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Literature summary for 2.7.1.238 extracted from

  • Schmeling, S.; Narmandakh, A.; Schmitt, O.; Gadon, N.; Schuehle, K.; Fuchs, G.
    Phenylphosphate synthase a new phosphotransferase catalyzing the first step in anaerobic phenol metabolism in Thauera aromatica (2004), J. Bacteriol., 186, 8044-8057 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
overproduced in Escherichia coli Thauera aromatica

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Thauera aromatica

Natural Substrates/ Products (Substrates)

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

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 (Commentary)

Purification (Comment) Organism
-
Thauera aromatica

Substrates and Products (Substrate)

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

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

General Information Comment Organism
physiological function the enzyme catalyses the first step in an anaerobic phenol degradation pathway Thauera aromatica