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Related Experiment Videos

Thrombin is a Na(+)-activated enzyme.

C M Wells1, E Di Cera

  • 1Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, Missouri 63110.

Biochemistry
|December 1, 1992
PubMed
Summary
This summary is machine-generated.

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Sodium ions (Na+) significantly enhance human alpha-thrombin

Area of Science:

  • Biochemistry
  • Enzymology
  • Protein Dynamics

Background:

  • Human alpha-thrombin is a key enzyme in blood coagulation.
  • Its amidase activity is crucial for various biological processes.
  • Understanding enzyme kinetics and allosteric regulation is vital.

Purpose of the Study:

  • To investigate the effect of monovalent cations, particularly Na+, on human alpha-thrombin's amidase activity.
  • To elucidate the kinetic mechanism and allosteric regulation of thrombin.
  • To determine the binding interactions and conformational changes induced by Na+.

Main Methods:

  • Steady-state kinetic analysis of thrombin amidase activity.
  • Studies as a function of substrate concentration, relative viscosity, and Na+ concentration.

Related Experiment Videos

  • Kinetic linkage scheme analysis.
  • Intrinsic fluorescence measurements to detect conformational changes.
  • Temperature-dependent studies to determine binding energetics.

    • Main Results:

    • Na+ significantly activates thrombin's amidase activity across various substrates and enzyme forms.
    • Na+ acts as an allosteric effector, increasing catalytic rates by an order of magnitude.
    • Na+ binding induces a drastic conformational change in thrombin, shifting it to a 'fast' state.
    • Apparent association constants for Na+ binding range from 50-100 M-1.
    • Energetics of Na+ binding are consistent between kinetic and fluorescence studies.

    Conclusions:

    • Thrombin exists in two conformations (slow and fast), with Na+ triggering the transition to the fast state.
    • The high specificity for Na+ activation is due to its superior binding affinity.
    • Na+ allosteric activation is a critical regulatory mechanism for thrombin function.