(Formate-C-acetyltransferase)-activating enzyme

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[formate-C-acetyltransferase]-activating enzyme
Identifiers
EC no.1.97.1.4
CAS no.206367-15-9
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MetaCycmetabolic pathway
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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 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 radical SAM 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).

References

  • 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 (17): 12432–7. doi:10.1016/S0021-9258(18)99892-3. 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 (3): 996–1000. Bibcode:1992PNAS...89..996W. doi:10.1073/pnas.89.3.996. PMC 48372. 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.