| EC |
1.97.1.4 |
| Accepted name: |
[formate-C-acetyltransferase]-activating enzyme |
| Reaction: |
S-adenosyl-L-methionine + dihydroflavodoxin + [formate C-acetyltransferase]-glycine = 5′-deoxyadenosine + L-methionine + flavodoxin semiquinone + [formate C-acetyltransferase]-glycin-2-yl radical |
| Other name(s): |
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) |
| Comments: |
An iron-sulfur protein. A single glycine residue in EC 2.3.1.54, formate C-acetyltransferase, is oxidized to the corresponding radical by transfer of H from its CH2 to 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: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 206367-15-9 |
| References: |
| 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 (1994) 12432–12437. [PMID: 8175649] |
| 2. |
Wagner, A.F.V., 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 (1992) 996–1000. [DOI] [PMID: 1310545] |
| 3. |
Frey, P.A. Radical mechanisms in enzymatic catalysis. Annu. Rev. Biochem. 70 (2001) 121–148. [DOI] [PMID: 11395404] |
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| [EC 1.97.1.4 created 1999, modified 2004] |
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