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Metabolic Modeling Tutorial
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Metabolic Modeling Tutorial
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Escherichia coli K-12 substr. MG1655 Reaction: 3.1.1.6

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

EC Number: 3.1.1.6

Enzymes and Genes:
acetyl esterase Inferred by computational analysis Inferred from experiment : aes

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: acetylesterase

Enzyme Commission Synonyms: C-esterase (in animal tissues), acetic ester hydrolase, chloroesterase, p-nitrophenyl acetate esterase, Citrus acetylesterase

Citations: [ALDRIDGE53, Bergmann60, JANSEN48]

Gene-Reaction Schematic: ?

Relationship Links: BRENDA:EC:3.1.1.6 , ENZYME:EC:3.1.1.6 , IUBMB-ExplorEnz:EC:3.1.1.6


References

ALDRIDGE53: ALDRIDGE WN (1953). "Serum esterases. I. Two types of esterase (A and B) hydrolysing p-nitrophenyl acetate, propionate and butyrate, and a method for their determination." Biochem J 53(1);110-7. PMID: 13032041

Bergmann60: Bergmann F, Rimon S (1960). "Fractionation of C-esterase from the hog's kidney extract." Biochem J 77(2);209-14. PMID: 16748846

JANSEN48: JANSEN EF, NUTTING MD, BALLS AK (1948). "The reversible inhibition of acetylesterase by diisopropyl fluorophosphate and tetraethyl pyrophosphate." J Biol Chem 175(2);975-87. PMID: 18880795


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by SRI International Pathway Tools version 18.5 on Thu Nov 20, 2014, BIOCYC14A.