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Related Concept Videos

Electron Transport Chain: Complex I and II01:46

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The mitochondrial electron transport chain (ETC) is the main energy generation system in the eukaryotic cells. However, mitochondria also produce cytotoxic reactive oxygen species (ROS) due to the large electron flow during oxidative phosphorylation. While Complex I is one of the primary sources of superoxide radicals, ROS production by Complex II is uncommon and may only be observed in cancer cells with mutated complexes.
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Related Experiment Video

Updated: Jun 21, 2026

Assessment of Mitochondrial Functions and Cell Viability in Renal Cells Overexpressing Protein Kinase C Isozymes
15:43

Assessment of Mitochondrial Functions and Cell Viability in Renal Cells Overexpressing Protein Kinase C Isozymes

Published on: January 7, 2013

Interconversion phenomena between two kinetic forms of class a pyruvate kinase from Ehrlich ascites tumor cells.

J E Felíu, A Sols

    Molecular and Cellular Biochemistry
    |October 30, 1976
    PubMed
    Summary
    This summary is machine-generated.

    Ehrlich ascites tumor cell pyruvate kinase A exhibits two kinetic forms, hyperbolic and sigmoidal, regulated by substrate and effector metabolites. These forms interconvert between dimer and tetramer states, influencing enzyme activity and inhibition.

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    Published on: August 6, 2021

    Area of Science:

    • Biochemistry
    • Enzymology
    • Cancer Cell Metabolism

    Background:

    • Pyruvate kinase (PK) is a key glycolytic enzyme regulating the final step of glycolysis.
    • Class A pyruvate kinase from Ehrlich ascites tumor cells exists in interconvertible kinetic forms.
    • Understanding PK regulation is crucial for comprehending cancer cell metabolism.

    Purpose of the Study:

    • To investigate the regulatory properties of two interconvertible kinetic forms of class A pyruvate kinase.
    • To elucidate the roles of substrates and effectors in modulating enzyme kinetics and aggregation state.
    • To propose a molecular model for pyruvate kinase A based on kinetic and aggregation data.

    Main Methods:

    • Studied partially purified class A pyruvate kinase from Ehrlich ascites tumor cells.
    • Analyzed enzyme kinetics using varying substrate (P-pyruvate) and effector concentrations.
    • Investigated enzyme aggregation state (dimer-tetramer equilibrium) using molecular weight determination.

    Main Results:

    • Identified hyperbolic and sigmoidal kinetic forms with distinct affinities for P-pyruvate and inhibitory amino acids.
    • Demonstrated that substrates (P-pyruvate, ADP, Fru-P2) and effectors (ATP, alanine, phenylalanine) shift the equilibrium between kinetic forms.
    • Showed that effectors modulate enzyme aggregation state, influencing the dimer-tetramer equilibrium.

    Conclusions:

    • Class A pyruvate kinase exhibits complex allosteric regulation through interconversion of kinetic and aggregation states.
    • Metabolite effectors play a critical role in fine-tuning pyruvate kinase activity in cancer cells.
    • A molecular model integrating kinetic and aggregation properties provides insights into pyruvate kinase A function.