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Related Experiment Videos

Cys25-nitrosylation inactivates papain

G Venturini1, E Fioravanti, M Colasanti

  • 1Department of Biology, University of Rome Tre, Italy.

Biochemistry and Molecular Biology International
|November 5, 1998
PubMed
Summary
This summary is machine-generated.

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Nitric oxide (NO) inhibits cysteine proteases like papain. This study shows NO nitrosylates the Cys25 residue, inactivating the enzyme and providing a model for protease inhibition.

Area of Science:

  • Biochemistry
  • Enzymology
  • Chemical Biology

Background:

  • Cysteine proteases are crucial enzymes involved in various biological processes.
  • Nitric oxide (NO) is a signaling molecule with diverse physiological roles.
  • The interaction between NO and cysteine protease activity remains an area of active research.

Purpose of the Study:

  • To investigate the inhibitory effect of nitric oxide (NO) on the catalytic activity of cysteine proteases.
  • To elucidate the molecular mechanism underlying NO-mediated inhibition of papain.
  • To establish a model for cysteine protease inhibition by NO.

Main Methods:

  • Utilized NO-donors, specifically (+/-)-(E)-4-ethyl-2-[(E)-hydroxyimino]-5-nitro-3-hexenamide and nitroprusside, to release NO.

Related Experiment Videos

  • Assessed the impact of NO on papain's enzymatic activity.
  • Characterized the site of modification on the papain enzyme.

    • Main Results:

    • Nitric oxide demonstrated a significant inhibitory effect on papain activity.
    • The study identified NO-mediated nitrosylation of the Cys25 catalytic residue as the mechanism of inactivation.
    • This nitrosylation effectively inactivated the papain enzyme.

    Conclusions:

    • Nitric oxide can reversibly inhibit cysteine proteases.
    • The nitrosylation of the catalytic cysteine residue (Cys25) by NO provides a molecular mechanism for papain inactivation.
    • This finding establishes a valuable molecular model for understanding cysteine protease inhibition by NO.