| Cloned (Comment) | Organism |
|---|---|
| overproduced in Escherichia coli | Thauera aromatica |
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | required | Thauera aromatica |
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + phenol + H2O | Thauera aromatica | the enzyme catalyses the first step in an anaerobic phenol degradation pathway | AMP + phenyl phosphate + phosphate | - |
? | |
| ATP + phenol + H2O | Thauera aromatica K172 | the enzyme catalyses the first step in an anaerobic phenol degradation pathway | AMP + phenyl phosphate + phosphate | - |
? |
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Thauera aromatica | A0A2R4BQP5 AND A0A2R4BQP1 | A0A2R4BQP5: phenylphosphate synthase subunit C, A0A2R4BQP1: phenylphosphate synthase subunit A | - |
| Thauera aromatica K172 | A0A2R4BQP5 AND A0A2R4BQP1 | A0A2R4BQP5: phenylphosphate synthase subunit C, A0A2R4BQP1: phenylphosphate synthase subunit A | - |
| Purification (Comment) | Organism |
|---|---|
- |
Thauera aromatica |
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + phenol + H2O | the enzyme catalyses the first step in an anaerobic phenol degradation pathway | Thauera aromatica | AMP + phenyl phosphate + phosphate | - |
? | |
| ATP + phenol + H2O | - |
Thauera aromatica | AMP + phenyl phosphate + phosphate | - |
? | |
| ATP + phenol + H2O | the enzyme catalyses the first step in an anaerobic phenol degradation pathway | Thauera aromatica K172 | AMP + phenyl phosphate + phosphate | - |
? | |
| ATP + phenol + H2O | - |
Thauera aromatica K172 | AMP + phenyl phosphate + phosphate | - |
? |
| Subunits | Comment | Organism |
|---|---|---|
| trimer | the enzyme consists of three proteins: protein 1 (70 kDa) resembles the central part of classical phosphoenolpyruvate synthase which contains a conserved histidine residue. It catalyzes the exchange of free [14C]phenol and the phenol moiety of phenylphosphate but not the phosphorylation of phenol. Phosphorylation of phenol requires protein 1, MgATP, and another protein, protein 2 (40 kDa), which resembles the N-terminal part of phosphoenolpyruvate synthase. The phosphoryl group in phenylphosphate is derived from the beta-phosphate group of ATP. The free energy of ATP hydrolysis obviously favors the trapping of phenol, even at a low ambient substrate concentration. The reaction is stimulated severalfold by another protein, protein 3 (24 kDa), which contains two cystathionine-beta-synthase domains of unknown function but does not show significant overall similarity to known proteins | Thauera aromatica |
| General Information | Comment | Organism |
|---|---|---|
| physiological function | the enzyme catalyses the first step in an anaerobic phenol degradation pathway | Thauera aromatica |