Inhibitors | Comment | Organism | Structure |
---|---|---|---|
actinonin | i.e. 3-[(1-[[2-(hydroxymethyl)-1-pyrrolidinyl]carbonyl]-2-methylpropyl)carbamoyl]octanohydroxamic acid, a naturally occurring potent PDF inhibitor | Escherichia coli |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Fe2+ | the native metal in Escherichia coli PDF is iron | Escherichia coli |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
N-formyl-L-methionine-polypeptide + H2O | Escherichia coli | - |
formate + L-methionine-polypeptide | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | P0A6K3 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
N-formyl-L-methionine-polypeptide + H2O | - |
Escherichia coli | formate + L-methionine-polypeptide | - |
? |
Synonyms | Comment | Organism |
---|---|---|
- |
Escherichia coli |
General Information | Comment | Organism |
---|---|---|
physiological function | PDF is an essential and highly conserved enzyme that functions in protein maturation by removing the N-formyl group from the methionine of nascently synthesized polypeptides | Escherichia coli |