Primary Information |
|---|
| BoMiProt ID | Bomi248 |
|---|
| Protein Name | Cholinesterase |
|---|
| Organism | Bos taurus |
|---|
| Uniprot ID | P32749 |
|---|
| Milk Fraction | Whey |
|---|
| Ref Sequence ID | NP_001070374.1 |
|---|
| Aminoacid Length | 602 |
|---|
| Molecular Weight | 68867 |
|---|
| FASTA Sequence |
Download |
|---|
| Gene Name | BCHE |
|---|
| Gene ID | 534616 |
|---|
| Protein Existence Status | Reviewed: Experimental evidence at transcript level |
|---|
Secondary Information |
|---|
| 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)
N-glycosylation,
O-glycosylation,
Phosphorylation
| |
|---|
| Predicted Disorder Regions | NA |
|---|
| DisProt Annotation | |
|---|
| 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. |
|---|
