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Sebastián Galaz, Luis Morales-Quintana, María Alejandra Moya-León and Raúl Herrera Structural analysis of the alcohol acyltransferase protein family from Cucumis melo shows that enzyme activity depends on an essential solvent channel FEBS Journal 280

Article first published online: 13 FEB 2013 | DOI: 10.1111/febs.12127

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CmAAT2-ligands complexes show the alcohol located far from the catalytic residues. The longer distance to both catalytic residues contrasts with the shorter distance to A268 in the alternative pocket. In the case of CmAAT1-ligands complex H161 establish a hydrogen bond with the hydroxyl group of acetyl-CoA and D165 establish a hydrogen bond with the hexanol. This explains the differences in the activity for both enzymes

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