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

for references in articles please use BRENDA:EC1.97.1.4
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EC Tree
IUBMB Comments
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 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.
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Word Map
The enzyme appears in viruses and cellular organisms
pfl-ae, pyruvate formate-lyase activating enzyme, pyruvate formate lyase activating enzyme, pfl activase, pfl-activating enzyme, pyruvate formate-lyase-activating enzyme, pfl activating enzyme, pyruvate formate-lyase activase, more
S-adenosyl-L-methionine + dihydroflavodoxin + [formate C-acetyltransferase]-glycine = 5'-deoxyadenosine + L-methionine + flavodoxin semiquinone + [formate C-acetyltransferase]-glycin-2-yl radical + H+
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Escherichia coli
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