Summary: Phosphotriesterase family
This is the Wikipedia entry entitled "Aryldialkylphosphatase". More...
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Aryldialkylphosphatase Edit Wikipedia article
|PDB structures||RCSB PDB PDBe PDBsum|
|Gene Ontology||AmiGO / EGO|
Structure of organophosphorus hydrolase
- an aryl dialkyl phosphate + H2O dialkyl phosphate + an aryl alcohol
An organophosphate is the general name for esters of phosphoric acid and is one of the organophosphorus compounds. They can be found as part of insecticides, herbicides, and nerve gases, amongst others. Some less-toxic organophosphates can be used as solvents, plasticizers, and EP additives.
Bacteria such as Pseudomonas diminuta harbor a plasmid that carries the gene for aryldialkylphosphatase (EC 18.104.22.168). 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 acts specifically on synthetic organophosphate triesters and phosphorofluoridates. It does not seem to have a natural occurring substrate and may thus have optimally evolved for utilizing paraoxon.
Aryldialkylphosphatase belongs to a family of enzymes that possess a binuclear zinc metal centre at their active site. The two zinc ions are coordinated by six different residues, six of which being histidines.
- Scanlan TS, Reid RC (1995). "Evolution in action". Chem. Biol. 2 (2): 71–75. doi:10.1016/1074-5521(95)90278-3. PMID 9383406.
- Fletterick RJ, Buchbinder JL, Stephenson RC, Dresser MJ, Pitera JW, Scanlan TS (1998). "Biochemical characterization and crystallographic structure of an Escherichia coli protein from the phosphotriesterase gene family". Biochemistry 37 (15): 5096–5106. doi:10.1021/bi971707. PMID 9548740.
 Further reading
- Aldridge WN (1953). "Serum esterases. 1. Two types of esterase (A and B) hydrolysing p-nitrophenyl acetate, propionate and butyrate, and a method for their determination". Biochem. J. 53 (1): 110–7. PMC 1198110. PMID 13032041.
- Bosmann HB (1972). "Membrane marker enzymes. Characterization of an arylesterase of guinea pig cerebral cortex utilizing p-nitrophenyl acetate as substrate". Biochim. Biophys. Acta. 276 (1): 180–91. PMID 5047702.
- Mackness MI, Thompson HM, Hardy AR, Walker CH (1987). "Distinction between 'A'-esterases and arylesterases. Implications for esterase classification". Biochem. J. 245 (1): 293–6. PMC 1148115. PMID 2822017.
- Main AR (1960). "The differentiation of the A-type esterases in sheep serum". Biochem. J. 75: 188–195.
- UK, 1989. Missing or empty
|This hydrolase article is a stub. You can help Wikipedia by expanding it.|
Phosphotriesterase family Provide feedback
No Pfam abstract.
Internal database links
|Similarity to PfamA using HHSearch:||Amidohydro_2 TatD_DNase|
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR001559
Synonym(s): Paraoxonase, A-esterase, Aryltriphosphatase, Phosphotriesterase, Paraoxon hydrolase
Bacteria such as Brevundimonas diminuta (Pseudomonas diminuta) harbour a plasmid that carries the gene for Aryldialkylphosphatase (EC) (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 acts 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.
Aryldialkylphosphatase belongs to a family [PUBMED:9383406, PUBMED:9548740] of enzymes that possess a binuclear zinc metal centre at their active site. The two zinc ions are coordinated by six different residues, six of which being histidines. This family so far includes, in addition to the parathion hydrolase, the following proteins:
- Escherichia coli protein Php, the substrate of which is not yet known.
- Mycobacterium tuberculosis phosphotriesterase homology protein Rv0230C.
- Mammalian phosphotriesterase related protein (PTER) (RPR-1).
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Molecular function||zinc ion binding (GO:0008270)|
|hydrolase activity, acting on ester bonds (GO:0016788)|
|Biological process||catabolic process (GO:0009056)|
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This example describes an architecture with one
Gladomain, followed by two consecutive
EGFdomains, and finally a single
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Curation and family details
|Author:||Mian N, Bateman A, Griffiths-Jones SR|
|Number in seed:||4|
|Number in full:||1183|
|Average length of the domain:||301.20 aa|
|Average identity of full alignment:||34 %|
|Average coverage of the sequence by the domain:||95.71 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||13|
|Download:||download the raw HMM for this family|
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There is 1 interaction for this family. More...
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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the PTE domain has been found. There are 100 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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