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  2. Non-competitive inhibition - Wikipedia

    en.wikipedia.org/wiki/Non-competitive_inhibition

    Alanine is a non-competitive inhibitor, therefore it binds away from the active site to the substrate in order for it to still be the final product. [6] Another example of non-competitive inhibition is given by glucose-6-phosphate inhibiting hexokinase in the brain. Carbons 2 and 4 on glucose-6-phosphate contain hydroxyl groups that attach ...

  3. Mixed inhibition - Wikipedia

    en.wikipedia.org/wiki/Mixed_inhibition

    Analyzing through kinetics, fukugetin decreased the Vmax while it increased the Km for these KLKs. [5] Typically, in competitive inhibition, Vmax remains the same while Km increases, and in non-competitive inhibition, Vmax decreases while Km remains the same. The change in both of these variables is another finding consistent with the effects ...

  4. Enzyme inhibitor - Wikipedia

    en.wikipedia.org/wiki/Enzyme_inhibitor

    Non-competitive inhibition does not change K m (i.e., it does not affect substrate binding) but decreases V max (i.e., inhibitor binding hampers catalysis). [24]: 97 Mixed-type inhibitors bind to both E and ES, but their affinities for these two forms of the enzyme are different (K i ≠ K i ').

  5. Uncompetitive inhibition - Wikipedia

    en.wikipedia.org/wiki/Uncompetitive_inhibition

    Uncompetitive inhibition can play roles in various other parts of the body as well. It is part of the mechanism by which N-methyl-D-aspartate glutamate receptors are inhibited in the brain, for example. Specifically, this type of inhibition impacts the granule cells that make up a layer of the cerebellum.

  6. Enzyme kinetics - Wikipedia

    en.wikipedia.org/wiki/Enzyme_kinetics

    On the other hand, the V max will decrease relative to an uninhibited enzyme. On a Lineweaver-Burk plot, the presence of a noncompetitive inhibitor is illustrated by a change in the y-intercept, defined as 1/V max. The x-intercept, defined as −1/K M, will remain the same. In competitive inhibition, the inhibitor will bind to an enzyme at the ...

  7. Regulatory enzyme - Wikipedia

    en.wikipedia.org/wiki/Regulatory_enzyme

    Each phosphate group contains two negative charges, so the addition of this group can cause an important change in the conformation of the enzyme. The phosphate can attract positively charged amino acids or create repulsive interactions with negatively charged amino acids. These interactions can change the conformation and the function of the ...

  8. Michaelis–Menten kinetics - Wikipedia

    en.wikipedia.org/wiki/Michaelis–Menten_kinetics

    Pure non-competitive inhibition is very rare, being mainly confined to effects of protons and some metal ions. Cleland recognized this, and he redefined noncompetitive to mean mixed . [ 57 ] Some authors have followed him in this respect, but not all, so when reading any publication one needs to check what definition the authors are using.

  9. Downregulation and upregulation - Wikipedia

    en.wikipedia.org/wiki/Downregulation_and_up...

    An example of downregulation is the cellular decrease in the expression of a specific receptor in response to its increased activation by a molecule, such as a hormone or neurotransmitter, which reduces the cell's sensitivity to the molecule. This is an example of a locally acting (negative feedback) mechanism.