Acetylcholine esterase is an important enzyme in neural synaptic signal transmission. It breaks down the neurotransmitter acetylcholine after it binds the acetylcholine receptor. Its active site has the same features used by serine proteases. Here is the reaction catalyzed by Acetylcholine esterase: Acetylcholine + H Choline OH + Acetate + H Acetylcholine is an ester, while peptide bonds cleaved by proteases are amides. How should acetylcholine estease's mechanism accommodate this? This cannot be determined from the information presented in class and in this question. For amides, the amide nitrogen is deprotonate to make it more like an ester. The same mechanism cleaves deprotonated amides and esters. No changes are needed. The mechanism same works for esters and amides. Prior to cleavage, a transamination converts the ester to an amide. The esterase will make a covalent intermediate to an amine to create the amide to be cleaved.

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Acetylcholine esterase is an important enzyme in neural synaptic signal transmission.
It breaks down the neurotransmitter acetylcholine after it binds the acetylcholine
receptor. Its active site has the same features used by serine proteases.
Here is the reaction catalyzed by Acetylcholine esterase:
Acetylcholine
Choline
OH
Acetate
+ H
Acetylcholine is an ester, while peptide bonds cleaved by proteases are amides. How
should acetylcholine estease's mechanism accommodate this?
This cannot be determined from the information presented in class and in this
question.
For amides, the amide nitrogen is deprotonate to make it more like an ester. The
same mechanism cleaves deprotonated amides and esters.
No changes are needed. The mechanism same works for esters and amides.
Prior to cleavage, a transamination converts the ester to an amide.
The esterase will make a covalent intermediate to an amine to create the amide
to be cleaved.
Transcribed Image Text:Acetylcholine esterase is an important enzyme in neural synaptic signal transmission. It breaks down the neurotransmitter acetylcholine after it binds the acetylcholine receptor. Its active site has the same features used by serine proteases. Here is the reaction catalyzed by Acetylcholine esterase: Acetylcholine Choline OH Acetate + H Acetylcholine is an ester, while peptide bonds cleaved by proteases are amides. How should acetylcholine estease's mechanism accommodate this? This cannot be determined from the information presented in class and in this question. For amides, the amide nitrogen is deprotonate to make it more like an ester. The same mechanism cleaves deprotonated amides and esters. No changes are needed. The mechanism same works for esters and amides. Prior to cleavage, a transamination converts the ester to an amide. The esterase will make a covalent intermediate to an amine to create the amide to be cleaved.
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