactocin precursor peptide]-glycyl-L-valyl-4-[2-aminoethenyl]phenol + S-adenosyl-L-methionine + AH2
C-terminal [mycofactocin precursor peptide]-glycyl-3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one + 5'-deoxyadenosine + L-methionine + A
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C-terminal [mycofactocin precursor peptide]-glycyl-L-valyl-4-[2-aminoethenyl]phenol + S-adenosyl-L-methionine + AH2
C-terminal [mycofactocin precursor peptide]-glycyl-3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one + 5'-deoxyadenosine + L-methionine + A
MftC catalyzes a radical-mediated oxidative decarboxylation of the C-terminal Tyr 30 in MftA and requires the presence of MftB
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C-terminal [mycofactocin precursor peptide]-glycyl-L-valyl-4-[2-aminoethenyl]phenol + S-adenosyl-L-methionine + AH2
C-terminal [mycofactocin precursor peptide]-glycyl-3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one + 5'-deoxyadenosine + L-methionine + A
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C-terminal [mycofactocin precursor peptide]-glycyl-L-valyl-4-[2-aminoethenyl]phenol + S-adenosyl-L-methionine + AH2
C-terminal [mycofactocin precursor peptide]-glycyl-3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one + 5'-deoxyadenosine + L-methionine + A
MftC catalyzes a radical-mediated oxidative decarboxylation of the C-terminal Tyr 30 in MftA and requires the presence of MftB
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additional information
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MftC reductively cleaves SAM to form a 5'-deoxyadenosine radical which in turn abstracts a hydrogen from the Cbeta of the C-terminal tyrosine. Following a subsequent abstraction of an electron from the substrate and the loss of the C-terminal carboxylate a new alpha/beta unsaturated bond is formed on the intermediate MftA**. In the next step of MftC catalysis, a second 5'-deoxyadenosine radical abstracts a hydrogen from the Cbeta of the penultimate valine residue. The Cbeta radical on the valine side chain forms a new bond with the sp2 hybridized C2 of the p-(2-aminoethenyl)phenol. As a result, the product from MftC catalysis, MftA*, contains a C-terminal 3-amino-5-[(p-hydroxyphenyl) methyl]-4,4-dimethyl-2-pyrrolidinone moiety
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additional information
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Rv0693 likely targets a small peptide for modification
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additional information
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Rv0693 likely targets a small peptide for modification
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additional information
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Rv0693 likely targets a small peptide for modification
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additional information
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enzyme additionally catalyzes the reaction of MftA peptide to MftA carrying the alpha/beta unsaturated bond, i.e. MftA**, reaction of EC 1.3.98.7
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additional information
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MftC catalyzes the cleavage of SAM to form dAdo and it converts MftA to MftA*
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additional information
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site-directed mutagenesis of MftA Tyr30 indicates that a labile proton is required for catalysis. SUbstrate mutants used are MftA M1W, MftA M1W/Y30F, MftA M1W/Y30S, and MftA M1W/Y30W
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additional information
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enzyme additionally catalyzes the reaction of MftA peptide to MftA carrying the alpha/beta unsaturated bond, i.e. MftA**, reaction of EC 1.3.98.7
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additional information
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site-directed mutagenesis of MftA Tyr30 indicates that a labile proton is required for catalysis. SUbstrate mutants used are MftA M1W, MftA M1W/Y30F, MftA M1W/Y30S, and MftA M1W/Y30W
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additional information
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in the absence of chaperone MtfB, MftC catalyzes the reductive cleavage of SAM
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additional information
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in the absence of chaperone MtfB, MftC catalyzes the reductive cleavage of SAM
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
C-terminal [mycofactocin precursor peptide MftA]-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
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?
