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Butyrylcholinesterase

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Glycosylated human butyrylcholinesterase complex with sulfate, glycerol, Cl- (green) and Na+ (purple) ions 2xmb
Ligands: , , , , , ,
Activity: Cholinesterase, with EC number 3.1.1.8
Related: 2wsl, 2j4c, 2wik, 1kcj, 1xlu, 1p0p, 2wij, 1xlv, 1eho, 1p0m, 1xlw, 1ehq, 1p0q, 2wid, 2wil, 2wif, 1p0i, 2wig, 2xmd, 2xmg, 2xmc


Resources: FirstGlance, OCA, RCSB, PDBsum
Coordinates: save as pdb, mmCIF, xml



Recombinant full length human butyrylcholinesterase 2pm8
Ligands: , , ,
Gene: BCHE, CHE1 (Homo sapiens)
Activity: Cholinesterase, with EC number 3.1.1.8
Related: 1xlw, 1vzj, 1xlu, 1p01, 1xlv, 2cek
Resources: FirstGlance, OCA, RCSB, PDBsum
Coordinates: save as pdb, mmCIF, xml



Butyrylcholinesterase (BChE) is an enzyme widely distributed throughout the body in humans, but particularly prevalent in serum, where it occurs as a tetramer of catalytic subunits. It is distinguished from the homologous enzyme, acetylcholinesterase, by its ability to hydrolyze the non-natural substrate butyrylcholine as well as the neurotransmitter, acetylcholine. Its biological role remains obscure, but mutations in the human BCHE gene result in prolonged post-surgical apnea due to the inability of the mutant BChEs to hydrolyse the local anaesthetic, succinylcholine. BChE finds medical use as a bioscavenger for overcoming organophosphate (OP) nerve agent and insecticide intoxication by interacting rapidly with the toxic agents. Crystal structures of both the native enzyme and of its conjugates with nerve agents are available. The image at the right correspond to one representative BChE, i.e. the crystal structure of recombinant full length human butyrylcholinesterase (2pm8).

Contents

3D structures of BChE

Updated on 07-March-2013

hBChE - Apo human

2pm8, 1p0i - hBChE - human
2xmb – hBChE (mutant)+SO4
2xmc - hBChE (mutant)+F
4aqd - hBChE (fully glycosylated)

BChE+OP irreversible inhibitors, including nerve agents and insecticides

3djy, 3dkk - hBChE+tabun
2wid, 2wif - hBChE+Tabun analogue TA1
2wsl, 2wig – hBChE+Tabun analogue TA4
2wil, 2wij - hBChE+Tabun analogue TA5
2wik - hBChE+Tabun analogue TA6
1xlw - hBChE+echothiophate
1xmd, 2xmd – hBChE (mutant)+echothiophate
1p0q - hBChE+soman
1xlu - hBChE+Di-Isopropyl-Phosphoro-Fluoridate (DFP)
2xmg - hBChE (mutant)+VX
1xlv – hBChE+ethyl dihydrogen phosphate
2y1k - hBChE (mutant) + CBDP
4b0p, 4b0o - hBChE (Aged) + pyridinium derivative
4axb – hBChE (aged) + 2-PAM

BChE+inhibitor binding at surface of the protein (far from the active site)

2j4c – hBChE+ HgCl2

BChE + substrate analogues mimicking the binding of the substrate butyrylcholine

1p0m - hBChE+choline
1p0p - hBChE+butyrylthiocholine
3o9m - hBChE + benzoic acid
1eho, 1ehq, 1kcj – hBChE + cocaine - model

Additional Resources

For additional information, see: Alzheimer's Disease

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Michal Harel, Lakshmi Venkatachalam, Joel L. Sussman, Alexander Berchansky, Jaime Prilusky, David Canner

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