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Literature summary for 1.97.1.4 extracted from

  • Wagner, A.F.V.; Demand, J.; Schilling, G.; Pils, T.; Knappe, J.
    A dehydroalanyl residue can capture the 5'-deoxyadenosyl radical generated from S-adenosylmethionine by pyruvate formate-lyase-activating enzyme (1999), Biochem. Biophys. Res. Commun., 254, 306-310.
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Escherichia coli
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Reaction

Reaction Comment Organism Reaction ID
S-adenosyl-L-methionine + dihydroflavodoxin + [formate C-acetyltransferase]-glycine = 5'-deoxyadenosine + L-methionine + flavodoxin semiquinone + [formate C-acetyltransferase]-glycin-2-yl radical + H+ mechanism, a deoxyadenosyl radical intermediate, generated by the reductive cleavage of S-adenosylmethionine serves as the actual H atom abstracting species Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information a DELTAAla-containing peptide which lacks hydrogens at the 734-Calpha atom is recognized by the enzyme and is able to trap covalently the nucleophilic 5-deoxyadenosine radical Escherichia coli ?
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S-adenosyl-L-methionine + dihydroflavodoxin + formate acetyltransferase-glycine
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Escherichia coli 5'-deoxyadenosine + methionine + flavodoxin + formate acetyltransferase-glycine-2-yl-radical
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?