C-terminal [mycofactocin precursor peptide]-glycyl-L-valyl-4-[2-aminoethenyl]phenol + S-adenosyl-L-methionine + AH2
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
C-terminal [mycofactocin precursor peptide]-glycyl-3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one + 5'-deoxyadenosine + L-methionine + A
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C-terminal [mycofactocin precursor peptide]-glycyl-L-valyl-4-[2-aminoethenyl]phenol + S-adenosyl-L-methionine + AH2
C-terminal [mycofactocin precursor peptide]-glycyl-3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one + 5'-deoxyadenosine + L-methionine + A
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C-terminal [mycofactocin precursor peptide]-glycyl-L-valyl-4-[2-aminoethenyl]phenol + S-adenosyl-L-methionine + AH2
C-terminal [mycofactocin precursor peptide]-glycyl-3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one + 5'-deoxyadenosine + L-methionine + A
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C-terminal [mycofactocin precursor peptide]-glycyl-L-valyl-4-[2-aminoethenyl]phenol + S-adenosyl-L-methionine + AH2
C-terminal [mycofactocin precursor peptide]-glycyl-3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one + 5'-deoxyadenosine + L-methionine + A
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C-terminal [mycofactocin precursor peptide]-glycyl-L-valyl-4-[2-aminoethenyl]phenol + S-adenosyl-L-methionine + AH2
C-terminal [mycofactocin precursor peptide]-glycyl-3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one + 5'-deoxyadenosine + L-methionine + A
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C-terminal [mycofactocin precursor peptide]-glycyl-L-valyl-4-[2-aminoethenyl]phenol + S-adenosyl-L-methionine + AH2
C-terminal [mycofactocin precursor peptide]-glycyl-3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one + 5'-deoxyadenosine + L-methionine + A
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?
C-terminal [mycofactocin precursor peptide]-glycyl-L-valyl-4-[2-aminoethenyl]phenol + S-adenosyl-L-methionine + AH2
C-terminal [mycofactocin precursor peptide]-glycyl-3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one + 5'-deoxyadenosine + L-methionine + A
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?
C-terminal [mycofactocin precursor peptide]-glycyl-L-valyl-4-[2-aminoethenyl]phenol + S-adenosyl-L-methionine + AH2
C-terminal [mycofactocin precursor peptide]-glycyl-3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one + 5'-deoxyadenosine + L-methionine + A
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?
additional information
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enzyme additionally catalyzes the reaction of MftA peptide to MftA carrying the alpha/beta unsaturated bond, i.e. MftA**, reaction of EC 1.3.98.7
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additional information
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enzyme additionally catalyzes the reaction of MftA peptide to MftA carrying the alpha/beta unsaturated bond, i.e. MftA**, reaction of EC 1.3.98.7
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
[4Fe-4S]-center
MftC binds a radical S-adenosylmethionine [4Fe-4S] cluster and two auxiliary [4Fe-4S] clusters that are required for MftA modification. Presence of S-adenosylmethionine and MftA affects the environments of the radical S-adenosylmethionine and Aux I cluster whereas the Aux II cluster is unaffected by the substrates. All three cluster are required for cataylsis
S-adenosyl-L-methionine
MftC utilizes 2 eq of SAM to crosslink Tyr30 and Val29
S-adenosyl-L-methionine
MtfC is a radical S-adenosylmethionine (RS, SAM) protein
S-adenosyl-L-methionine
residues Cys30, 34, and 37 are the radical S-adenosylmethionine ligands
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
in a [4Fe-4S] clusters, all three [Fe-S] clusters are required for MftC modification of substrate MftA
Iron
purified and reconstituted protein contains 10.8 mol of iron and 7.4 mol of sulfide per mol of MftC
additional information
iron and sulfur quantification, identification of conserved cysteines in MftC, overview
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
