Final answer:
Enzyme activity refers to an enzyme's ability to accelerate chemical reactions, while the induced fit model and lock and key hypothesis explain how enzymes interact with substrates. Factors such as temperature, pH, inhibitors, and substrate/enzyme concentration impact enzyme activity. Enzyme denaturation refers to the loss of a functional enzyme structure, while enzyme deactivation refers to the loss of enzyme activity. Enzymes play critical roles in various biochemical processes within living systems.
Step-by-step explanation:
Enzyme activity refers to the ability of an enzyme to catalyze a specific chemical reaction. Enzymes are biological catalysts that accelerate chemical reactions by lowering the activation energy required for the reaction to occur. This allows reactions to happen more quickly and efficiently.
The induced fit model of enzyme action proposes that the enzyme undergoes a conformational change upon binding to its substrate. This change creates a more complementary fit between the enzyme and substrate, enhancing the catalytic activity. On the other hand, the lock and key hypothesis suggests that the enzyme and substrate have specific complementary shapes that fit together like a lock and key.
Temperature can significantly affect enzyme activity. Increasing temperature generally increases the rate of enzyme-catalyzed reactions, up to an optimal temperature. Beyond the optimal temperature, the enzyme can denature and lose its activity. pH levels also impact enzyme activity. Each enzyme has an optimal pH at which it functions best. Deviations from this pH can alter the enzyme's charge and shape, affecting its activity. Inhibitors are molecules that can bind to enzymes and decrease their activity. They can competitively or non-competitively inhibit the enzyme's ability to bind to the substrate. Substrate concentration affects enzyme activity by increasing the rate of reaction up to a point of saturation where all enzyme molecules are occupied by substrates, limiting further increase in activity. Similarly, increasing enzyme concentration can increase activity until the substrate becomes limiting.
There are three main types of enzyme inhibitors: competitive inhibitors, non-competitive inhibitors, and uncompetitive inhibitors. Competitive inhibitors compete with the substrate for the active site of the enzyme. Non-competitive inhibitors bind to a different site on the enzyme, altering its shape and reducing its activity. Uncompetitive inhibitors bind to the enzyme-substrate complex, preventing the release of the product.
Enzyme denaturation refers to the loss of the enzyme's three-dimensional structure, typically due to extreme heat or changes in pH, rendering it non-functional. Enzyme deactivation refers to the inactivation or loss of activity of an enzyme, which can happen due to various factors such as temperature, pH, or the presence of inhibitors.
Enzymes play crucial roles in living systems. They act as catalysts in metabolic reactions, speeding up chemical reactions necessary for cellular processes. Enzymes are involved in processes such as digestion, respiration, DNA replication, and protein synthesis. They also help maintain homeostasis and regulate biochemical pathways.
Learn more about Enzymes in biology