Sandbox GGC14: Difference between revisions
No edit summary |
No edit summary |
||
| Line 5: | Line 5: | ||
== Function == | == 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 contributer to the activity of the enzyme is the | 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 contributer to the activity of the enzyme is the 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. The one located in the acyl ester intermediate functions as the main active site. It is located deep in the gorge lined largely by aromatic residues along with many Serines and this specific sites mutation causes a loss in activity. | ||
Another structure that contributes greatly to the function of the protein is the ligand binding and interactions of the molecule. It is important to note that there is a high binding affinity for ligands to the structure. This in turn is what increases the enzymes catalytic rate. | |||
== Disease == | == Disease == | ||