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architecture and distribution of the mycofactocin biosynthetic cluster, mftABCDEF, among the Actinobacteria phylum, overview. MftC belongs to a RS enzyme subfamily that contains an elongated C-terminal domain annotated as a SPASM domain, members are subtilosin A, pyrroloquinoline quinone, anaerobic sulfatase maturating enzyme, and mycofactocin. PqqE and MftC belong to a select group of RS-SPASM proteins that have been shown to form carbon-carbon bonds on their respective precursor peptide. The proteins associated with the RS-SPASM subfamily are known peptide modifiers that have been shown to catalyze intramolecular C-S bonds and C-C bonds and oxidative decarboxylation reactions on the precursor peptide. The mft cluster is evenly distributed in the genomes of both slow and rapid growing mycobacteria including notable species such as Mycobacterium tuberculosis, Mycobacterium avium, Mycobacterium bovis, Mycobacterium abscessus, Mycobacterium kansasii, Mycobacterium smegmatis, Mycobacterium ulcerans, Mycobacterium marinum, and Mycobacterium vanbaalenii. The average sequence identity of all MftC proteins within the Mycobacterium genus to the Mycobacterium tuberculosis strain H37Rv (Mtb) MftC is as high as 89%. Within the Actinobacteria phylum, the average sequence identity of MftC proteins to that of Mtb MftC remains quite high in genera such as Rhodococcus (79%), Nocardia (77%), Gordonia (79%), and Streptomyces (74%). But the sequence identity of MftC outside of the Actinobacteria undergoes a significant drop-off with averages in a range of 42% to 59%
evolution
enzyme MftC is a member of the radical S-adenosyl-L-methionine (SAM) superfamily, based on the presence of the CxxxCxxC motif
evolution
MftC belongs to a subfamily of RS proteins that contain an about 100-amino acid C-terminal domain annotated as a SPASM domain, named after subtilosin A, pyrroloquinoline quinone, anaerobic sulfatase maturating enzyme, and mycofactocin
evolution
the enzyme belongs to a subset of the RS proteins that modify peptides belong to the SPASM subfamily (subtilosin A, pyrroloquinoline quinone, anaerobic sulfatase maturating enzyme, and mycofactocin) and are annotated as RS-SPASM proteins. RS-SPASM proteins are comprised of a prototypical TIM barrel fold which binds the RS [4Fe-4S] cluster involved in the homolytic cleavage of S-adenosylmethionine (SAM). In addition, they contain an elongated C-terminal SPASM domain which binds up to two additional auxiliary [Fe-S] clusters. The cluster proximal to the RS cluster (annotated as Aux I) is typically a [4Fe-4S] (with the exception of PqqE in which a [2Fe-2S] cluster is reported) and the distal cluster (designated as Aux II) is a [4Fe-4S] cluster. MftC is a RS-SPASM enzyme that performs the first modifying step in the biosynthesis of the ribosomally synthesized and post-translationally modified peptide (RiPP), mycofactocin. The ability of MftC to redox-flip, or accommodate both oxidative to redox neutral reactions, is certainly unique to the RS-SPASM subfamily. The Aux I and Aux II clusters are required for catalysis, consistent with results shown for QhpD, AnSME, SCIFF, and PqqE
evolution
the enzyme belongs to the PqqE-like rSAM protein family, part of the radical SAM domain superfamily. Members occur clustered with a well-conserved small polypeptide mycofactocin, similar in size to bacteriocins and PqqA, precursor of pyrroloquinoline quinone (PQQ). Partial phylogenetic profiling identifies the mycofactocin cluster. The mycofactocin precursor is modified by the gene Rv0693 family rSAM protein and other enzymes in its cluster. Rv0693 belongs to a branch of the radical SAM family in which known or presumed substrates are short peptides. The Rv0693 family radical SAM protein modifies the TIGR03969 family peptide to produce a bioactive molecule: a bacteriocin, a redox cofactor like PQQ, or a signaling metabolite such as Pep1357. The neighboring glycosyltransferase (Rv0696) likely also participates. Based on its near universal distribution in the genus Mycobacterium (among many other Actinobacteria), and analogy of its biosynthesis cluster to PQQ cofactor and bacteriocin biosynthesis clusters, the name mycofactocin is proposed for members of this family. Additional protein families co-cluster with the mycofactocin precursor, mycofactocin cluster-containing genomes and linked oxidoreductases, detailed overview
evolution
-
