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Literature summary for 1.3.98.7 extracted from

  • 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 (2019), Biochemistry, 58, 940-950 .
    View publication on PubMedView publication on EuropePMC
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Protein Variants

Protein Variants Comment Organism
C251A insoluble Mycobacterium ulcerans
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** Mycobacterium ulcerans
C269A/C323A insoluble Mycobacterium ulcerans
C30A/C34A/C37A insoluble Mycobacterium ulcerans
C30A/C37A radical S-adenosylmethionine mutant, can neither cleave SAM nor modify MftA Mycobacterium ulcerans
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** Mycobacterium ulcerans
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** Mycobacterium ulcerans
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 were incapable of converting MftA to MftA* or MftA** Mycobacterium ulcerans

Organism

Organism UniProt Comment Textmining
Mycobacterium ulcerans A0PM49 cf. EC 4.1.99.26
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Mycobacterium ulcerans Agy99 A0PM49 cf. EC 4.1.99.26
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
C-terminal [mycofactocin precursor peptide MftA]-glycyl-L-valyl-L-tyrosine + S-adenosyl-L-methionine
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 Mycobacterium ulcerans C-terminal [mycofactocin precursor peptide MftA]-glycyl-L-valyl-4-[2-aminoethenyl]phenol + CO2 + 5'-deoxyadenosine + L-methionine
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 ?
C-terminal [mycofactocin precursor peptide MftA]-glycyl-L-valyl-L-tyrosine + S-adenosyl-L-methionine
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 Mycobacterium ulcerans Agy99 C-terminal [mycofactocin precursor peptide MftA]-glycyl-L-valyl-4-[2-aminoethenyl]phenol + CO2 + 5'-deoxyadenosine + L-methionine
-
 ?
additional information enzyme additionally catalyzes SAM-dependent C-C bond formation between the Cbeta of the penultimate valine and the Calpha of the former tyrosine, forming a 3-amino-5-[(4-hydroxyphenyl) methyl]-4,4-dimethyl-2-pyrrolidinone moiety, i.e. MftA*, reaction of EC 4.1.99.26 Mycobacterium ulcerans ?
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additional information enzyme additionally catalyzes SAM-dependent C-C bond formation between the Cbeta of the penultimate valine and the Calpha of the former tyrosine, forming a 3-amino-5-[(4-hydroxyphenyl) methyl]-4,4-dimethyl-2-pyrrolidinone moiety, i.e. MftA*, reaction of EC 4.1.99.26 Mycobacterium ulcerans Agy99 ?
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Synonyms

Synonyms Comment Organism
mftC
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 Mycobacterium ulcerans
mycofactocin maturase
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 Mycobacterium ulcerans

Cofactor

Cofactor Comment Organism Structure
S-adenosyl-L-methionine residues Cys30, 34, and 37 are the radical S-adenosylmethionine ligands Mycobacterium ulcerans
[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 Mycobacterium ulcerans