VSE knjižnice (vzajemna bibliografsko-kataložna baza podatkov COBIB.SI)
  • Exploring the aryl esterase catalysis of paraoxonase-1 through solvent kinetic isotope effects and phosphonate-based isosteric analogues of the tetrahedral reaction intermediate
    Bavec, Aljoša ...
    Although a recent study of Debord et al. in Biochimie (2014; 97:72-77) described the thermodynamics of the catalysed hydrolysis of phenyl acetate by human paraoxonase-1, the mechanistic details along ... the reaction route of this enzyme remain unclear. Therefore, we briefly present the solvent kinetic isotope effects on the phenyl acetate esterase activity of paraoxonase-1 and its inhibition with the phenyl methylphosphonate anion, which is a stable isosteric analogue that mimics the high-energy tetrahedral intermediate on the hydroxide-promoted hydrolysis pathway. The data show normal isotope effects, while proton inventory analysis indicates that two protons contribute to the kinetic isotope effect. Coherently, moderate competitive inhibition with the phenyl methylphosphonate anion reveals that the rate-limiting transition state suboptimally resembles the tetrahedral intermediate. The implications of these findings can be attributed to two possible reaction mechanisms that might occur during the paraoxonase-1-catalysed hydrolysis of phenyl acetate.
    Vir: Biochimie. - ISSN 0300-9084 (Vol. 106, 2014, str. 184-186)
    Vrsta gradiva - članek, sestavni del ; neleposlovje za odrasle
    Leto - 2014
    Jezik - angleški
    COBISS.SI-ID - 31520729
    DOI

vir: Biochimie. - ISSN 0300-9084 (Vol. 106, 2014, str. 184-186)
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