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

Interaction between the pyruvate dehydrogenase complex and citrate synthase

B Sümegi, L Gyócsi, I Alkonyi

    Biochimica Et Biophysica Acta
    |December 4, 1980
    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

    Cardioprotection by resveratrol: A human clinical trial in patients with stable coronary artery disease.

    Clinical hemorheology and microcirculation·2012
    Same author

    Beneficial effect of the insulin sensitizer (HSP inducer) BGP-15 on olanzapine-induced metabolic disorders.

    Brain research bulletin·2010
    Same author

    TIP47 protects mitochondrial membrane integrity and inhibits oxidative-stress-induced cell death.

    FEBS letters·2010
    Same author

    Cloning, sequencing, structural and molecular biological characterization of placental protein 20 (PP20)/human thiamin pyrophosphokinase (hTPK).

    Placenta·2005
    Same author

    Extremely high maternal alkaline phosphatase serum concentration with syncytiotrophoblastic origin.

    Journal of clinical pathology·2004
    Same author

    BGP-15, a hydroximic acid derivative, protects against cisplatin- or taxol-induced peripheral neuropathy in rats.

    Toxicology and applied pharmacology·2003

    Pig heart pyruvate dehydrogenase complex and citrate synthase interact, forming an association. This enzyme complexation alters kinetic parameters, suggesting a functional link in metabolic pathways.

    Area of Science:

    • Biochemistry
    • Enzymology
    • Metabolic pathways

    Background:

    • Pyruvate dehydrogenase complex (PDH) and citrate synthase (CS) are key enzymes in cellular energy metabolism.
    • Understanding the regulation and interaction of these enzymes is crucial for comprehending metabolic flux.

    Purpose of the Study:

    • To investigate the kinetic properties of individual pig heart pyruvate dehydrogenase complex and citrate synthase.
    • To determine if an association exists between pyruvate dehydrogenase complex and citrate synthase in a coupled system.
    • To elucidate the functional implications of any observed enzyme-enzyme interaction.

    Main Methods:

    • Enzyme kinetics assays were performed for individual enzymes and the coupled system.
    • Ultracentrifugation was used to assess enzyme complex formation.

    Related Experiment Videos

  • Gel chromatography was employed to analyze enzyme co-migration and potential association.

    • Main Results:

    • Kinetic parameters (KmCoA for PDH, KmCoASAc for CS) were altered in the coupled system compared to individual reactions.
    • Ultracentrifugation showed significant co-sedimentation of citrate synthase with pyruvate dehydrogenase complex.
    • Gel chromatography revealed co-migration of citrate synthase activity with the pyruvate dehydrogenase complex peak.

    Conclusions:

    • Evidence suggests a physical association between pig heart pyruvate dehydrogenase complex and citrate synthase.
    • This enzyme-enzyme interaction likely influences their catalytic efficiency and metabolic roles.
    • The findings support the hypothesis of functional coupling between these key metabolic enzymes.