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Literature summary extracted from

  • Cronin, A.; Mowbray, S.; Duerk, H.; Homburg, S.; Fleming, I.; Fisslthaler, B.; Oesch, F.; Arand, M.
    The N-terminal domain of mammalian soluble epoxide hydrolase is a phosphatase (2003), Proc. Natl. Acad. Sci. USA, 100, 1552-1557.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

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

Protein Variants

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

Inhibitors

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

KM Value [mM]

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

Localization

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
-

Metals/Ions

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

Organism

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
-
-
-

Purification (Commentary)

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

Reaction

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

Source Tissue

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
-

Storage Stability

EC Number Storage Stability Organism
3.1.3.76 -70°C, 0.5 mg/ml purified enzyme, completely stable Rattus norvegicus

Substrates and Products (Substrate)

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 ?
-
?

Subunits

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

Synonyms

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

Temperature Optimum [°C]

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

Turnover Number [1/s]

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

pH Optimum

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

Ki Value [mM]

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