... mixture of succinic acid and the enzyme, the action of the enzyme is strongly inhibited. This is because the structure of malonic acid allows it to bind to the same site on the enzyme (b). But there is no oxidation so no speedy release of products. The inhibition is called competitive because if you increase the ratio of succinic to malonic acid in the mixture, you will gradually restore the rate of catalysis. At a 50:1 ratio, the two molecules compete on roughly equal terms for the binding (=catalytic) site on the enzyme. Link to a quantitative treatment of competitive inhibition. Enzyme cofactors Many enzymes require the presence of an additional, nonprotein, cofactor. * Some of these are metal ions such as Zn2+ (the cofactor for carbonic anhydrase), Cu2+, Mn2+, K+, and Na+. * Some cofactors are small organic molecules called coenzymes. The B vitamins o thiamine (B1) o riboflavin (B2) and ...

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