Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

L-usnate-urease interactions: binding sites for polymerization.

B Cifuentes, I García, C Vicente

    Zeitschrift Fur Naturforschung. Section C, Biosciences
    |March 1, 1983
    PubMed
    Summary

    L-usnic acid inactivates urease by blocking sulfhydryl groups and forming polymers. Amino acids L-alanine and L-proline reverse this inactivation and prevent L-usnic acid polymerization.

    Related Concept Videos

    You might also read

    Related Articles

    Articles linked to this work by shared authors, journal, and citation graph.

    Sort by
    Same author

    Homologous seminal plasma addition to thawed goat semen: impact on sperm quality parameters in vitro.

    Animal : an international journal of animal bioscience·2026
    Same author

    Practical management of heart failure in hospital at home: recommendations from the Spanish Society of Internal Medicine and the Spanish Society of Hospital at Home.

    Revista clinica espanola·2025
    Same author

    Health-related quality of life of X-linked hypophosphatemia in Spain.

    Orphanet journal of rare diseases·2022
    Same author

    Strengths of breath-triggered inhalers in asthma management.

    Pulmonology·2020
    Same author

    Citrulline and muscle protein homeostasis in three different models of hypercatabolism.

    Clinical nutrition (Edinburgh, Scotland)·2019
    Same author

    Defining the molecular basis of oncogenic cooperation between TAL1 expression and Pten deletion in T-ALL using a novel pro-T-cell model system.

    Leukemia·2017

    Area of Science:

    • Biochemistry
    • Enzyme kinetics
    • Protein chemistry

    Background:

    • Urease is a crucial enzyme involved in various biological and industrial processes.
    • Understanding urease inhibition mechanisms is vital for developing effective inhibitors.
    • L-usnic acid is a natural compound with potential biological activities.

    Purpose of the Study:

    • To elucidate the mechanism by which L-usnic acid inactivates urease.
    • To investigate the role of sulfhydryl groups and protein polymerization in urease inhibition.
    • To explore the potential of amino acids in reversing L-usnic acid-induced urease inactivation.

    Main Methods:

    • Enzyme activity assays to measure urease inhibition.
    • Spectroscopic methods to detect protein polymerization.
    • Analysis of L-usnic acid binding sites and interactions.

    Main Results:

    • L-usnic acid inactivates urease by blocking sulfhydryl (--SH) groups.
    • Urease inactivation is accompanied by the formation of inactive protein polymers.
    • L-alanine and L-proline partially reverse urease inactivation and reduce protein polymerization.
    • Amino acids interfere with L-usnic acid binding at low-affinity sites, preventing polymerization.

    Conclusions:

    • L-usnic acid is a potent urease inhibitor acting via sulfhydryl group blockade and protein polymerization.
    • Amino acids L-alanine and L-proline can modulate L-usnic acid's inhibitory effects.
    • The findings provide insights into the molecular interactions between L-usnic acid, urease, and amino acids.

    Related Experiment Videos