Enzyme inhibitors

• so the non-competitive inhibitor binds into the allosteric site and it changes the shape of the enzyme causing it to no longer be complementary with the substrate and this inhibits the reaction from happening.
• Enzymes can be activated by various different cofactors which are important molecules that bind to the enzyme and help its function.
• Enzymes can also be deactivated by molecules known as inhibitors which reduce or stop a reaction from happening.
• Inhibitors are any molecules which reduce or stop a reaction from happening, acting as a blockade.
• If a small concentration of an inhibitor is added to an enzyme solution, it reduces the rate of reaction quite significantly.
• If an inhibitor is added in excess, the reaction drops down to zero and stops.
• Competitive inhibitors compete with the substrate for the enzyme's active site, making a physical barrier or block preventing the formation of the enzyme substrate complexes.
• Competitive inhibitors bind at the same site as the substrate and inhibit reactions, while non-competitive inhibitors bind at different sites and create chemical changes.
• Chemical changes have altered the active site to a point where the substrate can't properly fit, inhibiting the reaction.
• Non-competitive inhibitors bind at different sites and inhibit reactions in a different way than competitive inhibitors.
• End product inhibition is a type of inhibition where a cell only wants a certain amount of molecule being produced, and when a cell is doing a reaction, it only wants to produce the right amount of any chemical.
• Non-competitive inhibitors are very powerful and can inhibit something very strongly.
• If a substrate concentration is increased, the rate of reaction increases, but if an inhibitor is present, the rate of reaction does not increase, indicating that the inhibitor is non-competitive.
• Enzymes can work together to complete metabolic processes, for example, the product of one reaction can be the substrate for the next reaction.
• Non-competitive inhibitors bind permanently to their allosteric site, while competitive inhibitors bind reversibly and the inhibition is quite weak.
• Non-competitive inhibitors bind to a different part of the enzyme, known as the allosteric site, causing a conformational change in the enzyme and inhibiting the reaction from happening.
• Over time, the concentration of the product oscillates between being too high and too low but overall stays at a normal level.
• If the inhibitor is non-competitive, it binds to an allosteric site and the last product in the pathway is called end product inhibition.
• The inhibition decreases because it's no longer able to carry out this end product inhibition.
• The last product in the pathway can act as an inhibitor to stop itself from being made.
• The product itself goes and acts back on the first stage enzyme and inhibits it from doing that first step non-competitively, stopping the cell from going too far.
• The concentration of a product stays roughly constant through time.
• Greater inhibition will lead to a decrease in the amount of the end product being made.
• The concentration of the product initially keeps going up and then at a certain point it starts causing end product inhibition.
• As the product inhibits itself from being made, it comes back down and the concentration remains a normal level.
• As the concentration of the end product keeps going down, the inhibition decreases because it's no longer able to carry out this end product inhibition.
• If the concentration of the product ever drops too low, it will cause end product inhibition and the inhibition stops because it's no longer able to inhibit itself.
• ATP may end up starving the cell of energy, so any chemical that is made in an enzyme-controlled reaction needs to be controlled and they only want a certain amount of this chemical.
• One of the products can be used as an inhibitor in another enzyme in the pathway.
• The enzyme will become reactivated again and it can carry out the stages again and start making it.
• If the concentration of the final product starts getting high, it can create more inhibition on those other enzymes.
• The concentration of the product goes back up again when the inhibition stops.