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discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
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MetaCyc Enzyme: acetylcholinesterase

Gene: ache Accession Number: G-14654 (MetaCyc)

Synonyms: globular

Species: Torpedo californica

Subunit composition of acetylcholinesterase = [Ache]
         isoform H = Ache

Summary:
An essential enzyme of nervous system which rapidly stops the action of acetylcholine that is released into the synapse is acetylcholinesterase. An acetylcholine esterase has been characterized from the pacific ray (Torpedo californica). Two classes have been identified from multipe enxyme forms. Their catalytic action is similar differences lie in amino acid composition, pepride composition and in antibody assays [Schumacher].

Isoform H is a homodimer; has a disulfide-bonded oligomer composed of a collagenic subunit and a variable number of T catalytic subunits. The sequence of this subunit is chosen to be the canonical sequnce

Molecular Weight of Polypeptide: 65.9 kD (from nucleotide sequence), 65.9 kD (experimental)

Unification Links: Entrez-Nucleotide:X03439 , Mint:MINT-1518870 , NCBI Entrez Protein (GI):CAA27169 , Protein Model Portal:P04058 , SMR:P04058 , UniProt:P04058

Relationship Links: InterPro:IN-FAMILY:IPR000908 , InterPro:IN-FAMILY:IPR000997 , InterPro:IN-FAMILY:IPR002018 , InterPro:IN-FAMILY:IPR019819 , InterPro:IN-FAMILY:IPR019826 , PDB:Structure:1ACJ , PDB:Structure:1ACL , PDB:Structure:1AMN , PDB:Structure:1AX9 , PDB:Structure:1CFJ , PDB:Structure:1DX6 , PDB:Structure:1E3Q , PDB:Structure:1E66 , PDB:Structure:1EA5 , PDB:Structure:1EEA , PDB:Structure:1EVE , PDB:Structure:1FSS , PDB:Structure:1GPK , PDB:Structure:1GPN , PDB:Structure:1GQR , PDB:Structure:1GQS , PDB:Structure:1H22 , PDB:Structure:1H23 , PDB:Structure:1HBJ , PDB:Structure:1JGA , PDB:Structure:1JGB , PDB:Structure:1JJB , PDB:Structure:1OCE , PDB:Structure:1ODC , PDB:Structure:1QID , PDB:Structure:1QIE , PDB:Structure:1QIF , PDB:Structure:1QIG , PDB:Structure:1QIH , PDB:Structure:1QII , PDB:Structure:1QIJ , PDB:Structure:1QIK , PDB:Structure:1QIM , PDB:Structure:1QTI , PDB:Structure:1SOM , PDB:Structure:1U65 , PDB:Structure:1UT6 , PDB:Structure:1VOT , PDB:Structure:1VXO , PDB:Structure:1VXR , PDB:Structure:1W4L , PDB:Structure:1W6R , PDB:Structure:1W75 , PDB:Structure:1W76 , PDB:Structure:1ZGB , PDB:Structure:1ZGC , PDB:Structure:2ACE , PDB:Structure:2ACK , PDB:Structure:2BAG , PDB:Structure:2C4H , PDB:Structure:2C58 , PDB:Structure:2C5F , PDB:Structure:2C5G , PDB:Structure:2CEK , PDB:Structure:2CKM , PDB:Structure:2CMF , PDB:Structure:2DFP , PDB:Structure:2J3D , PDB:Structure:2J3Q , PDB:Structure:2J4F , PDB:Structure:2V96 , PDB:Structure:2V97 , PDB:Structure:2V98 , PDB:Structure:2VA9 , PDB:Structure:2VJA , PDB:Structure:2VJB , PDB:Structure:2VJC , PDB:Structure:2VJD , PDB:Structure:2VQ6 , PDB:Structure:2VT6 , PDB:Structure:2VT7 , PDB:Structure:2W6C , PDB:Structure:2W9I , PDB:Structure:2WFZ , PDB:Structure:2WG0 , PDB:Structure:2WG1 , PDB:Structure:2WG2 , PDB:Structure:2XI4 , PDB:Structure:3ACE , PDB:Structure:3GEL , PDB:Structure:3I6M , PDB:Structure:3I6Z , PDB:Structure:3M3D , PDB:Structure:3ZV7 , PDB:Structure:4ACE , Pfam:IN-FAMILY:PF00135 , Prints:IN-FAMILY:PR00878 , Prints:IN-FAMILY:PR00879 , Prosite:IN-FAMILY:PS00122 , Prosite:IN-FAMILY:PS00941

Gene-Reaction Schematic: ?

Credits:
Created 25-Sep-2011 by Pujar A , Boyce Thompson Institute


Enzymatic reaction of: acetylcholinesterase

EC Number: 3.1.1.7

acetylcholine + H2O <=> acetate + choline + H+

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is physiologically favored in the direction shown.


References

Schumacher: Schumacher M, Camp S, Maulet Y, Newton M, MacPhee-Quigley K, Taylor SS, Friedmann T, Taylor P "Primary structure of Torpedo californica acetylcholinesterase deduced from its cDNA sequence." Nature 319(6052);407-9. PMID: 3753747


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 18.5 on Sat Dec 20, 2014, biocyc12.