4.3.2.10 | 7-benzyl-8-[(1-[[(2-hydroxyethyl)amino]methyl]propyl)amino]-1,3-dimethyl-2,3,6,7-tetrahydro-1H-2,6-purinedione |
glutaminase activity is substantially suppressed upon binding of the inhibitor to the HisH-HisF interface. The allosteric inhibitor is able to uncouple motions induced by the effector ligand with essential motions in the distant active site, favoring an inactive conformation of this V-type enzyme |
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