Sandbox Reserved 714: Difference between revisions
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=== N-terminal domain === | === N-terminal domain === | ||
The N-terminal domain is responsible of the Mg<sup>2+</sup> dependant hydrolysis of | The N-terminal domain is responsible of the Mg<sup>2+</sup> dependant hydrolysis of dihydroxy lipid phosphates <ref>PMID:15096040</ref> <ref>PMID:12574510</ref>. Its <scene name='Sandbox_Reserved_714/Nter_activesite/1'>active site</scene> contains several conserved aspartates in phosphatases and phosphonatases: D9, D11, D184 and D185. This enzymatic activity is Mg<sup>2+</sup> dependant, because the structure of the active site is in its optimal conformation when the cation makes coordination interactions. When the catalytic activity of the N-term domain is available, Magnesium is octahedrally coordinated with the four aspartates, one water molecule and the phosphate belonging to the substrate. | ||
== Inhibitors == | == Inhibitors == |