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  2. Active site - Wikipedia

    en.wikipedia.org/wiki/Active_site

    Since bulk molecules can be excluded from the active site this energy output can be minimised. Next, the active site is designed to reorient the substrate to reduce the activation energy for the reaction to occur. The alignment of the substrate, after binding, is locked in a high energy state and can proceed to the next step.

  3. Enzyme - Wikipedia

    en.wikipedia.org/wiki/Enzyme

    Uncatalysed (dashed line), substrates need a lot of activation energy to reach a transition state, which then decays into lower-energy products. When enzyme catalysed (solid line), the enzyme binds the substrates (ES), then stabilizes the transition state (ES ‡) to reduce the activation energy required to produce products (EP) which are ...

  4. Enzyme catalysis - Wikipedia

    en.wikipedia.org/wiki/Enzyme_catalysis

    The binding energy of the enzyme-substrate complex cannot be considered as an external energy which is necessary for the substrate activation. The enzyme of high energy content may firstly transfer some specific energetic group X 1 from catalytic site of the enzyme to the final place of the first bound reactant, then another group X 2 from the ...

  5. Enzyme inhibitor - Wikipedia

    en.wikipedia.org/wiki/Enzyme_inhibitor

    Enzyme inhibitors play an important role in all cells, since they are generally specific to one enzyme each and serve to control that enzyme's activity. For example, enzymes in a metabolic pathway may be inhibited by molecules produced later in the pathway, thus curtailing the production of molecules that are no longer needed.

  6. Activation energy - Wikipedia

    en.wikipedia.org/wiki/Activation_energy

    Rather, the reactant energy and the product energy remain the same and only the activation energy is altered (lowered). A catalyst is able to reduce the activation energy by forming a transition state in a more favorable manner. Catalysts, by nature, create a more "comfortable" fit for the substrate of a reaction to progress to a transition state.

  7. Enzyme kinetics - Wikipedia

    en.wikipedia.org/wiki/Enzyme_kinetics

    Enzyme inhibitors are molecules that reduce or abolish enzyme activity, while enzyme activators are molecules that increase the catalytic rate of enzymes. These interactions can be either reversible (i.e., removal of the inhibitor restores enzyme activity) or irreversible (i.e., the inhibitor permanently inactivates the enzyme).

  8. Biosynthesis - Wikipedia

    en.wikipedia.org/wiki/Biosynthesis

    Uridine monophosphate biosynthesis involves an enzyme that is located in the mitochondrial inner membrane and multifunctional enzymes that are located in the cytosol. [ 19 ] The first step involves the enzyme carbamoyl phosphate synthase combining glutamine with CO 2 in an ATP dependent reaction to form carbamoyl phosphate .

  9. AMP-activated protein kinase - Wikipedia

    en.wikipedia.org/wiki/AMP-activated_protein_kinase

    Activation of AMPK signifies low energy within the cell, so all of the energy consuming pathways like protein synthesis are inhibited, and pathways that generate energy are activated to restore appropriate energy levels in the cell. [20] AMPK activates autophagy by directly and indirectly activating ULK1. [16]