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Literature summary for 3.1.1.2 extracted from

  • Bavec, A.; Knez, D.; Makovec, T.; Stojan, J.; Gobec, S.; Golicnik, M.
    Exploring the aryl esterase catalysis of paraoxonase-1 through solvent kinetic isotope effects and phosphonate-based isosteric analogues of the tetrahedral reaction intermediate (2014), Biochimie, 106, 184-186.
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Homo sapiens P27169
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the phenyl acetate esterase activity of paraoxonase-1 shows normal solvent kinetic isotope effects, while proton inventory analysis indicates that two protons contribute to the kinetic isotope effect. Moderate competitive inhibition with the phenyl methylphosphonate anion reveals that the rate-limiting transition state suboptimally resembles the tetrahedral intermediate. Despite the presence of the Ca2+-promoted oxyanion hole, the catalytic power can be mostly rationalized by concerted two-proton exchange reorganisation at the active site Homo sapiens ?
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Synonyms

Synonyms Comment Organism
PON1
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Homo sapiens
serum paraoxonase/arylesterase 1
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Homo sapiens