EC Number | Activating Compound | Comment | Organism | Structure |
---|---|---|---|---|
3.1.8.2 | 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 |
EC Number | Application | Comment | Organism |
---|---|---|---|
3.1.8.2 | 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 |
EC Number | Cloned (Comment) | Organism |
---|---|---|
3.1.8.2 | recombinant expression of His-tagged wild-type and engineered enzymes in Escherichia coli strain BL21 (IDE3) pLysS | Loligo vulgaris |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
3.1.8.2 | 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 |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
3.1.8.2 | additional information | - |
additional information | Michaelis-Menten kinetics | Loligo vulgaris |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
3.1.8.2 | Co2+ | activates | Loligo vulgaris |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.1.8.2 | diisopropyl fluorophosphate + H2O | Loligo vulgaris | - |
diisopropyl phosphate + fluoride | - |
? | |
3.1.8.2 | 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) | ? | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.1.8.2 | Loligo vulgaris | Q7SIG4 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
3.1.8.2 | recombinant His-tagged wild-type and engineered enzymes from Escherichia coli strain BL21 (IDE3) pLysS | Loligo vulgaris |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
3.1.8.2 | brain | - |
Loligo vulgaris | - |
3.1.8.2 | ganglion | - |
Loligo vulgaris | - |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
3.1.8.2 | 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 |
3.1.8.2 | 382.39 | - |
purified recombinant engineered His-tagged InaV-N-DFPase enzyme, substrate paraoxon, pH 7.2, 30°C | Loligo vulgaris |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.1.8.2 | diethyl-paraoxon + H2O | reaction of EC 3.1.8.1, paraoxonase | Loligo vulgaris | diethyl phosphate + 4-nitrophenol | - |
? | |
3.1.8.2 | diisopropyl fluorophosphate + H2O | - |
Loligo vulgaris | diisopropyl phosphate + fluoride | - |
? | |
3.1.8.2 | 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 | ? | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
3.1.8.2 | ? | 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 |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.1.8.2 | DFPase | - |
Loligo vulgaris |
3.1.8.2 | diisopropylfluorophosphatase | - |
Loligo vulgaris |
3.1.8.2 | More | cf. EC 3.1.8.1 | Loligo vulgaris |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.1.8.2 | additional information | - |
very low activity of whole cells at 60°C | Loligo vulgaris |
3.1.8.2 | 30 | - |
recombinant enzyme | Loligo vulgaris |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
3.1.8.2 | 7.2 | - |
assay at | Loligo vulgaris |