|PROSITE documentation PDOC01026|
Bacteria such as Pseudomonas diminuta harbor a plasmid that carries the gene for the enzyme phosphotriesterase (EC 126.96.36.199) (PTE) (also known as parathion hydrolase). This enzyme has attracted interest because of its potential use in the detoxification of chemical waste and warfare agents and its ability to degrade agricultural pesticides such as parathion. It act specifically on synthetic organophosphate triesters and phosphorofluoridates. It does not seem to have a natural occuring substrate and may thus have optimally evolved for utilizing paraoxon.
The two zinc ions are coordinated by six different residues, four of which being histidines. We have developed a signature pattern for this family of enzymes, which corresponds to a region located in the N-terminal section. That contains two histidines that bind the first of the two zinc ions. We also developed a profile that covers the entire phosphotriesterase and has been manually adapted to detect each of the six zinc-binding residues.Last update:
December 2007 / Pattern removed, profile added and text revised.
PROSITE methods (with tools and information) covered by this documentation:
|1||Authors||Scanlan T.S., Reid R.C.|
|Title||Evolution in action.|
|Source||Chem. Biol. 2:71-75(1995).|
|2||Authors||Buchbinder J.L., Stephenson R.C., Dresser M.J., Pitera J.W., Scanlan T.S., Fletterick R.J.|
|Title||Biochemical characterization and crystallographic structure of an Escherichia coli protein from the phosphotriesterase gene family.|