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Literature summary for 3.1.3.76 extracted from
- The soluble epoxide hydrolase encoded by EPXH2 is a bifunctional enzyme with novel lipid phosphate phosphatase activity (2003), Proc. Natl. Acad. Sci. USA, 100, 1558-1563.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression of wild-type and mutant enzymes in insect cells using the baculovirus infection system | Homo sapiens |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| Y465F | site-directed mutagenesis, mutant enzyme shows phosphatase, but no epoxide hydrolase activity | Homo sapiens |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| 4-fluorochalcone oxide | 8% inhibition at 0.1 mM | Homo sapiens |  |
| 4-Phenylchalcone oxide | 11% inhibition at 0.1 mM | Homo sapiens | |
| Cd2+ | - |
Homo sapiens | |
| Cu2+ | - |
Homo sapiens | |
| Hg2+ | - |
Homo sapiens | |
| additional information | poor or no inhibition by chalcone oxide, 1-cyclohexyl-3-ethyl urea, 1-cyclohexyl-3-hexyl urea, 1-cyclohexyl-3-dodecyl urea, 1,3-dicyclohexyl urea, okadaic acid, tartaric acid, and sodium orthovanadate | Homo sapiens | |
| Sodium fluoride | 10% inhibition at 1.0 mM | Homo sapiens | |
| Sodium molybdate | 8% inhibition at 1.0 mM | Homo sapiens | |
| Zn2+ | - |
Homo sapiens | |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | kinetics, recombinant enzyme | Homo sapiens | |
| 0.02 | - |
threo-10-phosphonooxy-9-hydroxy-octadecanoic acid | pH 7.0, 30°C, recombinant enzyme | Homo sapiens | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Co2+ | half as effective as Mg2+ | Homo sapiens | |
| Mg2+ | dependent on, optimal at 1 mM MgCl2, one Mg2+ per catalytic subunit, dissociation constants, recombinant enzyme | Homo sapiens | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| (9E)-12-phosphonooxyoctadec-9-enoic acid + H2O | Homo sapiens | - |
(9E)-12-hydroxyoctadec-9-enoic acid + phosphate | - |
? | |
| (9Z)-12-phosphonooxyoctadec-9-enoic acid + H2O | Homo sapiens | - |
(9Z)-12-hydroxyoctadec-9-enoic acid + phosphate | - |
? | |
| 12-phosphonooxyoctadecanoic acid + H2O | Homo sapiens | - |
12-hydroxyoctadecanoic acid + phosphate | - |
? | |
| erythro-9,10-phosphonooxy-hydroxy-octadecanoic acid + H2O | Homo sapiens | - |
? | - |
? | |
| threo-9,10-phosphonooxy-hydroxy-octadecanoic acid + H2O | Homo sapiens | - |
? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | - |
gene EPXH2 | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant wild-type and mutant enzymes from insect cells by affinity chromatography | Homo sapiens |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| (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 |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| additional information | - |
optimization of activity assay conditions with the recombinant enzyme, maximal in 25 mM Tris buffer, pH 7.0, 30°C, 1 mM MgCl2 | Homo sapiens |
| 0.0954 | - |
purified recombinant enzyme | Homo sapiens |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| (9E)-12-phosphonooxyoctadec-9-enoic acid + H2O | - |
Homo sapiens | (9E)-12-hydroxyoctadec-9-enoic acid + phosphate | - |
? | |
| (9Z)-12-phosphonooxyoctadec-9-enoic acid + H2O | - |
Homo sapiens | (9Z)-12-hydroxyoctadec-9-enoic acid + phosphate | - |
? | |
| 12-phosphonooxyoctadecanoic acid + H2O | - |
Homo sapiens | 12-hydroxyoctadecanoic acid + phosphate | - |
? | |
| 4-nitrophenyl phosphate + H2O | - |
Homo sapiens | 4-nitrophenol + phosphate | - |
? | |
| erythro-10-phosphonooxy-9-hydroxy-octadecanoic acid + H2O | - |
Homo sapiens | erythro-9,10-dihydroxyoctadecanoate + phosphate | - |
? | |
| erythro-9,10-phosphonooxy-hydroxy-octadecanoic acid + H2O | - |
Homo sapiens | ? | - |
? | |
| threo-10-phosphonooxy-9-hydroxy-octadecanoic acid + H2O | - |
Homo sapiens | threo-9,10-dihydroxyoctadecanoate + phosphate | - |
? | |
| threo-9,10-phosphonooxy-hydroxy-octadecanoic acid + H2O | - |
Homo sapiens | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| 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 |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| EPXH2 | - |
Homo sapiens |
| More | EC 3.1.3.76 belongs to the haloacid dehalogenase superfamily of enzymes, c.f. EC 3.3.2.10 | Homo sapiens |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | - |
recombinant enzyme | Homo sapiens |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7 | - |
recombinant enzyme | Homo sapiens |
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