Sandbox GGC14

Human acetylcholinesterase (AChE) is an enzyme which inhibits the function acetylcholine by way of a rapid hydrolysis. It is classified as a toxin/ hydrolase and has been linked to things such as snake venom and has been used in the the development of treatment for diseases which involve the nervous system and the transmission of signals to muscles. This specific enzyme has 3 active binding sites and 6 mutations. Each of which either causing a loss of activity or a mis-folding.

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Function

Acetylcholinesterase functions primarily in the synaptic cleft to stop the signal to the neurotransmitter. This is done by way of a rapid hydrolysis reaction of acetylcholine yielding the products acetate, choline and a hydrogen ion. In conjunction with its biological function it has an unusually high catalytic activity because considering the fact that it is a serine hydrolase it functions more closely to the rate of a limitation by diffusion control. [1] A big part of the reason that acetylcholinesterase is so active is because of mutagenesis. The mutations noted are at positions 234, 365, and 478, these are all also the active sites of the enzyme. One happens at the acyl ester intermediate while the other two are at a sort of charge relay system.

Disease

alzeihmers mutations

Relevance

treatment of diseases

testing

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Structural highlights

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Scene 5

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