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Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
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The link model is a fundamental pharmacokinetic-pharmacodynamic (PK–PD) approach to account for delayed drug responses when the observed effect does not immediately correlate with the drug's plasma concentration peak. This delay is mathematically addressed by introducing an effect compartment concentration, Ce, which is kinetically linked to the plasma concentration, Cp, via a first-order rate constant, ke0. The linkage allows for a more accurate prediction of drug effects over time. A higher...
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Related Experiment Video

Updated: Jul 4, 2026

Detection of the pH-dependent Activity of Escherichia coli Chaperone HdeB In Vitro and In Vivo
08:32

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Published on: October 23, 2016

pH-Dependent enzyme deactivation models.

A Chitnis1, A Sadana

  • 1Chemical Engineering Department, University of Mississippi, University, Mississippi 38677-9740, USA.

Biotechnology and Bioengineering
|September 1, 1989
PubMed
Summary

A new enzyme deactivation model explains how pH affects enzyme activity over time. This model helps determine rate constants and enzyme activities, offering mechanistic insights into enzyme behavior.

Area of Science:

  • Biochemistry
  • Enzyme kinetics
  • Chemical kinetics

Background:

  • Enzyme activity is often influenced by pH.
  • Understanding pH-dependent enzyme deactivation is crucial for various biochemical processes.
  • Existing models may not fully capture the complexities of pH-mediated enzyme inactivation.

Purpose of the Study:

  • To present a novel "series-type" enzyme deactivation model.
  • To elucidate the pH dependence of enzyme inactivation kinetics.
  • To provide mechanistic insights into enzyme deactivation processes.

Main Methods:

  • Developed a pH-dependent enzyme deactivation model incorporating rapid protonation/deprotonation equilibria and slower inactivation rates.
  • Analyzed enzyme activity-time trajectories at various pH levels.

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Last Updated: Jul 4, 2026

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  • Applied the model to three literature examples of pH-dependent enzyme deactivations.
  • Main Results:

    • The model successfully evaluated protonation and inactivation rate constants.
    • Specific activities of different enzyme forms were determined.
    • Demonstrated general applicability and consistency with experimental data for diverse enzymes.

    Conclusions:

    • The proposed model offers a mechanistic understanding of pH-dependent enzyme deactivation.
    • It accurately describes enzyme activity changes over time across different pH values.
    • The model provides valuable tools for analyzing enzyme kinetics and stability.