An organofluorophosphate-hydrolyzing activity in Tetrahymena thermophila.
An enzymatic activity that hydrolyzes O,O-diisoproplyphosphofluoridate (DFP) and O-1,2,2-trimethylpropylmethylphosphonofluoridate (Soman) was discovered in the ciliate protozoan Tetrahymena thermophila. The enzymatic activity classifies the protein as Mazur-type similar to that found in hog kidney and Escherichia coli. The rate of hydrolysis of Soman by the Tetrahymena-extract is the highest, on a per gram of extract basis, of any eucaryote. The molecular weight is approximately 75,400 as determined by Sephacryl column chromatography. A maximum fifteen-fold purification has been achieved. Potential exists for the detoxification and one-step detection of common organofluorophosphate pollutants. Additionally, Tetrahymena should prove an easier subject for manipulation than mammalian or squid sources. Protozoa may be a potentially important source of detoxification and degradation enzymes for other environmental contaminants.
D000818:Animals; D001673:Biodegradation, Environmental; D004950:Esterases; D006867:Hydrolases / Q000378:metabolism*; D007531:Isoflurophate / Q000378:metabolism; D044345:Phosphoric Triester Hydrolases; D012999:Soman / Q000378:metabolism; D013768:Tetrahymena / Q000201:enzymology*
D007531:Isoflurophate; D012999:Soman; D006867:Hydrolases; D004950:Esterases; D044345:Phosphoric Triester Hydrolases; C020061:diisopropyl-fluorophosphatase