Phenylphosphate synthase

Phenylphosphate synthase consists of three subunits with molecular masses of 70, 40, and 24kDa. Subunit 1 resembles the central part of classical phospho-enolpyruvate synthase which contains a conserved histidine residue. It catalyzes the exchange of free [ C] phenol and the phenol moiety of phenylphosphate but not the phosphorylation of phenol. Phosphorylation of phenol requires subunit 1, MgATP, and another protein, subunit 2 (40kDa), which resembles the N-terminal part of phosphoenolpyruvate synthase. Subunit 1 and 2 catalyze the following reaction ... 

The phosphoryl group in phenylphosphate is derived from the -phosphate group of ATP. The free energy of ATP hydrolysis obviously favors the trapping of phenol K, 0.04 mM), even at a low ambient substrate concentration. The reaction is stimulated several fold by another protein, subunit 3 (24kDa). The molecular and catalytic features of phenylphosphate synthase resemble those of phosphoenolpyruvate synthase, albeit with interesting modifications. ... 

Narmandakh A, N Gad on, F Drepper, B Knapp, W Haehnel, G Fuchs (2006) Phosphorylation of phenol by phenylphosphate synthase role of histidine phosphate in catalysis. J Bacteriol 188 7815-7822. 

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