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In the 21st Century, Alzheimer's disease has become a global concern. Comprehensive studies throughout the world are being done to investigate this issue. Unfortunately, the percentage of people with Alzheimer's disease is rapidly increasing(the number of people dealing with Alzheimer is rapidly increasing). The disease imposes high spiritual and material costs to society(This disease has led to many problems and costs in various fields for modern societies). Despite extensive researches, available pathogens that involved in the outbreak of Alzheimer's disease are still indefinite,( studies reveal that between 1 to 5 percent of patients are suffering from genetic disorders though). Although ...view middle of the document...

Another important cholinesterase with 65% identical sequence with the acetylcholinesterase enzyme (AChE) is butyrylcholinesterase(BChE). This enzyme is able to hydrolyze butyrylcholine with high-speed and acetylcholine with low-speed. Its molecular shape and active site are very similar to acetylcholinesterase. Coincides with disease progression, BChE levels in the brain are increasing. Although its operation speed is low but its considerable impacts in reducing acetylcholine levels are non-venial. The active site of the both enzymes is formed of three amino acids (serine, histidine and glutamate) that is called the catalytic triad. The catalytic site (CAS) in both enzymes is a narrow gorge at a depth of 20Å where hydrolysis reaction takes place in it. In AchE, acyl binding pocket is composed of Phe288 and Phe290 residues near the catalytic triad but for BChE, this site consist of Leu286 and Val288 residues at the same location. This site is responsible for substrate specificity. The differences in mentioned amino acids lead to specific interaction of these enzymes with different ligands.
Trp84 and Phe330 are two important aromatic amino acids that make up choline binding site of the acetylcholinesterase enzyme (anionic site). They play pivotal role in the hydrolysis process. Tryptophan amino acid (Trp82) plays its role again in choline binding site of human BuChE. The substrate quaternary ammonium group bindings in this place with cation-π interactions. These interactions with the anionic site are responsible for the proper orientation of acetylcholine in the gorge. This orientation enables inhibitor for the effective binding to the enzyme. Two glycine amino acids and one alanine amino acid are the components of oxyanion hole in the vicinity the choline binding site but...

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