KEGG   ENZYME: 3.1.1.7Help
Entry
EC 3.1.1.7                  Enzyme                                 

Name acetylcholinesterase;
true cholinesterase;
choline esterase I;
cholinesterase;
acetylthiocholinesterase;
acetylcholine hydrolase;
acetyl.beta-methylcholinesterase;
AcCholE
Class Hydrolases;
Acting on ester bonds;
Carboxylic-ester hydrolases
BRITE hierarchy
Sysname acetylcholine acetylhydrolase
Reaction(IUBMB) acetylcholine + H2O = choline + acetate [RN:R01026]
Reaction(KEGG) R01026
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Substrate acetylcholine [CPD:C01996];
H2O [CPD:C00001]
Product choline [CPD:C00114];
acetate [CPD:C00033]
Inhibitor Tacrine [CPD:C01453]
Comment Acts on a variety of acetic esters; also catalyses
transacetylations.
Pathway PATH: ec00564  Glycerophospholipid metabolism
Orthology KO: K01049  acetylcholinesterase
Genes HSA: 43(ACHE)
MCC: 713370(ACHE)
MMU: 11423(Ache)
RNO: 83817(Ache)
CFA: 489828(ACHE)
BTA: 540446(ACHE)
ECB: 100069149
MDO: 100017989
GGA: 396388(ACHE)
DRE: 114549(ache)
CIN: 100169895(ache)
SPU: 576746
DME: Dmel_CG17907(Ace)
DPO: Dpse_GA14718
AGA: AgaP_AGAP000466
AAG: AaeL_AAEL012141
AME: 406104(Ache)
TCA: 659368
CEL: W09B12.1(ace-1) Y44E3A.2(ace-2) Y48B6A.7(ace-4)
NVE: NEMVE_v1g171912
AFM: AFUA_7G01710
MSM: MSMEG_1432
Taxonomy
Structures PDB: 1ACJ  1ACL  1AMN  1AX9  1B41  1C2B  1C2O  1CFJ  1DX4  1DX6  
     1E3Q  1E66  1EA5  1EEA  1EVE  1F8U  1FSS  1GPK  1GPN  1GQR  
     1GQS  1H22  1H23  1HBJ  1J06  1J07  1JJB  1MAA  1MAH  1N5M  
     1N5R  1OCE  1ODC  1Q83  1Q84  1QID  1QIE  1QIF  1QIG  1QIH  
     1QII  1QIJ  1QIK  1QIM  1QO9  1QON  1QTI  1SOM  1U65  1UT6  
     1VOT  1VXO  1VXR  1VZJ  1W4L  1W6R  1W75  1W76  1ZGB  1ZGC  
     2ACE  2ACK  2BAG  2C0P  2C0Q  2C4H  2C58  2C5F  2C5G  2CEK  
     2CKM  2CMF  2DFP  2GYU  2GYV  2GYW  2H9Y  2HA0  2HA2  2HA3  
     2HA4  2HA5  2HA6  2HA7  2J3D  2J3Q  2J4F  2JEY  2JEZ  2JF0  
     2JGE  2JGF  2JGG  2JGH  2JGI  2JGJ  2JGK  2JGL  2JGM  2V96  
     2V97  2V98  2VA9  2VJA  2VJB  2VJC  2VJD  2VQ6  2VT6  2VT7  
     2W6C  2WFZ  2WG0  2WG1  2WHP  2WHQ  2WHR  2WLS  2WU3  2WU4  
     3DL4  3DL7  3I6M  3I6Z  
Reference
  Authors
  Title
  Journal
1
Augustinsson, K.-B.
Cholinesterases. A study in comparative enzymology.
Acta Physiol. Scand. 15, Suppl. 2 (1948)
Reference
  Authors
  Title

  Journal
  Organism
2  [PMID:13522650]
BERGMANN F, RIMON S, SEGAL R.
Effect of pH on the activity of eel esterase towards different
substrates.
Biochem. J. 68 (1958) 493-9.
Rattus norvegicus [GN:rno], Bos taurus [GN:bta]
Reference
  Authors
  Title

  Journal
  Organism
3  [PMID:5073758]
Ciliv G, Ozand PT.
Human erythrocyte acetylcholinesterase purification, properties and
kinetic behavior.
Biochim. Biophys. Acta. 284 (1972) 136-56.
Homo sapiens [GN:hsa]
Reference
  Authors
  Title

  Journal
  Organism
4  [PMID:5238989]
Leuzinger W, Baker AL, Cauvin E.
Acetylcholinesterase. II. Crystallization, absorption spectra,
isoionic point.
Proc. Natl. Acad. Sci. U. S. A. 59 (1968) 620-3.
Electrophorus electricus
Reference
  Authors
  Title
  Journal
5  [PMID:14885021]
NACHMANSOHN D, WILSON IB.
The enzymic hydrolysis and synthesis of acetylcholine.
Adv. Enzymol. Relat. Subj. Biochem. 12 (1951) 259-339.
Reference
  Authors
  Title

  Journal
  Organism
6  [PMID:14377597]
ZITTLE CA, DELLAMONICA ES, CUSTER JH, KRIKORIAN R.
Purification of human red cell acetylcholinesterase by
electrophoresis, ultracentrifugation and gradient extraction.
Arch. Biochem. 56 (1955) 469-75.
Homo sapiens [GN:hsa]
Other DBs ExplorEnz - The Enzyme Database: 3.1.1.7
IUBMB Enzyme Nomenclature: 3.1.1.7
ExPASy - ENZYME nomenclature database: 3.1.1.7
BRENDA, the Enzyme Database: 3.1.1.7
CAS: 9000-81-1

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