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Literature summary for 3.1.8.2 extracted from

  • Zhang, H.; Yang, L.; Ma, Y.Y.; Zhu, C.; Lin, S.; Liao, R.Z.
    Theoretical studies on catalysis mechanisms of serum paraoxonase 1 and phosphotriesterase diisopropyl fluorophosphatase suggest the alteration of substrate preference from paraoxonase to DFP (2018), Molecules, 23, 1660.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.1.8.2

Cloned(Commentary)

Cloned (Comment) Organism
phylogenetic analysis Loligo vulgaris

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ dependent on, PTE Ca2+ binding structure comparisons Loligo vulgaris
Zn2+ required Loligo vulgaris

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
diisopropyl fluorophosphate + H2O Loligo vulgaris
-
 diisopropyl phosphate + fluoride
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 ?

Organism

Organism UniProt Comment Textmining
Loligo vulgaris Q7SIG4
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-

Reaction

Reaction Comment Organism Reaction ID
diisopropyl fluorophosphate + H2O = diisopropyl phosphate + fluoride catalytic reaction mechanism involving residue Asp269, molecular dynamics and modelling, overview Loligo vulgaris
a

Source Tissue

Source Tissue Comment Organism Textmining
central nervous system
-
 Loligo vulgaris
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(RS)-propan-2-yl methylphosphonofluoridate + H2O i.e. sarin Loligo vulgaris isopropyl phosphate methylphosphonate + fluoride
-
 ?
3-[fluoro(methyl)phosphoryl]oxy-2,2-dimethylbutane + H2O i.e. soman Loligo vulgaris 3,3-dimethylbutan-2-yl methylphosphonate + fluoride
-
 ?
cyclohexyl methylphosphonofluoridate + H2O i.e. cyclosarin Loligo vulgaris cyclohexyl methylphosphonate + fluoride
-
 ?
diisopropyl fluorophosphate + H2O
-
 Loligo vulgaris diisopropyl phosphate + fluoride
-
 ?
ethyl dimethylphosphoramidocyanidate + H2O i.e. tabun Loligo vulgaris ?
-
 ?
additional information the squid phosphotriesterase diisopropyl fluorophosphatase (DFPase) from Loligo vulgaris shows relatively specific substrate preference, efficiently catalyzing the hydrolysis of diisopropyl fluorophosphate (DFP) and G-type nerve agents, including tabun (GA), sarin (GB), soman (GD), and cyclohexyl sarin (GF). The detoxification of the organophosphorous agent is achieved by the hydrolytic reaction producing a phosphate or phosphonate and a fluoride ion. The DFPase from squid central nervous system shows strong preference for the hydrolysis of P-F or P-CN bonds, which are absent in natural compounds Loligo vulgaris ?
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 ?

Synonyms

Synonyms Comment Organism
DFPase
-
 Loligo vulgaris
diisopropyl fluorophosphatase
-
 Loligo vulgaris
phosphotriesterase
-
 Loligo vulgaris

General Information

General Information Comment Organism
evolution the phosphotriesterase activity development between PON1, EC 3.1.8.1, and DFPase, EC 3.1.8.2, is investigated by using the hybrid density functional theory method B3LYP. Structure comparisons of evolutionarily related enzymes show that the mutation of Asn270 leads to the catalytic Ca2+ ion indirectly connecting the buried structural Ca2+ ion via hydrogen bonds in DFPase. It can reduce the plasticity of enzymatic structure, and possibly change the substrate preference from paraoxon (preferred substrate of PON1) to DFP (preferred substrate of DFPase), which implies an evolutionary transition from mono- to dinuclear catalytic centers, enzyme catalysis mechanism from an evolutionary perspective, overview Loligo vulgaris
additional information the phosphotriesterase diisopropyl fluorophosphatase (DFPase) is a calcium-dependent beta-propeller protein. PON1, EC 3.1.8.1, and DFPase, EC 3.1.8.2, seem to employ similar catalytic mechanisms as phosphotriesterase, due to their structural similarities of active sites. The attacking nucleophile for phosphotriester hydrolysis is identified to be an activated water molecule, with the nucleophile attacking the phosphorus center. The E53Q and D269N mutants in PON1 both possess measurable lactonase and paraoxonase activity, and mutation studies combined with related molecular dynamics simulations suggest that the water activated by Glu53 and Asp269 is the most likely attacking nucleophile. Analysis of the rate-determining reaction step of the organophosphorus compound hydrolysis catalyzed both by DFPase and PON1. Structure-function relationship, overview. Active site structure of DFPase (PDB ID 2GVW) and substrate docking Loligo vulgaris
physiological function the squid phosphotriesterase diisopropyl fluorophosphatase (DFPase) from Loligo vulgaris shows relatively specific substrate preference, efficiently catalyzing the hydrolysis of diisopropyl fluorophosphate (DFP) and G-type nerve agents, including tabun (GA), sarin (GB), soman (GD), and cyclohexyl sarin (GF). The detoxification of the organophosphorous (OP) agent is achieved by the hydrolytic reaction producing a phosphate or phosphonate and a fluoride ion Loligo vulgaris