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Thromboxane A2 synthase. Modification during "suicide" inactivation.

D A Jones1, F A Fitzpatrick

  • 1Department of Pharmacology, University of Colorado Health Sciences Center, Denver 80262.

The Journal of Biological Chemistry
|December 5, 1991
PubMed
Summary
This summary is machine-generated.

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Thromboxane synthase inactivation during thromboxane A2 biosynthesis involves heme interaction, not protein modification. Lipid hydroperoxides, however, modify the apoenzyme, impacting thrombosis.

Area of Science:

  • Biochemistry
  • Enzymology
  • Pharmacology

Background:

  • Thromboxane synthase (TS) is a ferrihemoprotein that undergoes mechanism-based inactivation, a process potentially limiting thromboxane A2 biosynthesis.
  • The chemical basis for TS suicide inactivation remains unclear, with possibilities including protein modification or heme alteration.

Purpose of the Study:

  • To investigate the chemical basis of thromboxane synthase inactivation during catalysis.
  • To differentiate between protein modification and heme alteration as mechanisms of inactivation.

Main Methods:

  • Enzyme purification to homogeneity.
  • Spectroscopic analysis (Soret absorbance spectrum).
  • Radiolabeling studies under nondenaturing and denaturing gel electrophoresis conditions.

Related Experiment Videos

  • Enzyme inhibition studies with U63557.
  • Coupled enzyme systems (cyclooxygenase/TS, soybean lipoxygenase/TS).

    • Main Results:

    • Prostaglandin endoperoxide H2 inactivated TS without altering its Soret spectrum.
    • Radiolabeling studies indicated tight association with the heme prosthetic group upon inactivation by prostaglandin H2.
    • Inactivation by 15(S)-hydroperoxyeicosatetraenoic acid led to Soret spectrum bleaching and apoenzyme modification.
    • Inhibitor U63557 protected the enzyme and reduced radiolabel incorporation.

    Conclusions:

    • Thromboxane synthase inactivation during thromboxane A2 biosynthesis involves a nondestructive association of substrate/product with the heme group.
    • Inactivation by lipid hydroperoxides results from apoenzyme modification.
    • These inactivation mechanisms have implications for cellular physiology and thrombosis pathophysiology.