|Ref Sequence ID||NP_001070374.1|
|Protein Existence Status||Reviewed: Experimental evidence at transcript level|
|Presence in other biological fluids/tissue/cells||expressed in cholinergic neurons|
|Protein Function||termination of impulse transmission at cholinergic synapses by rapid hydrolysis of the neurotransmitter, acetylcholine; serine hydrolases; key role in ending cholinergic neurotransmission|
|Biochemical Properties||possesses a high specific activity, functioning at a rate approaching that of a diffusion controlled reaction; potent irreversible inhibitors- organophosphorus (OP) poisons; active site of AChE contains two subsites, the ‘esteratic’ and ‘anionic’ subsites; type α/β hydrolase folded with an α helix bound with β sheet that contains a catalytic domain38 with catalytic triad Ser – His – Glu|
|Significance in milk||proinflammatory factors in milk|
|PTMs||three potential N-glycosylation sites Asn-265, Asn-350 and Asn-464|
| Site(s) of PTM(s) |
|Predicted Disorder Regions||NA|
|TM Helix Prediction||2TMHs; (5-23), (44-62)|
|Significance of PTMs||Asn-464 has the most pronounced effect on thermostability|
|Bibliography||1. Dvir, H. et al. (2010) ‘Acetylcholinesterase: From 3D structure to function’, Chemico-Biological Interactions, 187(1–3), pp. 10–22. doi: 10.1016/j.cbi.2010.01.042. |
2. Velan, B. et al. (1993) ‘N-glycosylation of human acetylcholinesterase: effects on activity, stability and biosynthesis’, Biochemical Journal, 296(3), pp. 649–656. doi: 10.1042/bj2960649.
3. Ollis, D. L. et al. (1992) ‘The alpha/beta hydrolase fold.’, Protein engineering, 5(3), pp. 197–211. doi: 10.1093/protein/5.3.197.