the enzyme belongs to a subset of the RS proteins that modify peptides belong to the SPASM subfamily (subtilosin A, pyrroloquinoline quinone, anaerobic sulfatase maturating enzyme, and mycofactocin) and are annotated as RS-SPASM proteins. RS-SPASM proteins are comprised of a prototypical TIM barrel fold which binds the RS [4Fe-4S] cluster involved in the homolytic cleavage of S-adenosylmethionine (SAM). In addition, they contain an elongated C-terminal SPASM domain which binds up to two additional auxiliary [Fe-S] clusters. The cluster proximal to the RS cluster (annotated as Aux I) is typically a [4Fe-4S] (with the exception of PqqE in which a [2Fe-2S] cluster is reported) and the distal cluster (designated as Aux II) is a [4Fe-4S] cluster. MftC is a RS-SPASM enzyme that performs the first modifying step in the biosynthesis of the ribosomally synthesized and post-translationally modified peptide (RiPP), mycofactocin. The ability of MftC to redox-flip, or accommodate both oxidative to redox neutral reactions, is certainly unique to the RS-SPASM subfamily. The Aux I and Aux II clusters are required for catalysis, consistent with results shown for QhpD, AnSME, SCIFF, and PqqE
-
evolution
-
MftC belongs to a subfamily of RS proteins that contain an about 100-amino acid C-terminal domain annotated as a SPASM domain, named after subtilosin A, pyrroloquinoline quinone, anaerobic sulfatase maturating enzyme, and mycofactocin
-
evolution
-
enzyme MftC is a member of the radical S-adenosyl-L-methionine (SAM) superfamily, based on the presence of the CxxxCxxC motif
-
evolution
-
the enzyme belongs to the PqqE-like rSAM protein family, part of the radical SAM domain superfamily. Members occur clustered with a well-conserved small polypeptide mycofactocin, similar in size to bacteriocins and PqqA, precursor of pyrroloquinoline quinone (PQQ). Partial phylogenetic profiling identifies the mycofactocin cluster. The mycofactocin precursor is modified by the gene Rv0693 family rSAM protein and other enzymes in its cluster. Rv0693 belongs to a branch of the radical SAM family in which known or presumed substrates are short peptides. The Rv0693 family radical SAM protein modifies the TIGR03969 family peptide to produce a bioactive molecule: a bacteriocin, a redox cofactor like PQQ, or a signaling metabolite such as Pep1357. The neighboring glycosyltransferase (Rv0696) likely also participates. Based on its near universal distribution in the genus Mycobacterium (among many other Actinobacteria), and analogy of its biosynthesis cluster to PQQ cofactor and bacteriocin biosynthesis clusters, the name mycofactocin is proposed for members of this family. Additional protein families co-cluster with the mycofactocin precursor, mycofactocin cluster-containing genomes and linked oxidoreductases, detailed overview
-
evolution
-
the enzyme belongs to the PqqE-like rSAM protein family, part of the radical SAM domain superfamily. Members occur clustered with a well-conserved small polypeptide mycofactocin, similar in size to bacteriocins and PqqA, precursor of pyrroloquinoline quinone (PQQ). Partial phylogenetic profiling identifies the mycofactocin cluster. The mycofactocin precursor is modified by the gene Rv0693 family rSAM protein and other enzymes in its cluster. Rv0693 belongs to a branch of the radical SAM family in which known or presumed substrates are short peptides. The Rv0693 family radical SAM protein modifies the TIGR03969 family peptide to produce a bioactive molecule: a bacteriocin, a redox cofactor like PQQ, or a signaling metabolite such as Pep1357. The neighboring glycosyltransferase (Rv0696) likely also participates. Based on its near universal distribution in the genus Mycobacterium (among many other Actinobacteria), and analogy of its biosynthesis cluster to PQQ cofactor and bacteriocin biosynthesis clusters, the name mycofactocin is proposed for members of this family. Additional protein families co-cluster with the mycofactocin precursor, mycofactocin cluster-containing genomes and linked oxidoreductases, detailed overview
-
malfunction
the enzyme knockout (KO) mutant can neither cleave SAM nor modify MftA, consistent with the successful knockout of the RS cluster. Both Aux I and Aux II KO's are capable of catalyzing the reductive cleavage of SAM to form dAdo, suggesting that the RS cluster remains intact and in an active conformation in the mutated proteins. When assayed against MftA, both Aux I and Aux II KO's are incapable of converting MftA to MftA* or MftA**
