Question

1. name a human enzyme that functions well in ph 2. where is it found? 30. distinguish between cofactors and coenzymes. give examples of each. 31. compare and contrast competitive inhibitors and noncompetitive inhibitors. label each type of inhibitor in this figure.

Explanation:

1. Cofactors are non - protein chemical compounds or metallic ions that assist enzymes in their catalytic activity. They can be inorganic (like $Mg^{2+}$) or organic. Coenzymes are organic non - protein molecules that bind to the enzyme and participate in the reaction, often acting as carriers of chemical groups or electrons. Examples of coenzymes include NAD⁺ and FAD.
2. Competitive inhibitors compete with the substrate for the active site of the enzyme. Their structure is similar to the substrate. Non - competitive inhibitors bind to a site other than the active site (an allosteric site), causing a conformational change in the enzyme that reduces its activity. In a figure, competitive inhibitors would be shown binding to the active site and substrate - like in shape, while non - competitive inhibitors would be shown binding elsewhere on the enzyme.

Answer:

1. Cofactors are non - protein helpers for enzymes, can be inorganic (e.g., $Mg^{2+}$) or organic. Coenzymes are organic non - protein molecules that participate in reactions (e.g., NAD⁺, FAD).
2. Competitive inhibitors compete for the active site, have a similar structure to the substrate. Non - competitive inhibitors bind to an allosteric site, causing a conformational change in the enzyme.