Biology:Diisopropyl-fluorophosphatase
| diisopropyl-fluorophosphatase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Diisopropyl fluorophosphatase monomer, Loligo vulgaris | |||||||||
| Identifiers | |||||||||
| EC number | 3.1.8.2 | ||||||||
| CAS number | 9032-18-2 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
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The enzyme diisopropyl-fluorophosphatase (EC 3.1.8.2)[1][2][3][4] catalyzes the reaction
- diisopropyl fluorophosphate + H2O [math]\displaystyle{ \rightleftharpoons }[/math] diisopropyl phosphate + fluoride
This enzyme belongs to the family of hydrolases, specifically those acting on ester bonds phosphoric-triester hydrolases. The systematic name is diisopropyl-fluorophosphate fluorohydrolase. Other names in common use include DFPase, tabunase, somanase, organophosphorus acid anhydrolase, organophosphate acid anhydrase, OPA anhydrase, diisopropylphosphofluoridase, dialkylfluorophosphatase, diisopropyl phosphorofluoridate hydrolase, isopropylphosphorofluoridase, and diisopropylfluorophosphonate dehalogenase. It employs one cofactor, divalent cation. At least one compound, chelating agent is known to inhibit this enzyme.
Structural studies
As of late 2007, 16 structures have been solved for this class of enzymes, with PDB accession codes 1E1A, 1PJX, 2GVU, 2GVV, 2GVW, 2GVX, 2IAO, 2IAP, 2IAQ, 2IAR, 2IAS, 2IAT, 2IAU, 2IAV, 2IAW, and 2IAX.
References
- ↑ Augustinsson K-B; Heimburger G (1954). "Enzymatic hydrolysis of organophosphorus compounds. II. Analysis of reaction products in experiments with Tabun and some properties of blood plasma tabunase". Acta Chem. Scand. 8: 762–767. doi:10.3891/acta.chem.scand.08-0762.
- ↑ Augustinsson K-B; Heimburger G (1954). "Enzymatic hydrolysis of organophosphorus compounds. I. Occurrence of enzymes hydrolysing dimethyl-amido-ethoxy-phosphoryl cyanide (Tabun)". Acta Chem. Scand. 8: 753–761. doi:10.3891/acta.chem.scand.08-0753.
- ↑ Augustinsson K-B; Heimburger G (1954). "Enzymatic hydrolysis of organophosphorus compounds. IV. Specificity studies". Acta Chem. Scand. 8: 1533–1541. doi:10.3891/acta.chem.scand.08-1533.
- ↑ "Purification and properties of dialkylfluorophosphatase". Biochim. Biophys. Acta 26 (1): 29–39. 1957. doi:10.1016/0006-3002(57)90050-1. PMID 13479457.
- Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd ed., vol. 4, Academic Press, New York, 1960, p. 541-550.
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