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Literature summary for 3.1.8.2 extracted from
- Efficient surface display of diisopropylfluorophosphatase (DFPase) in E. coli for biodegradation of toxic organophosphorus compounds (DFP and Cp) (2015), Appl. Biochem. Biotechnol., 177, 624-636 .
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| additional information | presence of glucose-mineral-salt (GMS) supplemented with tryptone and 100 mg/l Co2+ ion increases the specific activity of the recombinant enzyme | Loligo vulgaris |
Application
| Application | Comment | Organism |
|---|---|---|
| environmental protection | the engineered bacterium, prepared with an N-terminal domain of the ice nucleation protein (InaV-N) as an anchoring motif on cell surface of expressing bacteria, can be used in the bioremediation of pesticide-contaminated environments | Loligo vulgaris |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| recombinant expression of His-tagged wild-type and engineered enzymes in Escherichia coli strain BL21 (IDE3) pLysS | Loligo vulgaris |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | intracellular production of organophosphorus pesticides (OPs)-degrading enzymes or the use of native bacteria and fungi leads to a low degradation rate of OPs due to a mass transfer issue which reduces the overall catalytic efficiency. To overcome this challenge, DFPase is expressed on the surface of Escherichia coli for the first time by employing the N-terminal domain of the ice nucleation protein (InaV-N) as an anchoring motif. The recombinant DFPase is successfully located on the outer membrane and shows a significant ability for the biodegradation of diisopropylfluorophosphate (DFP) with a specific activity of 500 U/mg of wet cell weight. The recombinant cells can also degrade chlorpyrifos. No enzyme activity is measured by the fluoride ion-selective electrode in the control sample, inner membrane fraction, or cytoplasm fraction of pET-28a-InaV-N-DFPase cells. High potential of the InaV-N anchoring domain to produce an engineered bacterium that can be used in the bioremediation of pesticide-contaminated environments | Loligo vulgaris |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | Michaelis-Menten kinetics | Loligo vulgaris |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Co2+ | activates | 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 | - |
? | |
| additional information | Loligo vulgaris | the diisopropylfluorophosphatase (DFPase) from the ganglion and brain of Loligo vulgaris acts on P-F bonds present in some organophosphorus pesticides (OPs) | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Loligo vulgaris | Q7SIG4 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His-tagged wild-type and engineered enzymes from Escherichia coli strain BL21 (IDE3) pLysS | Loligo vulgaris |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| brain | - |
Loligo vulgaris | - |
| ganglion | - |
Loligo vulgaris | - |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| additional information | - |
a maximum number of 53560000 molecules of diisopropyl fluorophosphate is hydrolyzed per minute per whole cell in the presence of glucose-mineral-salt (GMS) supplemented with tryptone and 100 ppm Co2+ ion. 34.69 U/ml with substrate paraoxon, pH 7.2, 30°C | Loligo vulgaris |
| 382.39 | - |
purified recombinant engineered His-tagged InaV-N-DFPase enzyme, substrate paraoxon, pH 7.2, 30°C | Loligo vulgaris |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| diethyl-paraoxon + H2O | reaction of EC 3.1.8.1, paraoxonase | Loligo vulgaris | diethyl phosphate + 4-nitrophenol | - |
? | |
| diisopropyl fluorophosphate + H2O | - |
Loligo vulgaris | diisopropyl phosphate + fluoride | - |
? | |
| additional information | the diisopropylfluorophosphatase (DFPase) from the ganglion and brain of Loligo vulgaris acts on P-F bonds present in some organophosphorus pesticides (OPs) | Loligo vulgaris | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 56847, wild-type enzyme, sequence calculation, x * 55000, recombinant wild-type enzyme, SDS-PAGE, x * 77000, recombinant engineered His-tagged InaV-N-DFPase enzyme, SDS-PAGE | Loligo vulgaris |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| DFPase | - |
Loligo vulgaris |
| diisopropylfluorophosphatase | - |
Loligo vulgaris |
| More | cf. EC 3.1.8.1 | Loligo vulgaris |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| additional information | - |
very low activity of whole cells at 60°C | Loligo vulgaris |
| 30 | - |
recombinant enzyme | Loligo vulgaris |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.2 | - |
assay at | Loligo vulgaris |
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