what is the role of acetylcholinesterase in the neuromuscular junction
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. AChE is found at mainly neuromuscular junctions and in chemical synapses of the cholinergic type, where its activity serves to terminate synaptic transmission. It belongs to carboxylesterase family of enzymes. It is the primary target of inhibition by organophosphorus compounds such as nerve agents and pesticides.
Neuromuscular junction The neuromuscular junction differs from chemical synapses between neurons. Presynaptic motor axons stop 30 nanometers from the sarcolemma, the cell membrane of a muscle cell. This 30-nanometer space forms the synaptic cleft through which signalling molecules are released. The sarcolemma has invaginations called postjunctional folds, which increase the surface area of the membrane exposed to the synaptic cleft.[2] These postjunctional folds form what is referred to as the motor endplate, which possess nicotinic acetylcholine receptors (nAChRs) at a density of 10,000 receptors/micrometer2 in skeletal muscle.[3] The presynaptic axons form bulges called terminal boutons (or presynaptic terminals) that project into the postjunctional folds of the sarcolemma. The presynaptic terminals have active zones that contain vesicles, also called quanta, full of acetylcholine molecules. These vesicles can fuse with the presynaptic membrane and release ACh molecules into the synaptic cleft via exocytosis after depolarization.[2] AChRs are localized opposite the presynaptic terminals by protein scaffolds at the postjunctional folds of the sarcolemma. Dystrophin, a structural protein, connects the sarcomere, sarcolemma, and extracellular matrix components. Rapsyn is another protein that docks AChRs and structural proteins to the cytoskeleton. Also present is the receptor tyrosine kinase protein MuSK, a signaling protein involved in the development of the neuromuscular junction, which is also held in place by rapsyn.[2]
Small intestine Food from the stomach is allowed into the duodenum through the pylorus by a muscle called the pyloric sphincter.
Acetylcholinesterase AChE is a hydrolase that hydrolyzes choline esters. It has a very high catalytic activity - each molecule of AChE degrades about 25000 molecules of acetylcholine (ACh) per second, approaching the limit allowed by diffusion of the substrate.[6][7] The active site of AChE comprises 2 subsites - the anionic site and the esteratic subsite. The structure and mechanism of action of AChE have been elucidated from the crystal structure of the enzyme.[8][9]