Genetic and biochemical manipulation of a broad-spectrum organophosphate degrading system. Final report

Technical Report · Wed Jun 01 04:00:00 EDT 1994

OSTI ID:220310

Raushel, F M; Wild, J R

The phosphotriesterase from Pseudomonas diminuta has been isolated and extensively characterized. The protein has been found to catalyze the hydrolysis of a variety of organophosphate esters, including sarin and soman. Inactivation and pH-rate profiles have identified a critical hIstidine residue for binding and catalysis. The native enzyme contains two divalent cations that are required for activity. These metal ions are ligated to the protein via 4-5 histidine residues. The variation of enzyme reactivity with substrate structure indicates that paraoxon is hydrolyzed at the diffusion controlled rate. The purified protein can be immobilized on a solid support via interaction with triphenyl sepharose or, alternatively, by covalent attachment to nylon surfaces. The immobilized protein has proven to be effective in the hydrolysis and detoxification of organophosphate nerve agents.

• Research Organization: Texas A and M Univ., College Station, TX (United States). Research Foundation
• OSTI ID: 220310
• Report Number(s): AD-A--301746/4/XAB; CNN: Contract DAAL03-90-G-0045
• Country of Publication: United States
• Language: English

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