Metabolic Modeling Tutorial
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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
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
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MetaCyc Reaction: 3.1.1.7

Superclasses: Reactions Classified By Conversion Type Simple Reactions Chemical Reactions
Reactions Classified By Substrate Small-Molecule Reactions

EC Number: 3.1.1.7

Enzymes and Genes:
acetylcholinesterase Inferred from experiment : ache ( Torpedo californica )

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

Most BioCyc compounds have been protonated to a reference pH value of 7.3, and some reactions have been computationally balanced for hydrogen by adding free protons. Please see the PGDB Concepts Guide for more information.

Mass balance status: Balanced.

Enzyme Commission Primary Name: acetylcholinesterase

Enzyme Commission Synonyms: true cholinesterase, choline esterase I, cholinesterase, acetylthiocholinesterase, acetylcholine hydrolase, acetyl.β-methylcholinesterase, AcCholE

Standard Gibbs Free Energy (ΔrG in kcal/mol): -4.2871246 Inferred by computational analysis [Latendresse13]

Enzyme Commission Summary:
Acts on a variety of acetic esters; also catalyses transacetylations.

Citations: [NACHMANSOHN51, Leuzinger68, Ciliv72, BERGMANN58, ZITTLE55]

Gene-Reaction Schematic: ?

Unification Links: KEGG:R01026 , Rhea:17561

Relationship Links: BRENDA:EC:3.1.1.7 , ENZYME:EC:3.1.1.7 , IUBMB-ExplorEnz:EC:3.1.1.7 , UniProt:RELATED-TO:O61371 , UniProt:RELATED-TO:O61372 , UniProt:RELATED-TO:O61459 , UniProt:RELATED-TO:P04058 , UniProt:RELATED-TO:P07140 , UniProt:RELATED-TO:P07692 , UniProt:RELATED-TO:P21836 , UniProt:RELATED-TO:P22303 , UniProt:RELATED-TO:P36196 , UniProt:RELATED-TO:P37136 , UniProt:RELATED-TO:P38433 , UniProt:RELATED-TO:Q7LZ27 , UniProt:RELATED-TO:Q7LZG1 , UniProt:RELATED-TO:Q7LZJ6 , UniProt:RELATED-TO:Q7M2N6 , UniProt:RELATED-TO:Q7M382 , UniProt:RELATED-TO:Q8MXC4 , UniProt:RELATED-TO:Q8MXC5 , UniProt:RELATED-TO:Q8MXC6 , UniProt:RELATED-TO:Q8MXC7 , UniProt:RELATED-TO:Q8MXC8 , UniProt:RELATED-TO:Q8MXC9 , UniProt:RELATED-TO:Q95P20 , UniProt:RELATED-TO:Q95WV7 , UniProt:RELATED-TO:Q9PWR0 , UniProt:RELATED-TO:Q9TR27 , UniProt:RELATED-TO:Q9TX11 , UniProt:RELATED-TO:Q03637


References

BERGMANN58: BERGMANN F, RIMON S, SEGAL R (1958). "Effect of pH on the activity of eel esterase towards different substrates." Biochem J 68(3);493-9. PMID: 13522650

Ciliv72: Ciliv G, Ozand PT (1972). "Human erythrocyte acetylcholinesterase purification, properties and kinetic behavior." Biochim Biophys Acta 284(1);136-56. PMID: 5073758

Latendresse13: Latendresse M. (2013). "Computing Gibbs Free Energy of Compounds and Reactions in MetaCyc."

Leuzinger68: Leuzinger W, Baker AL, Cauvin E (1968). "Acetylcholinesterase. II. Crystallization, absorption spectra, isoionic point." Proc Natl Acad Sci U S A 59(2);620-3. PMID: 5238989

NACHMANSOHN51: NACHMANSOHN D, WILSON IB (1951). "The enzymic hydrolysis and synthesis of acetylcholine." Adv Enzymol Relat Subj Biochem 12;259-339. PMID: 14885021

ZITTLE55: ZITTLE CA, DELLAMONICA ES, CUSTER JH, KRIKORIAN R (1955). "Purification of human red cell acetylcholinesterase by electrophoresis, ultracentrifugation and gradient extraction." Arch Biochem Biophys 56(2);469-75. PMID: 14377597


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, biocyc11.