EC Number | Cloned (Comment) | Organism |
---|---|---|
3.1.3.76 | arabinose-inducible expression of His-tagged wild-type and D9A mutant enzymes and N-terminal domains from cDNA in Escherichia coli strain BL21-AI, expression of strep-tagged enzyme from full-length gene in Escherichia coli strain XL1-Blue | Homo sapiens |
3.1.3.76 | arabinose-inducible expression of the enzyme from full-length gene in Escherichia coli strain BL21-AI | Rattus norvegicus |
3.3.2.10 | expression of His-tagged wild-type and mutant enzymes from cDNA in Escherichia coli strain BL21-AI, expression of strep-tagged enzyme from full-length gene in Escherichia coli strain XL1-Blue | Homo sapiens |
3.3.2.10 | expression of the enzyme from full-length gene in Escherichia coli strain BL21-AI | Rattus norvegicus |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
3.1.3.76 | D9A | site-directed mutagenesis, inactive mutant N-terminal domain | Homo sapiens |
3.1.3.76 | additional information | the isolated recombinant N-terminal domain is a fully active phosphatase | Homo sapiens |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
3.1.3.76 | EDTA | complete inhibition at 20 mM | Homo sapiens | |
3.1.3.76 | EDTA | complete inhibition at 20 mM | Mus musculus | |
3.1.3.76 | EDTA | complete inhibition at 20 mM | Rattus norvegicus | |
3.1.3.76 | additional information | no inhibition of the phosphatase activity by dicyclohexylurea and 4-fluorochalcone oxide | Rattus norvegicus | |
3.3.2.10 | 4-fluorochalcone oxide | inhibition of the epoxide hydrolase activity | Rattus norvegicus | |
3.3.2.10 | dicyclohexylurea | inhibition of the epoxide hydrolase activity | Rattus norvegicus |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
3.1.3.76 | additional information | - |
additional information | kinetics | Homo sapiens | |
3.1.3.76 | additional information | - |
additional information | kinetics | Rattus norvegicus | |
3.1.3.76 | 0.24 | - |
4-nitrophenyl phosphate | pH 7.8, 37°C, native enzyme | Rattus norvegicus | |
3.1.3.76 | 0.37 | - |
4-nitrophenyl phosphate | pH 7.8, 37°C, recombinant enzyme | Rattus norvegicus | |
3.1.3.76 | 1.1 | - |
4-nitrophenyl phosphate | pH 7.8, 37°C, recombinant wild-type enzyme | Homo sapiens | |
3.1.3.76 | 2.3 | - |
4-nitrophenyl phosphate | pH 7.8, 37°C, recombinant wild-type N-terminal domain | Homo sapiens | |
3.3.2.10 | 0.003 | - |
trans-stilbene oxide | native enzyme | Rattus norvegicus |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
3.1.3.76 | cytosol | - |
Mus musculus | 5829 | - |
3.1.3.76 | cytosol | - |
Homo sapiens | 5829 | - |
3.1.3.76 | cytosol | - |
Rattus norvegicus | 5829 | - |
3.3.2.10 | cytosol | - |
Homo sapiens | 5829 | - |
3.3.2.10 | cytosol | - |
Rattus norvegicus | 5829 | - |
3.3.2.10 | cytosol | - |
Mus musculus | 5829 | - |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
3.1.3.76 | Mg2+ | - |
Mus musculus | |
3.1.3.76 | Mg2+ | - |
Homo sapiens | |
3.1.3.76 | Mg2+ | required for phosphatase activity | Rattus norvegicus |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.1.3.76 | Homo sapiens | - |
- |
- |
3.1.3.76 | Mus musculus | - |
- |
- |
3.1.3.76 | Rattus norvegicus | - |
male Fischer rats | - |
3.3.2.10 | Homo sapiens | - |
- |
- |
3.3.2.10 | Mus musculus | P34914 | - |
- |
3.3.2.10 | Rattus norvegicus | - |
- |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
3.1.3.76 | from liver to homogeneity by ultracentrifugation and affinity chromatography on a benzyl thio resin using 4-fluorochalcone oxide as eluent | Rattus norvegicus |
3.1.3.76 | recombinant His-tagged wild-type and D9A mutant enzymes and N-terminal domains from Escherichia coli strain BL21-AI by nickel affinity chromatography, recombinant strep-tagged wild-type enzyme from Escherichia coli strain XL1-Blue by streptavidin affinity chromatography | Homo sapiens |
