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Literature summary for extracted from

  • Broderick, J.B.; Henshaw, T.F.; Cheek, J.; Wojtuszewski, K.; Smith, S.R.; Trojan, M.R.; McGhan, R.M.; Kopf, A.; Kibbey, M.; Broderick, W.E.
    Pyruvate formate-lyase-activating enzyme: Strictly anaerobic isolation yields active enzyme containing a [3Fe-4S]+ cluster (2000), Biochem. Biophys. Res. Commun., 269, 451-456.
    View publication on PubMed


Metals/Ions Comment Organism Structure
Iron 2.8 mol per mol of enzyme, as (3Fe-4S)+ cluster Escherichia coli


Organism UniProt Comment Textmining
Escherichia coli

Purification (Commentary)

Purification (Comment) Organism
using strictly anaerobic conditions Escherichia coli

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
25°C, pH 8.1 Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
S-adenosyl-L-methionine + dihydroflavodoxin + formate acetyltransferase-glycine
Escherichia coli 5'-deoxyadenosine + methionine + flavodoxin + formate acetyltransferase-glycine-2-yl-radical