malfunction
-
the enzyme knockout (KO) mutant can neither cleave SAM nor modify MftA, consistent with the successful knockout of the RS cluster. Both Aux I and Aux II KO's are capable of catalyzing the reductive cleavage of SAM to form dAdo, suggesting that the RS cluster remains intact and in an active conformation in the mutated proteins. When assayed against MftA, both Aux I and Aux II KO's are incapable of converting MftA to MftA* or MftA**
-
metabolism
-
enzyme MftC is active in the mycofactocin biosynthetic pathway. Association and distribution of the mft genes. Potential molecular and physiological role of mycofactocin, and known biosynthetic steps involving MftA, MftB, MftC, and MftE in relation to pyrroloquinoline quinone biosynthesis, function of the remaining putative biosynthetic enzymes, MftD and MftF. Expression of the mycofactocin biosynthetic pathway is controlled by the regulator MftR, a member of the TetR family of regulators (TFRs). MftR is the mycofactocin regulator. In the first step of mycofactocin biosynthesis, MftC reductively cleaves SAM to form a 5'-deoxyadenosine radical which in turn abstracts a hydrogen from the Cbeta of the C-terminal tyrosine. Following a subsequent abstraction of an electron from the substrate and the loss of the C-terminal carboxylate, a new alpha/beta unsaturated bond is formed on the intermediate MftA**. In the next step of MftC catalysis, a second 5'-deoxyadenosine radical abstracts a hydrogen from the Cbeta of the penultimate valine residue. The Cbeta radical on the valine side chain forms a new bond with the sp2 hybridized C2 of the p-(2-aminoethenyl)phenol. As a result, the product from MftC catalysis, MftA*, contains a C-terminal 3-amino-5-[(p-hydroxyphenyl) methyl]-4,4-dimethyl-2-pyrrolidinone moiety
metabolism
following MftC modification, MftE hydrolyzes 3-amino-5-[(p-hydroxyphenyl) methyl]-4,4-dimethyl-2-pyrrolidinone (AHDP) moiety (MftA*) at the valine position, freeing AHDP from the peptide
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)
metabolism
-
following MftC modification, MftE hydrolyzes 3-amino-5-[(p-hydroxyphenyl) methyl]-4,4-dimethyl-2-pyrrolidinone (AHDP) moiety (MftA*) at the valine position, freeing AHDP from the peptide
-
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)
-
physiological function
MftC catalyzes the formation of two isomeric products. The major product, MftA*, is a tyramine-valine-cross-linked peptide formed by MftC through two S-adenosylmethionine-dependent turnovers. The hydroxyl group on MftA Tyr30 is required for MftC catalysis. A substitution in the penultimate substrate MftA Val29 position causes the accumulation of an MftA** minor product which contains an alphabeta-unsaturated bond that likely arises from an aborted intermediate of MftA* synthesis
physiological function
MftC is a RS-SPASM enzyme that performs the first modifying step in the biosynthesis of the ribosomally synthesized and post-translationally modified peptide (RiPP), mycofactocin. The mycofactocin maturase, MftC, is a unique radical S-adenosylmethionine (RS, SAM) protein that catalyzes the oxidative decarboxylation and C-C bond formation on the precursor peptide MftA
physiological function
the enzyme substrate MftA is about 30-60 amino acids in length and contains a conserved C-terminal sequence (-IDGXCGVY). The C-terminus is putatively modified by the remaining gene products to form mycofactocin, which is anticipated to serve as a redox cofactor for other nicotinamide-dependent proteins. MftC is a radical S-adenosyl-L-methionine (RS) protein responsible for the first step of the biosynthesis of mycofactocin. MftC catalyzes the formation of two isomeric MftA products annotated as MftA* and MftA**. And MftC catalyzes the conversion of MftA** to MftA*. MftC catalyzes a diverse array of chemical transformations, catalytic mechanism, overview
physiological function
the mycofactocin precursor is modified by the gene Rv0693 family rSAM protein and other enzymes in its cluster. It becomes an electron carrier molecule that serves in vivo as NDMA and other artificial electron acceptors do in vitro
physiological function
the mycofactocin precursor is modified by the Rv0693 family radical SAM protein and other enzymes in its cluster. It becomes an electron carrier molecule that serves in vivo as N,N-dimethyl-4-nitrosoaniline and other artificial electron acceptors do in vitro
