Diisopropyl-fluorophosphatase

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diisopropyl-fluorophosphatase
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Diisopropyl fluorophosphatase monomer, Loligo vulgaris
Identifiers
EC no. 3.1.8.2
CAS no. 9032-18-2
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MetaCyc metabolic pathway
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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

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.

Related Research Articles

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A catalytic triad is a set of three coordinated amino acid residues that can be found in the active site of some enzymes. Catalytic triads are most commonly found in hydrolase and transferase enzymes. An acid-base-nucleophile triad is a common motif for generating a nucleophilic residue for covalent catalysis. The residues form a charge-relay network to polarise and activate the nucleophile, which attacks the substrate, forming a covalent intermediate which is then hydrolysed to release the product and regenerate free enzyme. The nucleophile is most commonly a serine or cysteine, but occasionally threonine or even selenocysteine. The 3D structure of the enzyme brings together the triad residues in a precise orientation, even though they may be far apart in the sequence.

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Gösta Pettersson is an emeritus professor in biochemistry at Lund University, Sweden. He was born in 1937 in Varberg, Sweden. He gained his Ph.D. at Lund University in 1966 on the basis of a thesis on toluquinones, and his early research was mainly concerned with fumigatin and other products of fungal metabolism.

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References

  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.