Sandbox Reserved 714: Difference between revisions
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As many enzymes, the human soluble epoxide hydrolase can be inhibited by some inhibitors, causing a loss of activity for the enzyme. | As many enzymes, the human soluble epoxide hydrolase can be inhibited by some inhibitors, causing a loss of activity for the enzyme. | ||
The sEH can be inhibited by some metal ions such as Zn<sup>2+</sup>, Cu<sup>2+</sup>, Hg<sup>2+</sup>. It is a noncompetitive inhibition: the metal ion binding to the enzyme reduces its activity without affecting directly the substrate binding, so that the V<sub>max</sub> decreases but the K<sub>m</sub> remains unchanged. It may be that those metal ions replace the Mg<sup>2+</sup> in the N-term active site of the enzyme subunits, which can result in some conformation changes, but this is only an hypothesis. | The sEH can be inhibited by some metal ions such as Zn<sup>2+</sup>, Cu<sup>2+</sup>, Hg<sup>2+</sup> <ref name="EH" />. It is a noncompetitive inhibition: the metal ion binding to the enzyme reduces its activity without affecting directly the substrate binding, so that the V<sub>max</sub> decreases but the K<sub>m</sub> remains unchanged. It may be that those metal ions replace the Mg<sup>2+</sup> in the N-term active site of the enzyme subunits, which can result in some conformation changes, but this is only an hypothesis. | ||
However, there are also some chemical inhibitors that inhibit the sEH. They are 1-3 disubstitued ureas, carbamates and amides, which are stable inhibitors for the sEH. | However, there are also some chemical inhibitors that inhibit the sEH. They are 1-3 disubstitued ureas, carbamates and amides, which are stable inhibitors for the sEH. | ||