Abstract
Enzyme kinetic parameters of the bioactivation of thiourea-containing compounds by human flavin-containing monooxygenase enzymes (FMOs) FMO1 and FMO3 were investigated. A microtitre-based adaptation of methodology described for the thiourea-dependent oxidation of thiocholine was used to determine the turnover of thiourea-containing compounds by human FMO1 and FMO3. The results show that major differences in enzyme kinetic parameters for N-substituted N′-(4-imidazole-ethyl)thiourea exist between human FMO3 and human FMO1. Whereas K
| Original language | English |
|---|---|
| Pages (from-to) | 645-57 |
| Journal | Xenobiotica |
| Volume | 36 |
| Issue number | 7 |
| DOIs | |
| Publication status | Published - 2006 |
UN SDGs
This output contributes to the following UN Sustainable Development Goals (SDGs)
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SDG 6 Clean Water and Sanitation
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