Metabolic Modeling Tutorial
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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
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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 Thu Nov 27, 2014, biocyc11.