Butyrylcholinesterase: Difference between revisions

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<StructureSection load='2pm8' size='350' side='right' caption='Human butyrylcholinesterase (PDB code [[2pm8]])' scene='Butyrylcholinesterase/Cv/1'>
<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]])'>
<StructureSection load='1p0m' size='450' side='right' scene= caption='Lymnaea acetylcholine-binding protein pentamer complex with acetylcholine (PDB code 3wip)'>
[[Image:HuBChE.png|left|300px]]
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 


__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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BChE 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 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.
</StructureSection>


==3D structures of BChE==
== Structural highlights ==


Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
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.
{{#tree:id=OrganizedByTopic|openlevels=0|


* hBChE - Apo human
==3D structures of BChE==
[[Butyrylcholinesterase 3D structures]]


**[[2pm8]], [[1p0i]] - hBChE - human  <br />
</StructureSection>
**[[2xmb]] – hBChE (mutant)+SO4<br />
**[[2xmc]] - hBChE (mutant)+F <br />
**[[4aqd]] - hBChE (fully glycosylated)


* BChE+OP irreversible inhibitors, including nerve agents and insecticides
**[[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
* BChE+inhibitor binding at surface of the protein (far from the active site)
**[[2j4c]] – hBChE+ HgCl2 <br />
* BChE + substrate analogues mimicking the binding of the substrate butyrylcholine
**[[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]]
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== References ==
<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

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