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Is the inhibition produced by lead is noncompetitive?
Yes, lead is known to inhibit enzymes through noncompetitive inhibition, where the inhibitor binds to a site on the enzyme other than the active site, altering the enzyme's structure and reducing its activity. This type of inhibition does not compete with the substrate for binding to the enzyme.
Why does adding additional substrate overcome competitive but not noncompetitive inhibition?
Adding additional substrate can overcome competitive inhibition because the inhibitor and substrate compete for the active site on the enzyme, so increasing substrate concentration can outcompete the inhibitor. However, in noncompetitive inhibition, the inhibitor binds to a site other than the active site, so adding more substrate cannot overcome this inhibition as the inhibitor is not competing for the same binding site as the substrate.
What are the difference of competitive and non competitive inhibition...want the answer in term Km and Vmax?
In competitive inhibition, the inhibitor competes with the substrate for the active site of the enzyme, increasing Km (substrate concentration needed for half maximal velocity) but not affecting Vmax (maximum velocity of the reaction). In non-competitive inhibition, the inhibitor binds to a site other than the active site, reducing the enzyme's activity by lowering Vmax without affecting Km.
What end product from a metabolic pathway binds to an enzyme involved in a reaction at the beginning of the pathway. changing the shape of the active site and preventing the enzyme from?
The end product of a metabolic pathway can bind to the enzyme involved in the beginning of the pathway, acting as an inhibitor. This typically changes the shape of the enzyme's active site, preventing the enzyme from binding to its substrate and carrying out the reaction. This regulatory mechanism is known as feedback inhibition.
What are the two different types of inhibition?
Increasing the temperature excessively - if an enzyme is heated too much (usually around 40°C) the enzyme will become denatured. This will prevent it from working permanently. Decreasing the temperature - decreases enzyme activity Enzyme inhibitors - heavy metals poison enzymes by binding to the active site, preventing the enzyme from binding to the substrate molecule.
When was Retro Active created?
Retro Active was created in 1984.
When was Retro-active created?
Retro-active was created in 2005.
How is competitive inhibition different from competitive inhibition?
Competitive Inhibition is a substance that binds to the active site in place of the substance while Non-competitive Inhibition is a substance that binds to a location remote from the active site. (:
How is competitive inhibition different from non competitive inhibition?
Competitive inhibition involves a molecule binding to the active site of an enzyme, directly competing with the substrate. In non-competitive inhibition, the inhibitor binds to a site on the enzyme other than the active site, altering the enzyme's shape and preventing the substrate from binding.
What inhibitor binds into the active site of an enzyme not allowing the subrtate to bind?
This would be a competitive inhibitor. It can be a structural analog of the substrate. This type of inhibition can be out competed by adding more substrate. A competitive inhibitor increases the Km of the enzyme.
What are the two types of Feedback Inhibition?
The two types of feedback inhibition are competitive inhibition and non-competitive inhibition. In competitive inhibition, the inhibitor binds to the active site of the enzyme, competing with the substrate for binding. In contrast, non-competitive inhibition occurs when the inhibitor binds to a site other than the active site, causing a conformational change in the enzyme that inhibits its activity.
What are the types of feedback inhibition?
There are two main types of feedback inhibition: competitive inhibition, where an inhibitor competes with the substrate for the active site of an enzyme; and non-competitive inhibition, where an inhibitor binds to a site on the enzyme other than the active site, altering the enzyme's shape and reducing its activity.
Is the inhibition produced by lead is noncompetitive?
Yes, lead is known to inhibit enzymes through noncompetitive inhibition, where the inhibitor binds to a site on the enzyme other than the active site, altering the enzyme's structure and reducing its activity. This type of inhibition does not compete with the substrate for binding to the enzyme.
How active is the frontal and temporal lobe during sleep?
Frontal lobes are not very active during sleep; that is where the inhibition function lies. This is why (in your dreams) you do not make wise decisions.
What is retro activation of enzymes?
Retro activation of enzymes refers to the inhibition of an enzyme by one of its products, which then reduces the enzyme's activity. This negative feedback mechanism helps regulate metabolic pathways by slowing down the production of certain molecules when they reach a certain concentration. It is a form of enzyme regulation that helps maintain cellular homeostasis.
Why does adding additional substrate overcome competitive but not noncompetitive inhibition?
Adding additional substrate can overcome competitive inhibition because the inhibitor and substrate compete for the active site on the enzyme, so increasing substrate concentration can outcompete the inhibitor. However, in noncompetitive inhibition, the inhibitor binds to a site other than the active site, so adding more substrate cannot overcome this inhibition as the inhibitor is not competing for the same binding site as the substrate.
What are some differences and or similarities in the type of inhibition caused by heat acid or base and heavy metal ions on enzyme activity?
Heat, acid, and base can denature enzymes by disrupting their structure, leading to reversible inhibition. Heavy metal ions can bind to specific amino acid residues on enzyme active sites, causing irreversible inhibition. Both types of inhibition can decrease enzyme activity, although heavy metal ions typically have longer-lasting effects due to the irreversible nature of their inhibition.
