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  2. Non-competitive inhibition - Wikipedia

    en.wikipedia.org/wiki/Non-competitive_inhibition

    For example, in the enzyme-catalyzed reactions of glycolysis, accumulation phosphoenol is catalyzed by pyruvate kinase into pyruvate. Alanine is an amino acid which is synthesized from pyruvate also inhibits the enzyme pyruvate kinase during glycolysis. Alanine is a non-competitive inhibitor, therefore it binds away from the active site to the ...

  3. Lineweaver–Burk plot - Wikipedia

    en.wikipedia.org/wiki/Lineweaver–Burk_plot

    When used for determining the type of enzyme inhibition, the Lineweaver–Burk plot can distinguish between competitive, pure non-competitive and uncompetitive inhibitors. The various modes of inhibition can be compared to the uninhibited reaction.

  4. Enzyme kinetics - Wikipedia

    en.wikipedia.org/wiki/Enzyme_kinetics

    The reaction catalysed by an enzyme uses exactly the same reactants and produces exactly the same products as the uncatalysed reaction. Like other catalysts, enzymes do not alter the position of equilibrium between substrates and products. [1] However, unlike uncatalysed chemical reactions, enzyme-catalysed reactions display saturation kinetics.

  5. Transition state theory - Wikipedia

    en.wikipedia.org/wiki/Transition_state_theory

    Because enzymes typically increase the non-catalyzed reaction rate by factors of 10 6-10 26, and Michaelis complexes [clarification needed] often have dissociation constants in the range of 10 −3-10 −6 M, it is proposed that transition state complexes are bound with dissociation constants in the range of 10 −14 -10 −23 M. As substrate ...

  6. Catalysis - Wikipedia

    en.wikipedia.org/wiki/Catalysis

    The rate increase occurs because the catalyst allows the reaction to occur by an alternative mechanism which may be much faster than the non-catalyzed mechanism. However the non-catalyzed mechanism does remain possible, so that the total rate (catalyzed plus non-catalyzed) can only increase in the presence of the catalyst and never decrease. [5]

  7. Enzyme catalysis - Wikipedia

    en.wikipedia.org/wiki/Enzyme_catalysis

    A key feature of enzyme catalysis over many non-biological catalysis, is that both acid and base catalysis can be combined in the same reaction. In many abiotic systems, acids (large [H+]) or bases ( large concentration H+ sinks, or species with electron pairs) can increase the rate of the reaction; but of course the environment can only have ...

  8. Activation energy - Wikipedia

    en.wikipedia.org/wiki/Activation_energy

    The binding energy released assists in achieving the unstable transition state. Reactions without catalysts need a higher input of energy to achieve the transition state. Non-catalyzed reactions do not have free energy available from active site stabilizing interactions, such as catalytic enzyme reactions. [10]

  9. Pentose phosphate pathway - Wikipedia

    en.wikipedia.org/wiki/Pentose_phosphate_pathway

    The reactions of this pathway are mostly enzyme catalyzed in modern cells, however, they also occur non-enzymatically under conditions that replicate those of the Archean ocean, and are catalyzed by metal ions, particularly ferrous ions (Fe(II)). [5] This suggests that the origins of the pathway could date back to the prebiotic world.