physiological function
-
the protein MftC is a putative radical S-adenosylmethionine (RS) enzyme with low sequence homology to the pyrroloquinoline quinone (PQQ) biosynthetic enzyme PqqE
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
physiological function
-
MftC is a RS-SPASM enzyme that performs the first modifying step in the biosynthesis of the ribosomally synthesized and post-translationally modified peptide (RiPP), mycofactocin. The mycofactocin maturase, MftC, is a unique radical S-adenosylmethionine (RS, SAM) protein that catalyzes the oxidative decarboxylation and C-C bond formation on the precursor peptide MftA
-
physiological function
-
MftC catalyzes the formation of two isomeric products. The major product, MftA*, is a tyramine-valine-cross-linked peptide formed by MftC through two S-adenosylmethionine-dependent turnovers. The hydroxyl group on MftA Tyr30 is required for MftC catalysis. A substitution in the penultimate substrate MftA Val29 position causes the accumulation of an MftA** minor product which contains an alphabeta-unsaturated bond that likely arises from an aborted intermediate of MftA* synthesis
-
physiological function
-
the enzyme substrate MftA is about 30-60 amino acids in length and contains a conserved C-terminal sequence (-IDGXCGVY). The C-terminus is putatively modified by the remaining gene products to form mycofactocin, which is anticipated to serve as a redox cofactor for other nicotinamide-dependent proteins. MftC is a radical S-adenosyl-L-methionine (RS) protein responsible for the first step of the biosynthesis of mycofactocin. MftC catalyzes the formation of two isomeric MftA products annotated as MftA* and MftA**. And MftC catalyzes the conversion of MftA** to MftA*. MftC catalyzes a diverse array of chemical transformations, catalytic mechanism, overview
-
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
-
physiological function
-
the mycofactocin precursor is modified by the gene Rv0693 family rSAM protein and other enzymes in its cluster. It becomes an electron carrier molecule that serves in vivo as NDMA and other artificial electron acceptors do in vitro
-
physiological function
-
the mycofactocin precursor is modified by the Rv0693 family radical SAM protein and other enzymes in its cluster. It becomes an electron carrier molecule that serves in vivo as N,N-dimethyl-4-nitrosoaniline and other artificial electron acceptors do in vitro
-
physiological function
-
the mycofactocin precursor is modified by the gene Rv0693 family rSAM protein and other enzymes in its cluster. It becomes an electron carrier molecule that serves in vivo as NDMA and other artificial electron acceptors do in vitro
-
physiological function
-
the mycofactocin precursor is modified by the Rv0693 family radical SAM protein and other enzymes in its cluster. It becomes an electron carrier molecule that serves in vivo as N,N-dimethyl-4-nitrosoaniline and other artificial electron acceptors do in vitro
-
additional information
MtfC homology structure modelling using the structures of anSME (PDB ID 4K36), CteB (PDB ID 5WHY), or SuiB (PDB ID 5V1T) as templates. Identification of conserved cysteines in MftC, overview. The Aux I and Aux II clusters are required for catalysis
additional information
multiple sequence alignment of gene predictions for mycofactocin precursors, overview
additional information
-
MtfC homology structure modelling using the structures of anSME (PDB ID 4K36), CteB (PDB ID 5WHY), or SuiB (PDB ID 5V1T) as templates. Identification of conserved cysteines in MftC, overview. The Aux I and Aux II clusters are required for catalysis
-
additional information
-
multiple sequence alignment of gene predictions for mycofactocin precursors, overview
-
additional information
-
multiple sequence alignment of gene predictions for mycofactocin precursors, overview
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). MFTC_MYCS2
Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155)
392
0
42378
Swiss-Prot
-
MFTC_MYCTO
Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
391
0
42448
Swiss-Prot
-
MFTC_MYCTU
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
391
0
42448
Swiss-Prot
-
MFTC_MYCUA
Mycobacterium ulcerans (strain Agy99)
369
0
39558
Swiss-Prot
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C251A
C258A
site-directed mutagenesis, the mutant shows no altered phenotype
