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Literature summary for 1.97.1.4 extracted from

  • Crain, A.V.; Broderick, J.B.
    Pyruvate formate-lyase and its activation by pyruvate formate-lyase activating enzyme (2013), J. Biol. Chem., 289, 5723-5729.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.97.1.4

Organism

Organism UniProt Comment Textmining
Escherichia coli
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
S-adenosyl-L-methionine + dihydroflavodoxin + formate acetyltransferase-glycine the interaction with substrate formate C-acetyltransferase is very slow and rate-limited by large conformational changes. The enzyme binds S-adenosyl-L-methionine with the same affinity of about 0.006 mM regardless of the presence or absence of formate C-acetyltransferase. Activation of formate C-acetyltransferase in the presence of its substrate pyruvate or the analogue oxamate results in stoichiometric conversion of the [4Fe-4S]1+ cluster to the glycyl radical on formate C-acetyltransferase, however 3.7-fold less activation is achieved in the absence of these small molecules. Formate C-acetyltransferase, formate C-acetyltransferase activating enzyme, and S-adenosyl-L-methionine are essentially fully bound in vivo, whereas electron donor proteins are partially bound Escherichia coli 5'-deoxyadenosine + methionine + flavodoxin + formate acetyltransferase-glycine-2-yl-radical
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