Phosphonopyruvate hydrolase (PPH)

Phosphonopyruvate hydrolase (PPH; EC 3.11.1.3) is a bacterial enzyme that specifically catalyzes the hydrolytic cleavage of the carbon-phosphorus (C–P) bond in 3-phosphonopyruvate, producing pyruvate and phosphate[2][4][7][8]. PPH is highly substrate-specific, requiring phosphonopyruvate, with activity dependent on divalent cations such as Co²⁺, Mg²⁺, and Mn²⁺[2][6][8]. It is part of the phosphoenolpyruvate mutase/isocitrate lyase (PEPM/ICL) superfamily and plays a key role in the microbial degradation of phosphonates, contributing to the biogeochemical cycling of phosphorus in the environment[1][2][3][5]. PPH is not known as a human therapeutic target and has no established drug interactions or disease associations[8]. Its molecular structure is similar to other members of its superfamily, adopting an (α/β)₈ barrel fold, typically forming a tetramer[3][5]. It is chiefly studied for its biochemical mechanisms and environmental significance rather than for direct clinical or pharmacological applications.

Other names

PPH