A Thermostable Bacterial Metallohydrolase that Degrades Organophosphate Plasticizers.

ABSTRACT: A cyclase-phosphotriesterase (C-PTE) from Ruegeria pomeroyi DSS-3 has recently been identified for its capacity to detoxify several organophosphate compounds. However, several aspects of this enzyme remain unexplored, such as its activity with industrial organophosphates, its molecular structure, and its thermostability. In this work, the crystal structure of C-PTE is reported, which is solved to 2.3 Å resolution, providing insight into the enzyme's mechanism of action, revealing a binuclear Zn²⁺ active site and distant similarity to other phosphotriesterases from the amidohydrolase superfamily. It is shown that C-PTE catalyzes the hydrolysis of the OP plasticizers triphenyl phosphate (TPhP) and tris(2-chloropropyl) phosphate (TCPP), albeit with low efficiency, but not the steri

SUBMITTER: Ji D 

PROVIDER: S-EPMC12135135 | biostudies-literature | 2025 Jun

REPOSITORIES: biostudies-literature