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Literature summary extracted from

  • Sawers, G.; Watson, G.
    A glycyl radical solution: oxygen-dependent interconversion of pyruvate formate-lyase (1998), Mol. Microbiol., 29, 945-954.
    View publication on PubMed

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.97.1.4 S-Adenosyl-L-methionine + dihydroflavodoxin + formate acetyltransferase-glycine Escherichia coli
-
?
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?

Organism

EC Number Organism UniProt Comment Textmining
1.97.1.4 Escherichia coli
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-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.97.1.4 additional information the enzyme also activates an enzyme which has both pyruvate formate-lyase activity and 2-ketobutyrate formate-lyase activity Escherichia coli ?
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?
1.97.1.4 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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?
1.97.1.4 S-Adenosyl-L-methionine + dihydroflavodoxin + formate acetyltransferase-glycine
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Escherichia coli ?
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?