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When the active site of an enzyme is continuously filled and the maximum enzyme rate has been reached what happens if more substrates are added to the reaction?
If the active site of an enzyme is continuously filled and the maximum enzyme rate has been reached, adding more substrates will not increase the rate of the reaction. This is because all available enzyme active sites are already saturated with substrates, so increasing substrate concentration will not result in more enzyme-substrate complexes being formed.
What happens to an enzyme after it catalyzes a chemical reaction?
Enzymes are not used up in a chemical reaction. Usually, the enzyme will "reset" and be ready to use in another reaction. This is due to the fact that enzymes are proteins, and their shape is what they use in a chemical reaction. Initially, the enzyme has a particular shape. Something happens to the enzyme (usually a shape change, called a conformation change, brought on by the presence of two or more chemical reactants), and the enzyme catalyzes the reaction. After the reaction is catalyzed, the product is released, and the enzyme can "relax." This means it goes back to its normal shape, ready to do it all over again.
What happens to an enzyme after a biochemical reaction?
After a biochemical reaction, the enzyme remains unchanged and is free to catalyze more reactions. Enzymes are not consumed in the reaction and can be used repeatedly, making them efficient catalysts.
Does vmax increase with increasing amount of enzyme?
No, Vmax remains constant regardless of the amount of enzyme present. Vmax represents the maximum rate of reaction that can be achieved when all enzyme active sites are saturated with substrate. Once all enzyme active sites are filled, increasing the enzyme concentration further will not increase the reaction rate.
What happens when an enzyme is denatured?
When an enzyme is denatured the active site which allows it to catalyze reactions is destroyed, rendering the enzyme useless. This process is irreversible but the remains are recycled to form new enzymes.
What happens to the rate of enzyme concentration when you increase substrate concentration?
The rate of enzyme reaction is increased when the substrate concentration is also increased. However, when it reaches the maximum velocity of reaction, the reaction rate remains constant.
What happens to the enzymes after the substrate reacts?
It is either used again (many enzymes are used multiple times before broken down) or is broken down.
What name do we give the joined enzyme and substrate that remains together until the reaction is over?
The joined enzyme and substrate are referred to as the enzyme-substrate complex. This complex forms when the substrate binds to the active site of the enzyme, and it remains intact until the enzymatic reaction occurs, resulting in the formation of products. The enzyme itself is then free to catalyze additional reactions.
What happens if the substrate doesn't fit the enzyme?
If the substrate doesn't fit the enzyme, the enzyme-substrate complex cannot form, preventing the biochemical reaction from occurring. This misfit may result from changes in the enzyme's shape or the substrate's structure, which can be influenced by factors like pH, temperature, or mutations. Without a proper fit, the enzyme's active site remains unoccupied, and the reaction cannot proceed, affecting the overall metabolic pathway. Ultimately, this can disrupt cellular functions and biological processes.
What happens to an amylase after it has been used?
After amylase has catalyzed the breakdown of starch into sugars, it remains unchanged and can be reused. Enzymes like amylase do not get consumed in the reaction; instead, they facilitate the reaction and return to their original state. This allows them to act on additional substrate molecules repeatedly. However, factors such as temperature, pH, and substrate concentration can affect the enzyme's activity over time.
What happens when increasing the substrate concentration when there is less substrate than enzyme?
Dunno. But this is pretty cool. But if i search the question, i obvioudly don't know it, so why would i be given an optionto answer it?
What is residual substrate?
Residual substrate refers to any material leftover or remaining after a chemical reaction or process has taken place. In the context of biotechnology or enzymatic reactions, residual substrate may refer to the unutilized or partially degraded substrate that remains in the system after the reaction is complete. Understanding and managing residual substrates is important in optimizing reactions and maximizing product yields.
What is produced at the end enzyme catalyzed reaction?
At the end of an enzyme-catalyzed reaction, the substrate is converted into one or more products. The enzyme facilitates this transformation by lowering the activation energy required for the reaction to proceed. Once the reaction is complete, the enzyme remains unchanged and can catalyze additional reactions with new substrate molecules. Thus, the enzyme acts as a reusable catalyst throughout the reaction process.
What is where the enzyme and the substrate come together at the active site?
The active site of an enzyme is a specific region where the enzyme binds to its substrate, forming an enzyme-substrate complex. This site is typically complementary in shape, charge, and polarity to the substrate, allowing for precise binding. The interaction at the active site facilitates the chemical reaction, lowering the activation energy required for the reaction to occur. Ultimately, this process leads to the transformation of the substrate into the product while the enzyme remains unchanged and can be reused.
What happens to an enzyme after a biochemical reaction?
After a biochemical reaction, an enzyme typically remains unchanged and can be reused in other reactions.
What are the General steps in enzyme catalyzed reaction?
In an enzyme-catalyzed reaction, the general steps include: substrate binding to the active site of the enzyme, forming an enzyme-substrate complex. This complex undergoes a reaction, leading to the formation of products. Finally, the products are released from the enzyme, which remains unchanged and can continue catalyzing more reactions. The enzyme facilitates the reaction by lowering the activation energy required for the reaction to occur, increasing the reaction rate.
How does a competitive inhibitors work?
Competitive inhibitors work by binding to the active site of an enzyme, competing with the substrate for that site. This binding prevents the substrate from attaching, thereby reducing the rate of the enzyme-catalyzed reaction. The effect of a competitive inhibitor can be overcome by increasing the concentration of the substrate, which can outcompete the inhibitor for binding to the enzyme. As a result, the maximum reaction velocity (Vmax) remains the same, but the apparent affinity of the enzyme for the substrate (reflected in the Km value) is decreased.
