butyrylcholinesterase

Target id: 2471

Nomenclature: butyrylcholinesterase

Abbreviated Name: BChE

Family: Hydrolases, Acetylcholine turnover

Annotation status:  image of an orange circle Annotated and awaiting review. Please contact us if you can help with reviewing.  » Email us

   GtoImmuPdb view: OFF :     Currently no data for butyrylcholinesterase in GtoImmuPdb

Gene and Protein Information
Species TM AA Chromosomal Location Gene Symbol Gene Name Reference
Human - 602 3q26.1-q26.2 BCHE butyrylcholinesterase
Mouse - 603 3 E3 Bche butyrylcholinesterase
Rat - - 2q32 Bche butyrylcholinesterase
Previous and Unofficial Names
Acylcholine acylhydrolase | Butyrylcholine esterase | CHE1 | Choline esterase II | cholinesterase
Database Links
BRENDA
CATH/Gene3D
ChEMBL Target
DrugBank Target
Ensembl Gene
Entrez Gene
GenitoUrinary Development Molecular Anatomy Project
Human Protein Atlas
KEGG Enzyme
KEGG Gene
OMIM
Orphanet
RefSeq Nucleotide
RefSeq Protein
SynPHARM
UniProtKB
Wikipedia
Selected 3D Structures
Image of receptor 3D structure from RCSB PDB
Description:  Crystal structure of human butyryl cholinesterase
PDB Id:  1P0I
Resolution:  2.0Å
Species:  Human
References:  4
Enzyme Reaction
EC Number: 3.1.1.7 Acetylcholine + H2O = acetic acid + choline + H+

Download all structure-activity data for this target as a CSV file

Inhibitors
Key to terms and symbols View all chemical structures Click column headers to sort
Ligand Sp. Action Affinity Units Reference
tacrine Hs Inhibition 7.2 pKi 1
pKi 7.2 (Ki 7x10-8 M) [1]
bambuterol Hs Inhibition 8.5 pIC50 2
pIC50 8.5 [2]
physostigmine Hs Inhibition 7.6 – 7.8 pIC50 3
pIC50 7.6 – 7.8 [3]
rivastigmine Hs Inhibition 7.4 pIC50 3
pIC50 7.4 (IC50 3.7x10-8 M) [3]
pyridostigmine Hs Inhibition 6.1 pIC50 5
pIC50 6.1 (IC50 9x10-7 M) [5]
Description: Inhibition of human plasma BCHE activity by a modified Ellman assay.
Clinically-Relevant Mutations and Pathophysiology
Disease:  Butyrylcholinesterase deficiency
Orphanet: ORPHA132

References

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1. Butini S, Campiani G, Borriello M, Gemma S, Panico A, Persico M, Catalanotti B, Ros S, Brindisi M, Agnusdei M et al.. (2008) Exploiting protein fluctuations at the active-site gorge of human cholinesterases: further optimization of the design strategy to develop extremely potent inhibitors. J. Med. Chem.51 (11): 3154-70. [PMID:18479118]

2. Giacobini E. (2003) Cholinesterases: new roles in brain function and in Alzheimer's disease. Neurochem. Res.28 (3-4): 515-22. [PMID:12675140]

3. Luo W, Yu QS, Kulkarni SS, Parrish DA, Holloway HW, Tweedie D, Shafferman A, Lahiri DK, Brossi A, Greig NH. (2006) Inhibition of human acetyl- and butyrylcholinesterase by novel carbamates of (-)- and (+)-tetrahydrofurobenzofuran and methanobenzodioxepine. J. Med. Chem.49 (7): 2174-85. [PMID:16570913]

4. Nicolet Y, Lockridge O, Masson P, Fontecilla-Camps JC, Nachon F. (2003) Crystal structure of human butyrylcholinesterase and of its complexes with substrate and products. J. Biol. Chem.278 (42): 41141-7. [PMID:12869558]

5. Yu QS, Holloway HW, Luo W, Lahiri DK, Brossi A, Greig NH. (2010) Long-acting anticholinesterases for myasthenia gravis: synthesis and activities of quaternary phenylcarbamates of neostigmine, pyridostigmine and physostigmine. Bioorg. Med. Chem.18 (13): 4687-93. [PMID:20627738]

How to cite this page

Acetylcholine turnover: butyrylcholinesterase. Last modified on 25/01/2016. Accessed on 19/10/2017. IUPHAR/BPS Guide to PHARMACOLOGY, http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=2471.