Sandbox Reserved 714
From Proteopedia
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The C-terminal domain is called Cytosolic epoxide hydrolase 2: it catalyzes the trans-addition of water to epoxides in order to product glycols. The <scene name='Sandbox_Reserved_714/Cter_activesite/3'>active site</scene> is made of five residues. The 3D structure of this active site is maintained by hydrogen bonds, including those created by D496. The two tyrosines (Y383 and Y466) assist the proper positioning of the substrate by polarizing it, thanks to their hydroxyl groups. D335 plays the role of the nucleophilic acid. Finally, H524 plays the role of a base in order to release the final product. | The C-terminal domain is called Cytosolic epoxide hydrolase 2: it catalyzes the trans-addition of water to epoxides in order to product glycols. The <scene name='Sandbox_Reserved_714/Cter_activesite/3'>active site</scene> is made of five residues. The 3D structure of this active site is maintained by hydrogen bonds, including those created by D496. The two tyrosines (Y383 and Y466) assist the proper positioning of the substrate by polarizing it, thanks to their hydroxyl groups. D335 plays the role of the nucleophilic acid. Finally, H524 plays the role of a base in order to release the final product. | ||
| - | The N- | + | The N-terminal domain is responsible of the Mg2+ dependant hydrolysis of p-nitrophenyl phosphate. 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. |
Revision as of 20:05, 30 December 2012
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Proteopedia Page Contributors and Editors
DUTREUX Fabien, BONHOURE Anna
