Diisopropyl-fluorophosphatase

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diisopropyl-fluorophosphatase
Diisopropyl fluorophosphatase monomer, Loligo vulgaris
Identifiers
EC no.3.1.8.2
CAS no.9032-18-2
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
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PMCarticles
PubMedarticles
NCBIproteins

The enzyme diisopropyl-fluorophosphatase (EC 3.1.8.2)[1][2][3][4] catalyzes the reaction

diisopropyl fluorophosphate + H2O 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[edit]

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[edit]

  1. ^ 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.
  2. ^ 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.
  3. ^ 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.
  4. ^ COHEN JA, WARRINGA MG (1957). "Purification and properties of dialkylfluorophosphatase". Biochim. Biophys. Acta. 26 (1): 29–39. 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.