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Literature summary extracted from

  • Allahyari, H.; Latifi, A.
    Diisopropyl-fluorophosphatase as a catalytic bioscavenger (2016), J. Appl. Biotechnol. Rep., 3, 477-482 .
No PubMed abstract available

Application

EC Number Application Comment Organism
3.1.8.2 environmental protection enzyme DFPase can be used as in vivo detoxifying agent for elimination of organophosphorus chemicals, used as pesticides and warfare nerve agent, e.g. sarin, soman, or tabun Loligo vulgaris
3.1.8.2 medicine enzyme DFPase can be used as in vivo detoxifying agent for elimination of organophosphorus chemicals, used as pesticides and warfare nerve agent, e.g. sarin, soman, or tabun Loligo vulgaris

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.8.2 Ca2+ required, metal center ligation of DFPase, structure overview Loligo vulgaris

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.1.8.2 additional information Loligo vulgaris diisopropyl-fluorophosphatase (DFPase) from Loligo vulgaris is highly stable and robust biocatalyst for the hydrolysis of various chemical warfare agents such as sarin, soman, tabun, but no natural substrate for DFPase has been identified to date ?
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?

Organism

EC Number Organism UniProt Comment Textmining
3.1.8.2 Loligo vulgaris Q7SIG4
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-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.1.8.2 side-chain modification covalent attachment of polyethylene glycol (PEG) chains to enzymes is a prominent solution to overcome these issues. PEGylation enlarges the hydrodynamic radius of proteins and shields its surface. PEG modification increases the stability against proteases, reduces immunogenicity, and delays renal excretion significantly leading to prolonged half-life, reduced side effects, and increased pharmacological efficiency Loligo vulgaris

Reaction

EC Number Reaction Comment Organism Reaction ID
3.1.8.2 diisopropyl fluorophosphate + H2O = diisopropyl phosphate + fluoride analysis of the catalytic reaction mechanism of the enzyme. Proposed mechanism for phosphoenzyme intermediate formation involving Asp229 as the nucleophile. (i) Asp229 attacks the phosphorus center of DFP to form a pentavalent intermediate and (ii) the P-F bond dissociates to form a tetrahedral phosphoenzyme intermediate. Hydrolysis of the phosphoenzyme intermediate is not shown. And proposed mechanism for hydrolysis involving an activated water as the nucleophile. (i) Asp229 abstracts a proton from a water molecule either stepwise or in concert as (ii) water attacks the phosphorus center, (iii) Glu21 abstracts a proton either stepwise or in concert as water forms a bond with phosphorus, and (iv) the P-F bond dissociates Loligo vulgaris

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.1.8.2 brain
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Loligo vulgaris
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3.1.8.2 ganglion
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Loligo vulgaris
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.8.2 (RS)-propan-2-yl methylphosphonofluoridate + H2O i.e. sarin Loligo vulgaris isopropyl phosphate methylphosphonate + fluoride
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?
3.1.8.2 3-[fluoro(methyl)phosphoryl]oxy-2,2-dimethylbutane + H2O i.e. soman Loligo vulgaris 3,3-dimethylbutan-2-yl methylphosphonate + fluoride
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?
3.1.8.2 chlorpyrifos + H2O
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Loligo vulgaris ?
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?
3.1.8.2 cyclohexylmethylphosphonofluoridate + H2O i.e. cyclosarin Loligo vulgaris cyclohexyl methylphosphonate + fluoride
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?
3.1.8.2 diisopropyl fluorophosphate + H2O
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Loligo vulgaris diisopropyl phosphate + fluoride
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?
3.1.8.2 ethyl dimethylphosphoramidocyanidate + H2O i.e. tabun Loligo vulgaris ?
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?
3.1.8.2 additional information diisopropyl-fluorophosphatase (DFPase) from Loligo vulgaris is highly stable and robust biocatalyst for the hydrolysis of various chemical warfare agents such as sarin, soman, tabun, but no natural substrate for DFPase has been identified to date Loligo vulgaris ?
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?
3.1.8.2 additional information the enzyme is not hydrolytically active against compounds with P-O or P-S leaving group bonds, except for some soman derivatives, and shows no efficient hydrolytic activity against lactones or esters Loligo vulgaris ?
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?

Subunits

EC Number Subunits Comment Organism
3.1.8.2 More the molecular conformation of DFPase is similar to other phosphotriesterases such as paraoxonase 1 (PON1, EC 3.1.8.1) Loligo vulgaris

Synonyms

EC Number Synonyms Comment Organism
3.1.8.2 DFPase
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Loligo vulgaris

General Information

EC Number General Information Comment Organism
3.1.8.2 additional information in detoxification of nerve gas compounds or pesticides in the human body, due to non-human origin of the enzyme, immunological reactions occur when it is injected into body. In order to using DFPase as in vivo detoxifying agent, some manipulations to augment of its efficiency and to decrease of immunogenic problems are needed. Modifications such as PEGylation is one of the possible solutions to conquer these problems Loligo vulgaris