Characterization of organophosphorus hydrolases and the genetic manipulation of the phosphotriesterase from pseudomonas diminuta

Technical Report · Fri Dec 31 04:00:00 EST 1993

OSTI ID:91370

Dave, K I; Miller, C E; Wild, J R

There are a variety of enzymes which are specifically capable of hydrolyzing organophosphorus esters with different phosphoryl bonds from the typical phosphotriester bonds of common insecticidal neurotoxins (e.g. paraoxon or coumaphos) to the phosphonate-fluoride bonds of chemical warfare agents (e.g. soman or sarin). These enzymes comprise a diverse set of enzymes whose basic architecture and substrate specificities vary dramatically, yet they appear to be ubiquitous throughout nature. The most thoroughly studied of these enzymes is the organophosphate hydrolase (opd gene product) of Pseudomonas diminuta and Ftavobacterium sp. ATCC 27551, and the heterologous expression, post-translational modification, and genetic engineering studies undertaken with this enzyme are described.

• Research Organization: Texas A and M Univ., College Station, TX (United States). Dept. of Biochemistry and Biophysics
• OSTI ID: 91370
• Report Number(s): AD-A--290425/8/XAB; CNN: Contract DAAL03-90-G-0045
• Country of Publication: United States
• Language: English

Related Subjects

45 MILITARY TECHNOLOGY, WEAPONRY, AND NATIONAL DEFENSE
56 BIOLOGY AND MEDICINE
APPLIED STUDIES
CHEMICAL WARFARE AGENTS
PREVENTIVE MEDICINE
TOXICITY