Literature summary for 2.3.1.54 extracted from

Byer, A.S.; McDaniel, E.C.; Impano, S.; Broderick, W.E.; Broderick, J.B.
Mechanistic studies of radical SAM enzymes pyruvate formate-lyase activating enzyme and lysine 2,3-aminomutase case studies (2018), Methods Enzymol., 606, 269-318 .

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Activating Compound

Activating Compound	Comment	Organism	Structure
pyruvate formate-lyase activating enzyme	converts the enzyme to its catalytically active state by generating a stable glycyl radical in the active site at G734	Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
acetyl-CoA + formate	Escherichia coli	-	CoA + pyruvate	-	r
CoA + pyruvate	Escherichia coli	-	acetyl-CoA + formate	-	r

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
quaternary methylamine AP5-ion exchange column chromatography and phenyl Sepharose column chromatography	Escherichia coli

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
acetyl-CoA + formate	-	Escherichia coli	CoA + pyruvate	-	r
CoA + pyruvate	-	Escherichia coli	acetyl-CoA + formate	-	r

Subunits

Subunits	Comment	Organism
homodimer	2 * 85000, SDS-PAGE	Escherichia coli

Synonyms

Synonyms	Comment	Organism
PFL	-	Escherichia coli
pyruvate formate-lyase	-	Escherichia coli

General Information

General Information	Comment	Organism
metabolism	the enzyme catalyzes the conversion of pyruvate and CoA to formate and acetyl-CoA during anaerobic glucose metabolism	Escherichia coli

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Release 2023.1 (January 2023)