Diisopropyl-fluorophosphatase

In enzymology, a diisopropyl-fluorophosphatase is an enzyme that catalyzes the chemical reaction


 * diisopropyl fluorophosphate + H2O $$\rightleftharpoons$$ diisopropyl phosphate + fluoride

Thus, the two substrates of this enzyme are diisopropyl fluorophosphate and H2O, whereas its two products are diisopropyl phosphate and fluoride.

This enzyme belongs to the family of hydrolases, specifically those acting on ester bonds phosphoric-triester hydrolases. The systematic name of this enzyme class is diisopropyl-fluorophosphate fluorohydrolase. Other names in common use include DFPase, tabunase, somanase, organophosphorus acid anhydrolase, organophosphate acid anhydrase, OPA anhydrase, diisopropylphosphofluoridase, dialkylfluorophosphatase, diisopropyl phosphorofluoridate hydrolase, isopropylphosphorofluoridase, and diisopropylfluorophosphonate dehalogenase. It employs one cofactor, divalent cation. At least one compound, Chelating agent is known to inhibit this enzyme.

Structural studies
As of late 2007, 16 structures have been solved for this class of enzymes, with PDB accession codes, , , , , , , , , , , , , , , and.