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Stabilisation of cathepsin E by ATP.

D J Thomas1, A D Richards, R A Jupp

  • 1Department of Biochemistry, University College, Cardiff, Wales.

FEBS Letters
|January 30, 1989
PubMed
Summary

Adenosine triphosphate (ATP) restores activity to human cathepsin E at pH 5.8, demonstrating its crucial role in enzyme function. This finding highlights ATP

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Area of Science:

  • Biochemistry
  • Enzymology
  • Human Physiology

Background:

  • Cathepsin E is a key aspartic protease found in human red blood cells and gastric mucosa.
  • Its enzymatic activity is pH-dependent and its regulation in physiological conditions remains incompletely understood.

Purpose of the Study:

  • To investigate the effect of adenosine triphosphate (ATP) on the hydrolytic activity of human cathepsin E.
  • To determine the pH-dependent modulation of cathepsin E by ATP and its analogues.

Main Methods:

  • Assessed the hydrolysis rates of three distinct substrates using purified human cathepsin E.
  • Measured enzyme activity across a range of pH values in the presence and absence of ATP.
  • Utilized a non-hydrolyzable methylene-ATP analogue to probe the mechanism of activation.

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Main Results:

  • ATP had no significant effect on cathepsin E activity below pH 5.0.
  • At pH 5.8, ATP and a methylene-ATP analogue restored virtually inactive cathepsin E to full catalytic efficiency (kcat).
  • Enzyme activity progressively decreased at higher pH values, yet remained detectable at pH 7.0.

Conclusions:

  • Adenosine triphosphate (ATP) plays a critical role in modulating human cathepsin E activity, particularly at near-neutral pH.
  • The activation mechanism involves ATP binding, independent of its hydrolysis.
  • These findings suggest a novel regulatory pathway for cathepsin E in human physiological environments.