Due to the off catalytic binding site nature of the herbicidal small molecules with respect to the catalytic action it is interesting to understand what mutations do in regards to resistance. The simplest guess is that the entry door is closed by an herbicide and no pyruvates or 2ketobuyrate are allowed into the channel. In a typical inhibitor process the small molecule blocks the catalytic action by directly binding to the active amino acids, thus blocking natural function. A point mutation of an amino acid in this site could block the inhibitor from binding (non-covalently or covalently) or cause a conformational change in the region of the activity, both from a structural change of the catalytic site amino acids. With AHAS the catalytic site is unchanged, and a physical dynamical pathway to it is blocked by a small molecule if it bound strongly enough. Because the herbicide site is not a part of the AHAS function chemically in synthesis of amino acids, a simple explanation of resistance by point mutation is that the site is altered to not allow binding to the small molecule or to reduce it substantially. The wrong type of mutation, however, may facilitate the activity of the acetolactate production, by opening the entry door even wider; this would manifest through increased production of the 3 branched-chain amino acids .