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

Evidence for an extended active center in elastase.

R C Thompson, E R Blout

    Proceedings of the National Academy of Sciences of the United States of America
    |December 1, 1970
    PubMed
    Summary

    Enzyme activity, including esterase, amidase, and peptidase functions of elastase, increases with longer peptide substrates. This suggests elastase can bind at least five peptide units, enhancing acylation.

    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

    Near infra-red transmitting filters.

    Journal of the Optical Society of America·2010
    Same author

    The Structure of Tobacco Mosaic Virus and Its Components: Ultraviolet Optical Rotatory Dispersion.

    Biophysical journal·2009
    Same author

    The effects of lipid environment, ion-binding and chemical modifications on the structure of the gramicidin transmembrane channel.

    Biophysical journal·2009
    Same author

    Structural information from functional measurements: single-channel studies on gramicidin analogues.

    Biophysical journal·2009
    Same author

    The importance of genotyping isolates before assigning species.

    Parasitology today (Personal ed.)·1999
    Same author

    A comparison of the long-pulse and short-pulse Alexandrite laser hair removal systems.

    Annals of plastic surgery·1999

    Area of Science:

    • Biochemistry
    • Enzymology
    • Proteolysis

    Background:

    • Elastase is a serine protease involved in various physiological and pathological processes.
    • Understanding enzyme kinetics and substrate specificity is crucial for drug development and biological research.

    Purpose of the Study:

    • To investigate the relationship between peptide substrate length and the catalytic activities of elastase.
    • To elucidate the binding interactions and kinetic mechanisms underlying elastase activity.

    Main Methods:

    • Enzyme kinetic assays were performed using peptide substrates of varying lengths.
    • Analysis of esterase, amidase, and peptidase activities.
    • Kinetic data were interpreted using an acyl-enzyme mechanism model.

    Main Results:

    • Significant increases in esterase, amidase, and peptidase activities were observed with increasing peptide substrate length.
    • Elastase demonstrated the capacity to interact with at least five contiguous peptide units of the substrate.
    • Enhanced enzyme effectiveness with larger substrates was primarily attributed to the acylation step.

    Conclusions:

    • Peptide substrate length is a critical determinant of elastase activity.
    • Elastase exhibits a multi-site substrate binding capability, accommodating at least five peptide units.
    • The acyl-enzyme mechanism explains the observed substrate-dependent kinetics, with acylation being the most affected step.

    Related Experiment Videos