What does acetylcholinesterase break down?
Acetylcholinesterase (AChE) is a cholinergic enzyme primarily found at postsynaptic neuromuscular junctions, especially in muscles and nerves. It immediately breaks down or hydrolyzes acetylcholine (ACh), a naturally occurring neurotransmitter, into acetic acid and choline.
What enzyme breaks down acetylcholinesterase?
Cholinesterase
Cholinesterase is the enzyme that breaks down ACh. Anticholinesterases are the drugs that inhibit cholinesterase, resulting in increased levels of ACh everywhere in the body.
What is the role of acetylcholinesterase?
Acetylcholinesterase (HGNC symbol ACHE; EC 3.1. 1.7), also known as AChE or acetylhydrolase, is the primary cholinesterase in the body. It is an enzyme that catalyzes the breakdown of acetylcholine and of some other choline esters that function as neurotransmitters.
How does acetylcholinesterase break down acetylcholine?
Acetylcholinesterase in Action Acetylcholinesterase is found in the synapse between nerve cells and muscle cells. It waits patiently and springs into action soon after a signal is passed, breaking down the acetylcholine into its two component parts, acetic acid and choline.
What is the function of acetylcholinesterase quizlet?
What is the function of acetylcholinesterase? This enzyme breaks down acetylcholine and prevents the generation of multiple action potentials from a single nerve impulse.
What organisms have acetylcholinesterase?
Acetylcholinesterase (AChE, EC 3.1. 1.7) is one of the most important enzymes in many living organisms, including humans and vertebrates, and is located in the nervous system and in muscles [1].
Where is acetylcholinesterase expressed?
This very large protein consists of three catalytic tetramers covalently linked to the three-stranded collagen-like tail (ColQ). The transcripts encoding AChE in muscle are preferentially expressed at sites of nerve-muscle contact and the AChE locally synthesized and assembled.
What binds covalently to acetylcholinesterase?
Organophosphate (OP) and carbamate esters can inhibit acetylcholinesterase (AChE) by binding covalently to a serine residue in the enzyme active site, and their inhibitory potency depends largely on affinity for the enzyme and the reactivity of the ester.
What is the function of the enzyme acetylcholinesterase quizlet?
Which bond is hydrolyzed by acetylcholinesterase?
ester bond
Figure 8 Hydrolysis of acetylcholine catalyzed by acetylcholinesterase generates choline and acetic acid. As acetylcholine approaches the enzyme, electrostatic forces pull them together to bind and in the presence of water the ester bond (in green) is broken and they separate from the enzyme (lower section).
What is the role of acetylcholinesterase at a synapse quizlet?