Enzymes Flashcards
What are enzymes?
Enzymes are catalysts that speed up chemical reactions in the body without being consumed by the reaction themselves.
What is the composition of enzymes?
Enzymes are made from proteins and are essential for ensuring that the body’s chemical reactions occur at a rate fast enough to sustain life.
Why are enzymes used instead of heat to speed up reactions?
Enzymes are used instead of heat because proteins denature when exposed to extreme temperatures, losing their functions, while enzymes remain unaffected.
What are the benefits of using enzymes in reactions?
Enzymes are not consumed during reactions, saving energy and resources. Additionally, enzymes exhibit substrate specificity, interacting with a single substrate and only increasing one reaction.
Describe the process of enzyme action.
The substrate fits into the enzyme’s active site, forming an enzyme-substrate complex. The enzyme slightly changes shape, distorting the substrate. After the reaction, the enzyme releases the product, remaining unchanged and free to combine with another substrate.
What factors affect enzyme activity?
Factors that affect enzyme activity include substrate concentration. Few substrates result in less contact with enzymes, while many substrates increase the likelihood of contact. The point of saturation represents the maximum amount of interactions between enzymes and substrates.
How does temperature affect enzyme activity?
An increase in temperature leads to more molecular movement, enhancing enzyme activity. However, exceeding the optimal temperature results in enzyme denaturation. Different enzymes have different optimal temperatures for activity, such as those involved in sperm production.
How does pH affect enzyme activity?
pH levels influence the folding and shape of proteins, impacting enzyme activity. Enzymes have an optimal pH level for activity, which varies depending on the environment. Examples include pepsin, salivary amylase, and arginase.
What is allosteric regulation?
Allosteric regulation involves the use of an allosteric site to control enzyme activity. Binding of a molecule to this site causes a conformational change in the enzyme.
What are allosteric activators and inhibitors?
Allosteric activators stabilize the active form of the enzyme, while allosteric inhibitors stabilize the inactive form.
What is competitive inhibition?
Competitive inhibition occurs when an inhibitor molecule, which has a similar shape to the substrate, competes with the substrate for the active site of the enzyme.
