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: 3.1.1.2

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

EC Number: 3.1.1.2

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: arylesterase

Enzyme Commission Synonyms: A-esterase, paraoxonase, aromatic esterase

Standard Gibbs Free Energy (ΔrG in kcal/mol): 16.255127 Inferred by computational analysis [Latendresse13]

Enzyme Commission Summary:
Acts on many phenolic esters. The reactions of EC 3.1.8.1 aryldialkylphosphatase, were previously attributed to this enzyme. It is likely that the three forms of human paraoxonase are lactonases rather than aromatic esterases [Khersonsky05, Draganov05]. The natural substrates of the paraoxonases are lactones [Khersonsky05, Draganov05], with (±)-5-hydroxy-6E,8Z,11Z,4Z-eicostetraenoic-acid 1,5-lactone being the best substrate [Draganov05].

Citations: [Kim90, Mackness87, Bosmann72, AUGUSTINSSON59, ALDRIDGE53]

Unification Links: KEGG:R07342

Relationship Links: BRENDA:EC:3.1.1.2 , ENZYME:EC:3.1.1.2 , IUBMB-ExplorEnz:EC:3.1.1.2 , UniProt:RELATED-TO:P22862 , UniProt:RELATED-TO:Q07792


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

AUGUSTINSSON59: AUGUSTINSSON KB, OLSSON B (1959). "Esterases in the milk and blood plasma of swine. I. Substrate specificity and electrophoresis studies." Biochem J 71(3);477-84. PMID: 13638253

Bosmann72: Bosmann HB (1972). "Membrane marker enzymes. Characterization of an arylesterase of guinea pig cerebral cortex utilizing p-nitrophenyl acetate as substrate." Biochim Biophys Acta 276(1);180-91. PMID: 5047702

Draganov05: Draganov DI, Teiber JF, Speelman A, Osawa Y, Sunahara R, La Du BN (2005). "Human paraoxonases (PON1, PON2, and PON3) are lactonases with overlapping and distinct substrate specificities." J Lipid Res 46(6);1239-47. PMID: 15772423

Khersonsky05: Khersonsky O, Tawfik DS (2005). "Structure-reactivity studies of serum paraoxonase PON1 suggest that its native activity is lactonase." Biochemistry 44(16);6371-82. PMID: 15835926

Kim90: Kim DH, Yang YS, Jakoby WB (1990). "Nonserine esterases from rat liver cytosol." Protein Expr Purif 1(1);19-27. PMID: 2152179

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

Mackness87: Mackness MI, Thompson HM, Hardy AR, Walker CH (1987). "Distinction between 'A'-esterases and arylesterases. Implications for esterase classification." Biochem J 245(1);293-6. PMID: 2822017


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 Dec 18, 2014, BIOCYC14B.