Gene_locus Report for: human-EPHX1
human-EPHX1 | Name | Homo sapiens (Human) microsomal epoxide hydrolase HYEP mEH, epoxide hydratase EPHX1 |
| Species | Homo sapiens |
| Organism | man |
| Gene_name | EPHX1 |
| | mEH |
| | HmEH |
| Block | X |
| Family | Epoxide_hydrolase |
| Disease | Lipoatrophic diabetes |
| | Familial hypercholanemia |
| Allelic_variant | 4kbup_human-EPHX1 |
| | IVS1_human-EPHX1 |
| Xenobiotic_sensitivity | Defect in hydroxylation of diphenylhydantoin |
| Database (12) |
| Paper (20) |
| Comment | Epoxide hydrolases (EC 3.3.2.3) play an important role in both the activation and detoxification of exogenous chemicals such as polycyclic aromatic hydrocarbons. Mutant form of microsomal epoxide hydrolase is the molecular basis for abnormal reactions to phenytoin (diphenylhydantoin, dilantin) and some other drugs. Hydantoin used during pregnancy for seizure prophylaxis can result in children with the fetal hydantoin syndrome (FHS)(major birth defects including congenital heart disease, cleft lip/palate, microcephaly, and major genitourinary, eye, and limb defects) Defect in hydroxylation of diphenylhydantoin is related to a mutation in human-EPHX1 resulting in low activity. Familial hypercholanemia is characterized by elevated serum bile acid concentrations, itching, and fat malabsorption. In a patient with hypercholanemia. Zhu et al. (2003) identified compound heterozygosity for 2 mutations in the EPHX1 gene, which resulted in a significant decrease in EPHX1 promoter activity |
| Sequence | human-EPHX1 |
| Protein | human-EPHX1 |
| Peptide | human-EPHX1 |
| Mutation (6) |
| Inhibitor (6) |
| Substrate (6) |
| Tree_node | Epoxide-hydrolase_like190019 |
| | Epoxide_hydrolase193517 |
| OldTrembl | B2R8N0 |
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