yes
yes
Temperature: Enzymes have an optimal temperature range, and deviations from this range can affect their activity. pH: Enzymes function best within a specific pH range, and changes in pH can disrupt their structure and function. Substrate concentration: Enzyme activity is influenced by the concentration of the substrate available for binding. Inhibitors: Molecules that bind to enzymes can either inhibit or enhance their activity, affecting their function.
inhibitors
In the context of a scientific experiment, inhibitors are substances that reduce or prevent the activity of enzymes or other biochemical processes. Without specific details about the mixture in D, it's difficult to identify the exact substances that acted as inhibitors. Typically, common inhibitors can include certain chemicals like competitive inhibitors, non-competitive inhibitors, or specific ions that bind to enzymes and alter their function. If you can provide more context or details about the mixture, I could give a more precise answer.
Enzymes are highly sensitive to changes in temperature and pH. They also can be affected by the presence of specific cofactors or inhibitors that can modulate their activity. Additionally, the substrate concentration can impact the rate at which enzymes function.
Competitive inhibitors bind to the active site of enzymes, blocking the substrate from binding and inhibiting the enzyme's activity.
Enzymes can malfunction due to changes in temperature and pH levels, which can alter their structure and function. Additionally, the presence of inhibitors, which are substances that bind to enzymes and reduce their activity, can also disrupt enzyme function. These factors can lead to decreased reaction rates and impaired biological processes.
Anti enzymes or enzyme inhibitors, are substances which inhibit counteracts the action of an enzyme.
inhibitors
Often enzymes require a cofactor in order for them to function as a catalyst
They're catalysts like enzimes, but they're not actually enzymes, which are proteic.
No, uncompetitive inhibitors do not bind to the active site of enzymes. They bind to a different site on the enzyme, causing a conformational change that prevents the substrate from binding to the active site.