Crystallization (Comment) | Organism |
---|---|
crystal structures of prephenate dehydratase in a relaxed (R) state | Staphylococcus aureus |
crystal structures of prephenate dehydratase in a tense (T) state | Chlorobaculum tepidum |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
prephenate | Staphylococcus aureus | converts prephenate to phenylpyruvate in L-phenylalanine biosynthesis | phenylpyruvate + H2O + CO2 | - |
? | |
prephenate | Chlorobaculum tepidum | converts prephenate to phenylpyruvate in L-phenylalanine biosynthesis | phenylpyruvate + H2O + CO2 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Chlorobaculum tepidum | - |
- |
- |
Staphylococcus aureus | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
prephenate | converts prephenate to phenylpyruvate in L-phenylalanine biosynthesis | Staphylococcus aureus | phenylpyruvate + H2O + CO2 | - |
? | |
prephenate | converts prephenate to phenylpyruvate in L-phenylalanine biosynthesis | Chlorobaculum tepidum | phenylpyruvate + H2O + CO2 | - |
? | |
prephenate | at the interface two ACT regulatory domains create two highly conserved pockets. Upon binding of the L-Phe inside the pockets, PDT transits from an open to a closed conformation | Staphylococcus aureus | phenylpyruvate + H2O + CO2 | - |
? | |
prephenate | at the interface two ACT regulatory domains create two highly conserved pockets. Upon binding of the L-Phe inside the pockets, PDT transits from an open to a closed conformation | Chlorobaculum tepidum | phenylpyruvate + H2O + CO2 | - |
? |
Subunits | Comment | Organism |
---|---|---|
tetramer | - |
Staphylococcus aureus |
tetramer | in crystal and solution | Chlorobaculum tepidum |
Synonyms | Comment | Organism |
---|---|---|
Ct-PDT | - |
Chlorobaculum tepidum |
Sa-PDT | - |
Staphylococcus aureus |