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What are ACE inhibitors also called?
They are also called Angiotensin-converting enzyme inhibitors
What are AADC inhibitors also called?
They are also called DC inhibitors
What are DC inhibitors also called?
They are also called DC inhibitors
What blocks enzyme activity by binding to the active site of an enzyme?
Competitive inhibitors reduce enzyme activity by binding (in competition with the enzyme's substrate) to the active site. These inhibitors may be reversible or irreversible. With reversible inhibitors, which may release the enzyme, concentrations much higher than the concentration of the substrate would be required to completely block enzyme activity, and even then one or two reactions may take place over long periods of time. With irreversible inhibitors, which permanently attach to the enzyme, enzyme activity could be completely blocked when the amount of inhibitor matches the amount of enzyme. Competitive inhibition reduces the enzymes ability to bind substrate (so it lowers the KM) but does not alter the maximum rate (very high substrate concentrations would out compete for enzyme binding).Other types of inhibitors work in other ways. Non-competitive inhibitors bind to the enzyme on a site other than the active site. These too may be reversible or irreversible. Binding does not compete with substrate, so concentrations to completely block enzyme activity do not have to be as high as reversible competitive inhibitors. Non-competitive inhibition reduces the apparent maximum rate for the enzyme.Uncompetitive inhibitors bind only when the substrate is also bound to the enzyme (they bind to the enzyme-substrate complex). Both the maximum rate and substrate binding affinities appear lower.
What can you do to regain the activity of the enzyme?
To regain the activity of an enzyme, you can try adjusting the pH and temperature to the optimal conditions for that specific enzyme. You can also remove any inhibitors that may be present, such as heavy metals or competitive inhibitors. Additionally, you can try adding cofactors or coenzymes that may be necessary for the enzyme to function properly.
What is angiotensin-converting enzyme also called?
Serum Angiotensin-Converting Enzyme
What is an enzyme that is also an antibiotic that kill disease-causing bacteria?
Lysozyme is an enzyme that acts as an antibiotic by breaking down the cell walls of bacteria, causing them to burst and die. It is found in tears, saliva, and other bodily fluids as part of the immune system's defense against bacterial infections.
What are all of the factors that affect enzyme activity except for temperature and pH?
There are a number of factors that can influence how efficiently a certain enzyme can catalyse a reaction: the amount of substrate present, whether there are chemicals present that inhibit enzymes by either binding to their active site or cofactor site, the amount of enzymes present...
What factors affect enzyme production?
Factors that affect enzyme production include the availability of substrate for the enzyme to act on, the pH and temperature of the environment, the presence of cofactors or coenzymes, and the regulation of gene expression through factors like inducers or inhibitors. Additionally, factors such as stress, nutrient availability, and feedback inhibition can also influence enzyme production.
What reduces the activity of an enzyme?
In vitro, Temperature, pH and other factors leading to degradation or suboptimal activity affect enzymatic activity. All enzymes are not created equal, each enzyme functions its best at different optimal conditions.
What are three that ways to control enzymes?
Temperature: Enzyme activity can be controlled by adjusting the temperature, as most enzymes have an optimal temperature at which they function best. pH: Enzyme activity is also influenced by the pH of the environment, and maintaining an appropriate pH level can help regulate enzyme function. Inhibitors: Enzyme activity can be inhibited by specific molecules that bind to the enzyme and prevent it from carrying out its catalytic function. This can be used as a way to control enzyme activity in biological systems.
What factors can affect the turnover number in metabolism?
The turnover number in metabolism, which reflects the efficiency of enzyme-catalyzed reactions, can be influenced by several factors. These include substrate concentration, enzyme concentration, temperature, and pH, as each can affect enzyme activity and stability. Additionally, the presence of inhibitors or activators can modify the enzyme's efficiency, thereby impacting the turnover number. Lastly, the intrinsic properties of the enzyme, such as its structure and affinity for the substrate, also play a significant role.
