EC - [formate-C-acetyltransferase]-activating enzyme

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IntEnz Enzyme Nomenclature


Accepted name:
[formate-C-acetyltransferase]-activating enzyme
Other names:
PFL activase
PFL-glycine:S-adenosyl-L-methionine H transferase (flavodoxin-oxidizing, S-adenosyl-L-methionine-cleaving)
formate acetyltransferase activating enzyme
formate acetyltransferase-glycine dihydroflavodoxin:S-adenosyl-L-methionine oxidoreductase (S-adenosyl-L-methionine cleaving)
[pyruvate formate-lyase]-activating enzyme
pyruvate formate-lyase 1 activating enzyme
Systematic name:
[formate C-acetyltransferase]-glycine dihydroflavodoxin:S-adenosyl-L-methionine oxidoreductase (S-adenosyl-L-methionine cleaving)




An iron-sulfur protein. A single glycine residue in EC, formate C-acetyltransferase, is oxidized to the corresponding radical by transfer of H from its CH2 to S-adenosyl-L-methionine (AdoMet) with concomitant cleavage of the latter. The reaction requires Fe2+. The first stage is reduction of the AdoMet to give methionine and the 5'-deoxyadenosin-5'-yl radical, which then abstracts a hydrogen radical from the glycine residue.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Protein domains and families: PROSITE:PDOC00834
Structural data: CSA , EC2PDB
Gene Ontology: GO:0043365
CAS Registry Number: 206367-15-9
UniProtKB/Swiss-Prot: (23) [show] [UniProt]


  1. Frey, M., Rothe, M., Wagner, A.F.V. and Knappe, J.
    Adenosylmethionine-dependent synthesis of the glycyl radical in pyruvate formate-lyase by abstraction of the glycine C-2 pro-S hydrogen atom.
    J. Biol. Chem. 269: 12432-12437 (1994). [PMID: 8175649]
  2. Wagner, A.F., Frey, M., Neugebauer, F.A., Schäfer, W. and Knappe, J.
    The free radical in pyruvate formate-lyase is located on glycine-734.
    Proc. Natl. Acad. Sci. USA 89: 996-1000 (1992). [PMID: 1310545]
  3. Frey, P.A.
    Radical mechanisms of enzymatic catalysis.
    Annu. Rev. Biochem. 70: 121-148 (2001). [PMID: 11395404]

[EC created 1999, modified 2004]