Literature summary extracted from

Frey, M.; Rothe, M.; Wagner, A.F.V.; Knappe, J.
Adenosylmethionine-dependent synthesis of the glycyl radical in pyruvate formate-lyase by abstraction of the glycine C-2 pro-S hydrogen atom (1994), J. Biol. Chem., 269, 12432-12437.

Inhibitors

EC Number	Inhibitors	Comment	Organism	Structure
1.97.1.4	peptides	peptides homologous to the Gly734 site of pyruvate formate-lyase that are active as substrates	Escherichia coli

Organism

EC Number	Organism	UniProt	Comment	Textmining
1.97.1.4	Escherichia coli	-	-	-

Reaction

EC Number	Reaction	Comment	Organism	Reaction ID
1.97.1.4	S-adenosyl-L-methionine + dihydroflavodoxin + [formate C-acetyltransferase]-glycine = 5'-deoxyadenosine + L-methionine + flavodoxin semiquinone + [formate C-acetyltransferase]-glycin-2-yl radical + H+	the glycyl radical in pyruvate formate-lyase is produced by stereospecific abstraction of the pro-S hydrogen of Gly734 by the 5'-deoxyadenosine radical generated in the active center of the enzyme	Escherichia coli	a

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
1.97.1.4	S-adenosyl-L-methionine + dihydroflavodoxin + formate acetyltransferase-glycine	the glycyl radical in pyruvate formate-lyase is produced by stereospecific abstraction of the pro-S hydrogen of Gly734 by the 5'-deoxyadenosine radical generated in the active center of the enzyme	Escherichia coli	5'-deoxyadenosine + methionine + flavodoxin + formate acetyltransferase-glycine-2-yl-radical	-	?

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Release 2023.1 (January 2023)