3.3.2.10 | native enzyme from liver to homogeneity by ultracentrifugation and affinity chromatography on a benzyl thio resin using 4-fluorochalcone oxide as eluent | Rattus norvegicus |
3.3.2.10 | recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21-AI by nickel affinity chromatography, recombinant strep-tagged wild-type enzyme from Escherichia coli strain XL1-Blue by streptavidin affinity chromatography | Homo sapiens |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
3.1.3.76 | (9S,10S)-10-hydroxy-9-(phosphooxy)octadecanoate + H2O = (9S,10S)-9,10-dihydroxyoctadecanoate + phosphate | the phosphatase activity of the enzyme is located at the N-terminal part, the C-terminal part harbors the epoxide hydrolase activity of EC 3.3.2.10, both catalytic sites act independently | Mus musculus | |
3.1.3.76 | (9S,10S)-10-hydroxy-9-(phosphooxy)octadecanoate + H2O = (9S,10S)-9,10-dihydroxyoctadecanoate + phosphate | the phosphatase activity of the enzyme is located at the N-terminal part, the C-terminal part harbors the epoxide hydrolase activity of EC 3.3.2.10, both catalytic sites act independently | Homo sapiens | |
3.1.3.76 | (9S,10S)-10-hydroxy-9-(phosphooxy)octadecanoate + H2O = (9S,10S)-9,10-dihydroxyoctadecanoate + phosphate | the phosphatase activity of the enzyme is located at the N-terminal part, the C-terminal part harbors the epoxide hydrolase activity of EC 3.3.2.10, both catalytic sites act independently | Rattus norvegicus | |
3.3.2.10 | an epoxide + H2O = a glycol | the C-terminal part harbors the epoxide hydrolase activity, the phosphatase activity of the enzyme is located at the N-terminal part of EC 3.1.3.76, both catalytic sites act independently | Homo sapiens | |
3.3.2.10 | an epoxide + H2O = a glycol | the C-terminal part harbors the epoxide hydrolase activity, the phosphatase activity of the enzyme is located at the N-terminal part of EC 3.1.3.76, both catalytic sites act independently | Rattus norvegicus | |
3.3.2.10 | an epoxide + H2O = a glycol | the C-terminal part harbors the epoxide hydrolase activity, the phosphatase activity of the enzyme is located at the N-terminal part of EC 3.1.3.76, both catalytic sites act independently | Mus musculus |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
3.1.3.76 | liver | - |
Mus musculus | - |
3.1.3.76 | liver | - |
Homo sapiens | - |
3.1.3.76 | liver | - |
Rattus norvegicus | - |
3.3.2.10 | liver | - |
Homo sapiens | - |
3.3.2.10 | liver | - |
Rattus norvegicus | - |
3.3.2.10 | liver | - |
Mus musculus | - |
EC Number | Storage Stability | Organism |
---|---|---|
3.1.3.76 | -70°C, 0.5 mg/ml purified enzyme, completely stable | Rattus norvegicus |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.1.3.76 | 4-methylumbelliferyl phosphate + H2O | - |
Rattus norvegicus | 4-methylumbelliferone + phosphate | - |
? | |
3.1.3.76 | 4-nitrophenyl phosphate + H2O | - |
Mus musculus | 4-nitrophenol + phosphate | - |
? | |
3.1.3.76 | 4-nitrophenyl phosphate + H2O | - |
Homo sapiens | 4-nitrophenol + phosphate | - |
? | |
3.1.3.76 | 4-nitrophenyl phosphate + H2O | - |
Rattus norvegicus | 4-nitrophenol + phosphate | - |
? | |
3.1.3.76 | additional information | no activity with 4-nitrophenyl sulfate of the isolated recombinant N-terminal domain | Homo sapiens | ? | - |
? | |
3.3.2.10 | trans-stilbene oxide + H2O | - |
Homo sapiens | ? | - |
? | |
3.3.2.10 | trans-stilbene oxide + H2O | - |
Rattus norvegicus | ? | - |
? | |
3.3.2.10 | trans-stilbene oxide + H2O | - |
Mus musculus | ? | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
3.1.3.76 | dimer | - |
