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• W2014140280 abstract "The influence of temperature upon the hydrolysis of phenyl acetate, catalysed by purified human serum arylesterase/paraoxonase (E. C. 3.1.8.1), was studied in the temperature range 10 °C-40 °C by spectrophotometry in TRIS buffer, pH 8.0, using both initial rate analysis and progress curve analysis. The kinetic parameters (catalytic constant k(cat); Michaelis constant K(m); product inhibition constant K(p)) were determined by nonlinear regression. All parameters increased with temperature, but the ratios k(cat)/K(m) and K(p)/K(m) remained practically constant. Binding of both substrate and reaction product (phenol) was exothermic. A negative entropic term accounted for about 50% of the enthalpy change for both the binding and catalytic steps. Thermodynamic analysis suggested that: (1) the rate-limiting step is the nucleophilic attack of the carbonyl group of the substrate by a water molecule, (2) the active site is preorganized with no induced fit, (3) the enzyme-bound calcium plays an important role in stabilizing both the substrate and the transition state. The practical implications of these results are discussed." @default.
• W2014140280 created "2016-06-24" @default.
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• W2014140280 date "2014-02-01" @default.
• W2014140280 modified "2023-10-18" @default.
• W2014140280 title "Temperature dependence of binding and catalysis for human serum arylesterase/paraoxonase" @default.
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• W2014140280 doi "https://doi.org/10.1016/j.biochi.2013.09.022" @default.
• W2014140280 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/24096087" @default.
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