C269A
C269A/C323A
C30A/C34A/C37A
C30A/C37A
C310A/C341A
C323A
additional information
C269A
auxiliary [4Fe-4S] cluster I mutant, capable of catalyzing the reductive cleavage of SAM to form dAdo but incapable of converting MftA to MftA* or MftA**
C269A
site-directed mutagenesis, an Aux I KO variant mutant, the mutant is soluble
C269A/C323A
site-directed mutagenesis, an Aux I KO variant mutant, the mutant is insoluble
C30A/C37A
radical S-adenosylmethionine mutant, can neither cleave SAM nor modify MftA
C30A/C37A
site-directed mutagenesis, a RS KO variant double mutant
C310A/C341A
auxiliary [4Fe-4S] cluster II mutant, capable of catalyzing the reductive cleavage of SAM to form dAdo, incapable of converting MftA to MftA* or MftA**
C310A/C341A
site-directed mutagenesis, an Aux II KO variant double mutant
C323A
auxiliary [4Fe-4S] cluster I mutant, capable of catalyzing the reductive cleavage of SAM to form dAdo, incapable of converting MftA to MftA* or MftA**
C323A
site-directed mutagenesis, an Aux I KO variant mutant, the mutant is soluble
additional information
EPR analysis of MftC variants with substrate bound providing insight to the function of the [Fe-S] clusters
additional information
systematical replacement of Cys residues by Ala. The RS KO could neither cleave SAM nor modify MftA, consistent with the successful knockout of the RS cluster. Activity assays for Aux I and Aux II KO's also provided insightful results. Both Aux I and Aux II KO's were capable of catalyzing the reductive cleavage of SAM to form dAdo (Figure 3A), suggesting that the RS cluster remained intact and in an active conformation in the mutated proteins. However, when assayed against MftA, both Aux I and Aux II KO's are incapable of converting MftA to MftA* or MftA**
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and ultrafiltration
recombinant His-tagged enzyme from Escherichia coli strain Bl21(DE3) by nickel affinity chromatography to near homogeneity/over 95% purity
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain Bl21(DE3) by nickel affinity chromatography to near homogeneity
recombinant protein, anaerobically purified using a N-terminal His6-tag. Enzyme is brown in color
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene mftC, recombinant expression of His-tagged enzyme from plasmid pPH151, which contains the isc operon, in Escherichia coli strain Bl21(DE3)
gene mftC, recombinant expression of His-tagged enzyme in Escherichia coli strain Bl21(DE3)
gene mftC, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain Bl21(DE3)
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
reconstitution of purified recombinant His-tagged enzyme MftC by addition of DTT and FeCl3, followed by Na2S addition, and ultrafiltration
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ayikpoe, R.; Govindarajan, V.; Latham, J.A.
Occurrence, function, and biosynthesis of mycofactocin
Appl. Microbiol. Biotechnol.
103
2903-2912
2019
Mycobacterium sp.
brenda
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
Biochemistry
55
2813-2816
2016
Mycolicibacterium smegmatis (A0QSB8), Mycolicibacterium smegmatis ATCC 700084 (A0QSB8)
brenda
Ayikpoe, R.; Ngendahimana, T.; Langton, M.; Bonitatibus, S.; Walker, L.; Eaton, S.; Eaton, G.; Pandelia, M.; Elliott, S.; Latham, J.
Spectroscopic and electrochemical characterization of the mycofactocin biosynthetic protein, MftC, provides insight into its redox flipping mechanism
Biochemistry
58
940-950
2019
Mycobacterium ulcerans (A0PM49), Mycobacterium ulcerans Agy99 (A0PM49)
brenda
Haft, D.
Bioinformatic evidence for a widely distributed, ribosomally produced electron carrier precursor, its maturation proteins, and its nicotinoprotein redox partners
BMC Genomics
12
21
2011
Mycobacterium tuberculosis (P9WJ79), Mycobacterium tuberculosis H37Rv (P9WJ79), Mycobacterium tuberculosis ATCC 25618 (P9WJ79)
brenda
Khaliullin, B.; Ayikpoe, R.; Tuttle, M.; Latham, J.
Mechanistic elucidation of the mycofactocin-biosynthetic radical S-adenosylmethionine protein, MftC
J. Biol. Chem.
292
13022-13033
2017
Mycobacterium ulcerans (A0PM49), Mycobacterium ulcerans Agy99 (A0PM49)
brenda
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)
J. Biol. Chem.
292
4371-4381
2017
Mycolicibacterium smegmatis (A0QSB8), Mycolicibacterium smegmatis ATCC 700084 (A0QSB8)
brenda
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