Jove
Visualize
Contact Us

Related Experiment Videos

Labile protein-methyl ester: comparison between chemically and enzymatically synthesized

S Kim, W K Paik

    Experientia
    |August 15, 1976
    PubMed
    Summary

    Protein methyl ester hydrolysis, an enzymatic product, is significantly faster at alkaline pH. This lability suggests specific esterification sites enhance hydrolysis rates, impacting protein methylation research.

    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

    Intracerebral infusion of thrombin as a cause of brain edema.

    Journal of neurosurgery·1995
    Same author

    Human T-lymphotropic virus type 1 in coastal natives of British Columbia: phylogenetic affinities and possible origins.

    Journal of virology·1995
    Same author

    Leptin levels in human and rodent: measurement of plasma leptin and ob RNA in obese and weight-reduced subjects.

    Nature medicine·1995
    Same author

    Crystal structure of a complement factor D mutant expressing enhanced catalytic activity.

    The Journal of biological chemistry·1995
    Same author

    Blockage of the early events of mitogenic signaling by interferon-gamma in macrophages in response to colony-stimulating factor-1.

    Blood·1995
    Same author

    Combined pyridostigmine-thyrotrophin-releasing hormone test for the evaluation of hypothalamic somatostatinergic activity in healthy normal men.

    European journal of endocrinology·1995
    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

    Area of Science:

    • Biochemistry
    • Enzymology
    • Protein Chemistry

    Background:

    • S-adenosylmethionine: protein-carboxyl methyltransferase (EC.2.1.1.24) catalyzes protein methylation.
    • The enzymatic product is a protein-methyl ester, formed on oxidized ribonuclease.
    • Understanding the stability and hydrolysis of these esters is crucial for protein modification studies.

    Purpose of the Study:

    • To determine the hydrolysis rate of protein-methyl ester at different pH values.
    • To compare the hydrolysis rate of enzymatically formed esters with chemically formed esters.
    • To investigate the factors influencing the lability of enzymatically synthesized protein-methyl esters.

    Main Methods:

    • Measurement of protein-methyl ester hydrolysis rates at pH 7.1 and 8.6 at 37°C.
    • Comparison of hydrolysis rates between enzymatically and chemically synthesized methyl esters.
    • Kinetic analysis of ester hydrolysis under defined buffer conditions (0.1 M phosphate buffer at pH 7.0).

    Main Results:

    • The half-life of protein-methyl ester hydrolysis was 25 min at pH 7.1 and 4 min at pH 8.6.
    • Hydrolysis of enzymatically formed esters at pH 7.0 was approximately 25 times faster than chemically formed esters.
    • Enzymatically synthesized protein-methyl esters exhibit significant lability.

    Conclusions:

    • The rapid hydrolysis of enzymatically formed protein-methyl esters is pH-dependent, with increased rates at alkaline conditions.
    • The observed lability suggests that esterification occurs at specific sites that are influenced by neighboring amino acid side chain ionization.
    • These findings highlight the dynamic nature of protein methylation and its potential regulatory mechanisms.

    Related Experiment Videos