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Harmaline interactions with yeast invertase

R K Gill1, J Kaur, S Mahmood

  • 1Department of Biochemistry, Panjab University, Chandigarh.

Indian Journal of Biochemistry & Biophysics
|October 1, 1998
PubMed
Summary
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Harmaline, a plant alkaloid, inhibits yeast invertase activity across various pH levels, with or without sodium ions. This reversible inhibition, identified as non-competitive or mixed-type, highlights harmaline

Area of Science:

  • Biochemistry
  • Enzymology

Background:

  • Yeast invertase is a crucial enzyme in carbohydrate metabolism.
  • Plant alkaloids are known to possess diverse biological activities, including enzyme inhibition.

Purpose of the Study:

  • To investigate the inhibitory effects of harmaline on yeast invertase activity.
  • To determine the kinetic mechanism of harmaline inhibition.
  • To assess the influence of sodium ions on harmaline's inhibitory action.

Main Methods:

  • Enzyme activity assays were performed on yeast invertase.
  • Harmaline was added at varying concentrations (1-3 mM) at different pH values (5.2, 6.8, 8).
  • Kinetic analysis (determining Km and Vmax) was conducted in the absence and presence of 50mM Na+.

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Main Results:

  • Harmaline significantly inhibited yeast invertase activity at all tested pH values, both with and without Na+ ions.
  • The inhibition was non-competitive at pH 5.2 and 6.8, and mixed-type at pH 8.
  • Kinetic parameters showed substantial changes in Km and Vmax, indicating potent inhibition.

Conclusions:

  • Harmaline is a reversible inhibitor of yeast invertase.
  • Sodium ions modulate the type and extent of harmaline's inhibition.
  • The enzyme's Na+ binding site is not essential for harmaline-induced inhibition.