Literature summary for 1.97.1.4 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.

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Metals/Ions

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

Organism

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
43	-	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	-	?

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Release 2023.1 (January 2023)