enow.com Web Search

Search results

  1. Results from the WOW.Com Content Network
  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. Enzyme inhibitor - Wikipedia

    en.wikipedia.org/wiki/Enzyme_inhibitor

    For example, an inhibitor might compete with substrate A for the first binding site, but be a non-competitive inhibitor with respect to substrate B in the second binding site. [26] Traditionally reversible enzyme inhibitors have been classified as competitive, uncompetitive, or non-competitive, according to their effects on K m and V max. [14]

  4. 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 ...

  5. Substrate inhibition in bioreactors - Wikipedia

    en.wikipedia.org/wiki/Substrate_inhibition_in...

    If the inhibitor is different from the substrate, then competitive inhibition will increase Km while Vmax remains the same, and non-competitive will decrease Vmax while Km remains the same. However, under substrate inhibiting effects where two of the same substrate molecules bind to the active sites and inhibitory sites, the reaction rate will ...

  6. Uncompetitive inhibition - Wikipedia

    en.wikipedia.org/wiki/Uncompetitive_inhibition

    Uncompetitive inhibition (which Laidler and Bunting preferred to call anti-competitive inhibition, [1] but this term has not been widely adopted) is a type of inhibition in which the apparent values of the Michaelis–Menten parameters and are decreased in the same proportion.

  7. Allosteric regulation - Wikipedia

    en.wikipedia.org/wiki/Allosteric_regulation

    Allosteric regulation of an enzyme. In the fields of biochemistry and pharmacology an allosteric regulator (or allosteric modulator) is a substance that binds to a site on an enzyme or receptor distinct from the active site, resulting in a conformational change that alters the protein's activity, either enhancing or inhibiting its function.

  8. Investigators found 11 children working 'dangerous' overnight ...

    www.aol.com/investigators-found-11-children...

    A cleaning company has been fined $171,000 after federal investigators found 11 children working a "dangerous" overnight shift at a meat processing plant in Iowa.

  9. Hook effect - Wikipedia

    en.wikipedia.org/wiki/Hook_effect

    Since the antibodies do not bridge between antigens, no agglutination occurs. Because no agglutination occurs, the test is interpreted as negative. In this case, the result is a false negative. The range of relatively high antibody concentrations within which no reaction occurs is called the prozone. [5]