EC Number   |
Substrates |
Organism |
Products |
Reversibility |
|---|
   1.97.1.4 | more |
the enzyme also activates an enzyme which has both pyruvate formate-lyase activity and 2-ketobutyrate formate-lyase activity |
Escherichia coli |
? |
- |
? |
| 1.97.1.4 | more |
a DELTAAla-containing peptide which lacks hydrogens at the 734-Calpha atom is recognized by the enzyme and is able to trap covalently the nucleophilic 5-deoxyadenosine radical |
Escherichia coli |
? |
- |
? |
| 1.97.1.4 | more |
pyruvate formate-lyase-activating enzyme (PFL-AE) activates pyruvate formate-lyase by generating a catalytically essential radical on Gly-734 of pyruvate formate-lyase. PFL-AE shifts the closed/open formation of pyruvate formate-lyase to the open conformation, in which Gly-734 is more solvent-exposed and accessible to the PFL-AE active site |
Escherichia coli |
? |
- |
? |
| 1.97.1.4 | more |
in vivo concentrations of the entire PFL system is calculated to estimate the amount of bound protein in the cell. PFL, PFL-AE, and S-adenosyl-L-methionine are essentially fully bound in vivo, whereas electron donor proteins are partially bound |
Escherichia coli |
? |
- |
? |
| 1.97.1.4 | more |
PFL-AE utilizes S-adenosylmethionine (SAM) and reduced flavodoxin as the cosubstrates to generate a 5'-deoxyadenosyl radical, which then activates PFL by abstracting a hydrogen atom from residue G734 |
Escherichia coli |
? |
- |
? |
| 1.97.1.4 | more |
usage of an S-adenosyl-L-methionine binding assay to accurately determine the equilibrium constants for S-adenosyl-L-methionine binding to enzyme PFL-AE alone and in complex with substrate PFL, activation of PFL 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 PFL. 3.7fold less activation is achieved in the absence of these small molecules, demonstrating that pyruvate or oxamate are required for optimal activation. For the assay, the enzyme PFL-AE is attached to a CM5 sensor chip using standard thiol coupling procedures |
Escherichia coli |
? |
- |
? |
| 1.97.1.4 | S-adenosyl-L-methionine + 5-deazariboflavin + [formate C-acetyltransferase]-glycine |
- |
Escherichia coli |
5'-deoxyadenosine + L-methionine + 5-deazariboflavin semiquinone + [formate C-acetyltransferase]-glycin-2-yl radical |
- |
? |
| 1.97.1.4 | S-adenosyl-L-methionine + dihydroflavodoxin + formate acetyltransferase-glycine |
- |
Escherichia coli |
5'-deoxyadenosine + methionine + flavodoxin + formate acetyltransferase-glycine-2-yl-radical |
- |
? |
| 1.97.1.4 | S-adenosyl-L-methionine + dihydroflavodoxin + formate acetyltransferase-glycine |
- |
Clostridium pasteurianum |
5'-deoxyadenosine + methionine + flavodoxin + formate acetyltransferase-glycine-2-yl-radical |
- |
? |
| 1.97.1.4 | S-adenosyl-L-methionine + dihydroflavodoxin + formate acetyltransferase-glycine |
formate acetyltransferase-glycine is the inactive form of the enzyme |
Escherichia coli |
5'-deoxyadenosine + methionine + flavodoxin + formate acetyltransferase-glycine-2-yl-radical |
formate acetyltransferase-glycine-2-yl-radical is the active form of the enzyme |
? |
