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Briefly explain the role of glutamic acid E327, histidine H440 and serine S220 in acetylcholinesterase catalysis.

Briefly explain the role of glutamic acid E327, histidine H440 and serine S220 in acetylcholinesterase catalysis.

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Answer :

One conserved domain of Acetyl Choline esterase, is a catalytic triad of residues at the active site. Composed of a serine, glutamate and histidine.

The active site consists of the forementioned catalytic triad of residues, Glu 327, His 440, and Ser 220. They cleave the substrate molecule.

Serine acts as a nucleophile to attack the carbonyl carbon of its substrate, acetyl choline.

Histidine functions as a general acid base catalyst to increase nucleophilicity of serine.

Glutamate stabilizes the transition state through low barrier hydrogen bonding.

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