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: 3.1.8.1

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

EC Number: 3.1.8.1

Enzymes and Genes:
organophosphate acid anhydrase Inferred from experiment : opd ( Sphingobium fuliginis )

In Pathway: paraoxon degradation

Note that this reaction equation differs from the official Enzyme Commission reaction equation for this EC number, which can be found here .

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: aryldialkylphosphatase

Enzyme Commission Synonyms: organophosphate hydrolase, paraoxonase, A-esterase, aryltriphosphatase, organophosphate esterase, esterase B1, esterase E4, paraoxon esterase, pirimiphos-methyloxon esterase, OPA anhydrase, organophosphorus hydrolase, phosphotriesterase, paraoxon hydrolase, OPH, organophosphorus acid anhydrase

Standard Gibbs Free Energy (ΔrG in kcal/mol): 3.5787811 Inferred by computational analysis [Latendresse13]

Enzyme Commission Summary:
Acts on organophosphorus compounds (such as paraoxon) including esters of phosphonic and phosphinic acids. Inhibited by chelating agents; requires divalent cations for activity. Previously regarded as identical with EC 3.1.1.2 arylesterase.

Citations: [Mackness87, ALDRIDGE53, Bosmann72, MAIN60, Reiner89]

Gene-Reaction Schematic: ?

Unification Links: KEGG:R05548

Relationship Links: BRENDA:EC:3.1.8.1 , ENZYME:EC:3.1.8.1 , IUBMB-ExplorEnz:EC:3.1.8.1


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

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

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

MAIN60: MAIN AR (1960). "The differentiation of the A-type esterases in sheep serum." Biochem J 75;188-95. PMID: 14420012

Reiner89: Reiner, E., Aldridge, W.N, Hoskin, C.G (1989). "Enzymes Hydrolysing Organophosphorus Compounds, Ellis Horwood, Chichester, UK,."


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 Nov 22, 2014, BIOCYC14A.