Mus musculus |
3.1.3.76 | dimer | - |
Homo sapiens |
3.1.3.76 | dimer | - |
Rattus norvegicus |
3.1.3.76 | More | the phosphatase activity of the enzyme is located at the 35 kDa N-terminal part which has a alpha/beta-fold, the 25 kDa C-terminal part, with a different hydrolase alpha/beta-fold, harbors the epoxide hydrolase activity of EC 3.3.2.10, structure analysis | Mus musculus |
3.1.3.76 | More | the phosphatase activity of the enzyme is located at the 35 kDa N-terminal part which has a alpha/beta-fold, the 25 kDa C-terminal part, with a different hydrolase alpha/beta-fold, harbors the epoxide hydrolase activity of EC 3.3.2.10, structure analysis | Homo sapiens |
3.1.3.76 | More | the phosphatase activity of the enzyme is located at the 35 kDa N-terminal part which has a alpha/beta-fold, the 25 kDa C-terminal part, with a different hydrolase alpha/beta-fold, harbors the epoxide hydrolase activity of EC 3.3.2.10, structure analysis | Rattus norvegicus |
3.3.2.10 | dimer | - |
Homo sapiens |
3.3.2.10 | dimer | - |
Rattus norvegicus |
3.3.2.10 | dimer | - |
Mus musculus |
3.3.2.10 | More | the 25 kDa C-terminal part, with a different hydrolase alpha/beta-fold, harbors the epoxide hydrolase activity, the enzyme's phosphatase activity of EC3.1.3.76 is located at the 35 kDa N-terminal part which has a alpha/beta-fold, structure analysis | Homo sapiens |
3.3.2.10 | More | the 25 kDa C-terminal part, with a different hydrolase alpha/beta-fold, harbors the epoxide hydrolase activity, the enzyme's phosphatase activity of EC3.1.3.76 is located at the 35 kDa N-terminal part which has a alpha/beta-fold, structure analysis | Rattus norvegicus |
3.3.2.10 | More | the 25 kDa C-terminal part, with a different hydrolase alpha/beta-fold, harbors the epoxide hydrolase activity, the enzyme's phosphatase activity of EC3.1.3.76 is located at the 35 kDa N-terminal part which has a alpha/beta-fold, structure analysis | Mus musculus |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.1.3.76 | More | EC 3.1.3.76 belongs to the haloacid dehalogenase superfamily of enzymes, c.f. EC 3.3.2.10 | Homo sapiens |
3.1.3.76 | More | EC 3.1.3.76 belongs to the haloacid dehalogenase superfamily of enzymes, see also EC 3.3.2.10 | Mus musculus |
3.1.3.76 | More | EC 3.1.3.76 belongs to the haloacid dehalogenase superfamily of enzymes, see also EC 3.3.2.10 | Rattus norvegicus |
3.3.2.10 | SEH | - |
Homo sapiens |
3.3.2.10 | SEH | - |
Rattus norvegicus |
3.3.2.10 | SEH | - |
Mus musculus |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.1.3.76 | 37 | - |
assay at | Mus musculus |
3.1.3.76 | 37 | - |
assay at | Homo sapiens |
3.1.3.76 | 37 | - |
assay at | Rattus norvegicus |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
3.1.3.76 | 0.0061 | - |
4-nitrophenyl phosphate | pH 7.8, 37°C, recombinant wild-type enzyme | Homo sapiens | |
3.1.3.76 | 0.013 | - |
4-nitrophenyl phosphate | pH 7.8, 37°C, recombinant wild-type N-terminal domain | Homo sapiens | |
3.1.3.76 | 0.84 | - |
4-nitrophenyl phosphate | pH 7.8, 37°C, native enzyme | Rattus norvegicus | |
3.1.3.76 | 1.61 | - |
4-nitrophenyl phosphate | pH 7.8, 37°C, recombinant enzyme | Rattus norvegicus | |
3.3.2.10 | 0.5 | - |
trans-stilbene oxide | native enzyme | Rattus norvegicus |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
3.1.3.76 | 7.8 | - |
assay at | Mus musculus |
3.1.3.76 | 7.8 | - |
assay at | Homo sapiens |
3.1.3.76 | 7.8 | - |
assay at | Rattus norvegicus |
EC Number | Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|---|
3.3.2.10 | 0.00003 | - |
dicyclohexylurea | native enzyme | Rattus norvegicus | |
3.3.2.10 | 0.0005 | - |
4-fluorochalcone oxide | native enzyme | Rattus norvegicus |