Phenylphosphate synthase (PPS)

Phenylphosphate synthase (PPS), also known as phenol phosphorylase (EC 2.7.1.238), is a microbial enzyme complex essential for the anaerobic metabolism of phenolic compounds [1][2]. It is primarily identified in denitrifying bacteria such as Thauera aromatica, where it catalyzes the first step of phenol degradation by converting phenol into phenylphosphate [3][4]. This process requires MgATP and proceeds via a multi-component mechanism involving a phosphohistidine intermediate on one of its three subunits, typically designated Protein 1, 2, and 3 [1][6]. The enzyme is structurally related to phosphoenolpyruvate (PEP) synthase and represents an evolutionary adaptation for the activation of aromatic rings in the absence of oxygen [3][7]. From a therapeutic perspective, Phenylphosphate synthase is not a recognized target for any pharmaceutical agents in humans and is not currently a focus for antimicrobial therapy [2][5]. Its significance is predominantly limited to environmental microbiology and the study of bioremediation pathways for aromatic pollutants, such as those found in contaminated groundwater [3][5]. There are currently no drugs, clinical trials, or established disease associations involving this enzyme [5][13]. Consequently, it is not considered a therapeutic target and lacks recognized biomarkers or safety profiles in a clinical context [5][13].

Other names

Phenol phosphorylaseATP:phenol phosphotransferase (AMP-forming)Phenol-phosphorylating enzymeppsAppsBppsC

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