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ACHE

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. The primary role of AChE is to terminate neuronal transmission and signaling between synapses to prevent ACh dispersal and activation of nearby receptors. Organophosphates inhibit AChE. They are an important component of pesticides and nerve agents.
Protein class

Blood group antigen proteins, Enzymes, FDA approved drug targets, Metabolic proteins

Predicted location

Intracellular, Membrane (different isoforms)

Single cell type specificity

Cell type enhanced (Paneth cells, Distal enterocytes, Horizontal cells, Proximal enterocytes, Exocrine glandular cells, Erythroid cells)

Immune cell specificity

Not detected in immune cells

Cell line specificity

Cell line enhanced (BEWO, CACO-2, K-562, Karpas-707, U-2 OS)

Interaction

Interacts with PRIMA1. The interaction with PRIMA1 is required to anchor it to the basal lamina of cells and organize into tetramers (By similarity). Isoform H generates GPI-anchored dimers; disulfide linked. Isoform T generates multiple structures, ranging from monomers and dimers to collagen-tailed and hydrophobic-tailed forms, in which catalytic tetramers are associated with anchoring proteins that attach them to the basal lamina or to cell membranes. In the collagen-tailed forms, isoform T subunits are associated with a specific collagen, COLQ, which triggers the formation of isoform T tetramers, from monomers and dimers. Isoform R may be monomeric.

Molecular function

Blood group antigen, Hydrolase, Serine esterase

More Types Infomation

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For Research Use Only. Not For Clinical Use.

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