Crystallization (Comment) | Organism |
---|---|
structure of the pyruvate formate-lyase monomer in complex with pyruvate and CoA, structure of active site, small model computational studies of the pyruvate formate-lyase substrate transformation | Escherichia coli |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
CoA + pyruvate | Escherichia coli | - |
acetyl-CoA + formate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | P09373 | - |
- |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
additional information | - |
mechanistic effect of choosing different protonation states for a substrate carboxylate group that is involved in a salt bridge with an arginine residue analyzed, modeling of arginine-bound carboxylates, computational details, neutral model and anionic model presented, extended model consists of pyruvate in a complex with methylguanidinum and methylthiyl radical, neutral carboxylic acid as a more realistic approximation to the salt bridge arrangement than a bare anionic carboxylate substituent | Escherichia coli |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
CoA + pyruvate | - |
Escherichia coli | acetyl-CoA + formate | - |
? | |
CoA + pyruvate | mechanism to truncate an arginine-bound carboxylate motif, substrate mechanism of pyruvate formate-lyase used as a case study | Escherichia coli | acetyl-CoA + formate | - |
? |
Synonyms | Comment | Organism |
---|---|---|
PFL | - |
Escherichia coli |
pyruvate formate-lyase | - |
Escherichia coli |