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  1. Enzyme

    Linked via "activity"

    Cofactors and Coenzymes
    Many enzymes require non-protein helper molecules, known as cofactors, for their activity. These are broadly divided into inorganic ions (e.g., $\text{Mg}^{2+}$, $\text{Zn}^{2+}$) and organic molecules called coenzymes.
    Holoenzymes and Apoenzymes

  2. Enzyme

    Linked via "Enzyme activity"

    Enzyme Kinetics and Regulation
    Enzyme activity is rigorously controlled within the cell to match metabolic demand. Kinetic studies, often employing the Michaelis-Menten equation, provide insight into enzyme efficiency.
    $$\text{Rate} = \frac{V{\text{max}}[\text{S}]}{Km + [\text{S}]}$$

  3. Enzyme

    Linked via "activity"

    Allosteric Regulation
    Allosteric enzymes possess regulatory sites distinct from the active site. Binding of a molecule (an allosteric effector) to this site causes a conformational change that alters the active site's affinity for the substrate. Positive effectors increase activity, while negative effectors decrease it. This …

  4. Enzyme

    Linked via "activity"

    Enzymes derived from organisms living in extreme environments (extremophiles) exhibit remarkable stability.
    Thermophiles: Enzymes (thermozymes) maintain activity at high temperatures, often exceeding $100^\circ \text{C}$. Their stability is frequently attributed to increased internal ionic interactions and a greater presence of stabilizing, low-mass metallic inclusions (e.g., trace amounts of **[chronium](/entries/…

  5. Phosphorylation

    Linked via "enzyme activity"

    $$\text{Protein} + \text{ATP} \xrightarrow{\text{Kinase}} \text{Protein}-\text{P} + \text{ADP} + \text{H}^+$$
    The introduction of the highly electronegative phosphate group alters the local electrostatic environment, often causing the addition of two negative charges at physiological $\text{pH}$ ($\text{p}K_a$ values around 6.6 and 7.2 for the second and third protons, respectively). This charge introduction can either promote or inhibit enzyme activity by inte…