Literature summary for 1.97.1.4 extracted from

Krebs, C.; Broderick, W.E.; Henshaw, T.F.; Broderick, J.B.; Huynh, B.H.
Coordination of adenosylmethionine to a unique iron site of the [4Fe-4S] of pyruvate formate-lyase activating enzyme: a moessbauer spectroscopic study (2002), J. Am. Chem. Soc., 124, 912-913.

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Metals/Ions

Metals/Ions	Comment	Organism	Structure
Iron	anaerobically purified enzyme, 4FE-4S cluster in a diamagnetic 2+ oxidation state	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

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+	4Fe-4S cluster is involved in catalysis by coordinating S-adenosyl-L-methionine	Escherichia coli	a

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Release 2023.1 (January 2023)