A thermostable bacterial metallohydrolase that degrades organophosphate plasticizers.

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, we report the crystal structure of C-PTE, which was 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. We show 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 sterically bulkier tri-otolyl phosphate (ToTP). Finally, we show that, even though Ruegeria pomeroyi DSS-3 is not a thermophile, C-PTE exhibits remarkable thermostability and retains structure up to 90 °C. Overall, our findings advance our understanding of C-PTE, suggest that it is a good candidate for engineering owing to its thermostability and that it could contribute to bioremediation strategies to reduce the impact of pollution by industrial organophosphates.