Butyrylcholinesterase
From Proteopedia
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| - | <StructureSection load='1p0m' size=' | + | <StructureSection load='1p0m' size='350' side='right' scene='39/399020/Cv/3' caption='Glycosylated human butyrylcholinesterase complex with choline, glycerol, sulfate and Cl- ions (PDB code [[1p0m]])'> |
__TOC__ | __TOC__ | ||
== Function == | == Function == | ||
| - | [[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. | + | [[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. <ref>PMID:12563284</ref> |
== Relevance == | == Relevance == | ||
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== Structural highlights == | == Structural highlights == | ||
| - | Like in the AChE structure, BChE active site is located at the bottom of a ca. 20A deep gorge. The active site of BChE is similar to that of AChE. | + | Like in the AChE structure, BChE active site is located at the bottom of a ca. 20A deep gorge. The <scene name='39/399020/Cv/6'>active site of BChE</scene> is similar to that of AChE. <ref>PMID:12869558</ref> Water molecule is shown as red sphere. The differences are noticed in the lining of the gorge were some of the aromatic residues in AChE are substituted by hydrophobic ones and in the active site acyl-binding pocket where 2 Phe residues are replaced by Leu and Val in BChE. |
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==3D structures of BChE== | ==3D structures of BChE== | ||
| + | [[Butyrylcholinesterase 3D structures]] | ||
| - | + | </StructureSection> | |
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| - | * hBChE - Apo human | ||
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| - | **[[2pm8]], [[1p0i]] - hBChE - human <br /> | ||
| - | **[[2xmb]] – hBChE (mutant)+SO4<br /> | ||
| - | **[[2xmc]] - hBChE (mutant)+F <br /> | ||
| - | **[[4aqd]] - hBChE (fully glycosylated) | ||
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| - | * BChE+OP irreversible inhibitors, including nerve agents and insecticides | ||
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| - | **[[3djy]], [[3dkk]] - hBChE+tabun <br /> | ||
| - | **[[2wid]], [[2wif]] - hBChE+Tabun analogue TA1 <br /> | ||
| - | **[[2wsl]], [[2wig]] – hBChE+Tabun analogue TA4 <br /> | ||
| - | **[[2wil]], [[2wij]] - hBChE+Tabun analogue TA5 <br /> | ||
| - | **[[2wik]] - hBChE+Tabun analogue TA6 <br /> | ||
| - | **[[1xlw]] - hBChE+echothiophate <br /> | ||
| - | **[[1xmd]], [[2xmd]] – hBChE (mutant)+echothiophate<br /> | ||
| - | **[[1p0q]] - hBChE+soman <br /> | ||
| - | **[[1xlu]] - hBChE+Di-Isopropyl-Phosphoro-Fluoridate (DFP)<br /> | ||
| - | **[[2xmg]] - hBChE (mutant)+VX<br /> | ||
| - | **[[1xlv]] – hBChE+ethyl dihydrogen phosphate<br /> | ||
| - | **[[2y1k]], [[4bbz]] - hBChE (mutant) + CBDP <br /> | ||
| - | **[[4b0p]], [[4b0o]] - hBChE (Aged) + pyridinium derivative<br /> | ||
| - | **[[4axb]] – hBChE (aged) + 2-PAM | ||
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| - | * BChE+inhibitor binding at surface of the protein (far from the active site) | ||
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| - | **[[2j4c]] – hBChE+ HgCl2 <br /> | ||
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| - | * BChE + substrate analogues mimicking the binding of the substrate butyrylcholine | ||
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| - | **[[1p0m]] - hBChE+choline <br /> | ||
| - | **[[1p0p]] - hBChE+butyrylthiocholine<br /> | ||
| - | **[[3o9m]] - hBChE + benzoic acid<br /> | ||
| - | **[[1eho]], [[1ehq]], [[1kcj]] – hBChE + cocaine - model<br /> | ||
| - | **[[4bds]] – hBChE + tacrine<br /> | ||
| - | }} | ||
==Additional Resources== | ==Additional Resources== | ||
For additional information, see: [[Alzheimer's Disease]] | For additional information, see: [[Alzheimer's Disease]] | ||
<br /> | <br /> | ||
| - | + | == References == | |
| + | <references/> | ||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Current revision
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Additional Resources
For additional information, see: Alzheimer's Disease
References
- ↑ Darvesh S, Hopkins DA, Geula C. Neurobiology of butyrylcholinesterase. Nat Rev Neurosci. 2003 Feb;4(2):131-8. PMID:12563284 doi:http://dx.doi.org/10.1038/nrn1035
- ↑ Nicolet Y, Lockridge O, Masson P, Fontecilla-Camps JC, Nachon F. Crystal structure of human butyrylcholinesterase and of its complexes with substrate and products. J Biol Chem. 2003 Oct 17;278(42):41141-7. Epub 2003 Jul 17. PMID:12869558 doi:http://dx.doi.org/10.1074/jbc.M210241200
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