Activating Compound | Comment | Organism | Structure |
---|---|---|---|
pyruvate formate-lyase activating enzyme | PFL-AE, EC 1.97.1.4, pyruvate formate-lyase is a glycyl radical enzyme activated by a radical AdoMet-activating enzyme PFL-AE, that exists largely in complex with enzyme PFL and S-adenosyl-L-methionine, all fully bound. Activation of pyruvate formate-lyase by pyruvate formate-lyase activating enzyme involves formation of a specific glycyl radical on pyruvate formate-lyase by the pyruvate formate-lyase activating enzyme in a reaction requiring S-adenosyl-L-methionine. 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 PF, 3.7fold less activation is achieved in the absence of these small molecules, demonstrating that pyruvate or oxamate are required for optimal activation. The [4Fe-4S] cluster of PFL-AE is coordinated by the cysteines of a conserved CX3CX2C motif, with the fourth unique iron coordinated by S-adenosyl-L-methionine. PFL-AE cycles between two different oxidation states during hydrogen abstraction, [4Fe-4S]2+/1+, with the [4Fe-4S]1+ being the state capable of reductive cleavage of AdoMet to generate the glycyl radical | Escherichia coli |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
acetyl-CoA + formate | Escherichia coli | - |
CoA + pyruvate | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | P09373 | gene pflB | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
acetyl-CoA + formate | - |
Escherichia coli | CoA + pyruvate | - |
r |
Synonyms | Comment | Organism |
---|---|---|
PFL | - |
Escherichia coli |
pyruvate formate-lyase | - |
Escherichia coli |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Escherichia coli |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.4 | - |
assay at | Escherichia coli |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
acetyl-CoA | - |
Escherichia coli |