Stereoselective Hydrolysis of Organophosphate Nerve Agents by the Bacterial Phosphotriesterase

Detoxification of organophosphate nerve agents by bacterial phosphotriesterase.

Organophosphates have been widely used as insecticides and chemical warfare agents. The health risks associated with these agents have necessitated the need for better detoxification and bioremediation tools. Bacterial enzymes capable of hydrolyzing the lethal organophosphate nerve agents are of special interest. Phosphotriesterase (PTE) isolated from the soil bacteria Pseudomonas diminuta disp...

Stereochemical Constraints on the Catalytic Hydrolysis of Organophosphate Nerve Agents by Phosphotriesterase

Enzymes for the homeland defense: optimizing phosphotriesterase for the hydrolysis of organophosphate nerve agents.

Phosphotriesterase (PTE) from soil bacteria is known for its ability to catalyze the detoxification of organophosphate pesticides and chemical warfare agents. Most of the organophosphate chemical warfare agents are a mixture of two stereoisomers at the phosphorus center, and the S(P)-enantiomers are significantly more toxic than the R(P)-enantiomers. In previous investigations, PTE variants wer...

Bacterial detoxification of organophosphate nerve agents.

Bacterial enzymes have been isolated that catalyze the hydrolysis of organophosphate nerve agents with high-rate enhancements and broad substrate specificity. Mutant forms of these enzymes have been constructed through rational redesign of the active-site binding pockets and random mutagenesis to create protein variants that are optimized for the detoxification of agricultural insecticides and ...

Mechanism for the hydrolysis of organophosphates by the bacterial phosphotriesterase.

Phosphotriesterase (PTE) from Pseudomonas diminuta is a zinc metalloenzyme that hydrolyzes a variety of organophosphorus compounds. The kinetic parameters of Zn/Zn PTE, Cd/Cd PTE, and a mixed-metal Zn/Cd hybrid PTE were obtained with a variety of substrates to determine the role of each metal ion in binding and catalysis. pH-rate profiles for the hydrolysis of diethyl p-nitrophenyl phosphate (I...