(formate-C-acetyltransferase)-activating enzyme

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In enzymology, a [formate-C-acetyltransferase]-activating enzyme (EC 1.97.1.4) is an enzyme that catalyzes the chemical reaction

S-adenosyl-L-methionine + dihydroflavodoxin + [formate C-acetyltransferase]-glycine $\rightleftharpoons$ 5'-deoxyadenosine + L-methionine + flavodoxin semiquinone + [formate C-acetyltransferase]-glycin-2-yl radical

The 3 substrates of this enzyme are S-adenosyl-L-methionine, dihydroflavodoxin, and formate C-acetyltransferase-glycine, whereas its 4 products are 5'-deoxyadenosine, L-methionine, flavodoxin semiquinone, and formate C-acetyltransferase-glycin-2-yl radical.

This enzyme belongs to the family of oxidoreductases. The systematic name of this enzyme class is [formate C-acetyltransferase]-glycine dihydroflavodoxin:S-adenosyl-L-methionine oxidoreductase (S-adenosyl-L-methionine cleaving). Other names in common use include 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).

[edit] References

IUBMB entry for 1.97.1.4
BRENDA references for 1.97.1.4 (Recommended.)
PubMed references for 1.97.1.4
PubMed Central references for 1.97.1.4
Google Scholar references for 1.97.1.4
Frey M, Rothe M, Wagner AF, Knappe J (1994). "Adenosylmethionine-dependent synthesis of the glycyl radical in pyruvate formate-lyase by abstraction of the glycine C-2 pro-S hydrogen atom. Studies of [2H]glycine-substituted enzyme and peptides homologous to the glycine 734 site". J. Biol. Chem. 269: 12432–7. PMID 8175649.
Wagner AF, Frey M, Neugebauer FA, Schafer W, Knappe J (1992). "The free radical in pyruvate formate-lyase is located on glycine-734". Proc. Natl. Acad. Sci. U. S. A. 89: 996–1000. doi:10.1073/pnas.89.3.996. PMID 1310545.
Frey PA (2001). "Radical mechanisms of enzymatic catalysis". Annu. Rev. Biochem. 70: 121–48. doi:10.1146/annurev.biochem.70.1.121. PMID 11395404.