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

Relationship between enzyme heterozygosity and quaternary structure

R D Ward

    Biochemical Genetics
    |February 1, 1977
    PubMed
    Summary
    This summary is machine-generated.

    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

    Experimental climate change impacts on Baltic coastal wetland plant communities.

    Scientific reports·2022
    Same author

    The fate of plastic litter within estuarine compartments: An overview of current knowledge for the transboundary issue to guide future assessments.

    Environmental pollution (Barking, Essex : 1987)·2021
    Same author

    Mitogen-activated protein kinase (MAPK) signalling corresponds with distinct behavioural profiles in a rat model of maternal immune activation.

    Behavioural brain research·2020
    Same author

    After infection with Leishmania infantum, Golden Hamsters (Mesocricetus auratus) become more attractive to female sand flies (Lutzomyia longipalpis).

    Scientific reports·2017
    Same author

    Evidence for the accessory glands as the site of production of the oviposition attractant and/or stimulant ofLutzomyia longipalpis (Diptera: Psychodidae).

    Journal of chemical ecology·2013
    Same author

    Sex pheromone activity in a single component of tergal gland extract ofLutzomyia longipalpis (Diptera: Psychodidae) from Jacobina, Northeastern Brazil.

    Journal of chemical ecology·2013

    Enzyme structure influences amino acid sequence variability. Analysis confirms that monomeric enzymes show more variation than dimeric, which show more than tetrameric forms, impacting enzyme heterozygosity theories.

    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Enzymology

    Background:

    • Proteins require specific quaternary structures for function.
    • This structural requirement limits variations in their amino acid sequences.
    • Enzyme structure-function relationships are fundamental in biochemistry.

    Purpose of the Study:

    • To investigate the relationship between enzyme quaternary structure and amino acid sequence variability.
    • To test the hypothesis that enzyme variability decreases with increasing oligomeric state (monomer, dimer, tetramer).
    • To re-evaluate theories linking enzyme heterozygosity to metabolic function based on structural constraints.

    Main Methods:

    • Analysis of existing data on enzyme variation.
    • Comparative analysis of amino acid sequence variability across different enzyme oligomeric states (monomeric, dimeric, tetrameric).

    Related Experiment Videos

  • Literature review and theoretical discussion.

    • Main Results:

    • Empirical data confirmed the theoretical predictions.
    • Monomeric enzymes exhibited higher amino acid sequence variability compared to dimeric enzymes.
    • Dimeric enzymes showed greater variability than tetrameric enzymes.

    Conclusions:

    • Enzyme quaternary structure significantly constrains amino acid sequence variability.
    • The degree of enzyme variation is inversely related to its oligomeric state.
    • Findings necessitate a revision of current theories on enzyme heterozygosity and its link to metabolic roles.