0
What affect does too much substrate have on the rate of an enzyme reaction?
Wiki User
∙ 11y ago
The enzyme becomes saturated by the substrate and enzyme activity plateaus.
Wiki User
∙ 11y ago
Add your answer:
Earn +20 pts
What conditions affects the function of enzymes?
The activity of an enzyme is affected by temperature, pH and the concentration of the substrate.
Enzymes are affected by?
There are several factors that affect enzyme itself. 1. Temperature As the shape specificity of the enzyme's active site is vital for any enzyme reaction, therefore an optimal temperature is important for enzymes. Enzymes will be inactive under low temperatures since it has too low kinetic energy to start the reaction or quickens the reaction. Alternatively, enzyme's structure and the shape of active site will changed in high temperature. Eventually, enzymes are denature and never can be used again. 2. pH value As mentioned, the structure of enzyme is highly sensitive to the external environment, therefore pH value of the environment also has an effect on enzymes. Again, the shape of enzymes changed outside the range of pH value that suits particular enzymes. For instance, the optimum pH value for enzymes in stomach is around pH 2 whereas most are pH 7. 3. Presence of inhibitor There are 2 types of inhibitor, one is non-competition inhibitor. These inhibitors will bind to the allosteric site (alternative site) of the enzymes that alters the shape of active site, therefore preventing the substrate from binding the enzymes and having reactions.
Why do enzymes only work with the specific substrates?
Enzymes act only on a specific substrate due to the active site of the enzymes fits perfectly with the substrate. Like 2 puzzle pieces, they can only go together and not with anything else. Enzymes catalyze or help a reaction take place. They bind substrates and then help position them in order that the chemical reaction between these substrates can take place. If they bound things other than the substrates they would be much less efficient in catalyzing the reactions.
How enzyme catalyze chemical reaction?
Enzymes lower the activation energy of a reaction (that is, the amount of energy that is needed in order for the reaction to occur).Without an enzyme, a reaction may need so much energy that it is impossible to obtain in a normal biological timespan. With enzymes, reactions require much less energy, so that they can occur hundreds of times a second.Enzymes can achieve this catalysis in many ways - for instance, if a reaction involves two substances combining to form one, the enzyme can bind each substance in a specific site that forces them close together, making the reaction much more likely to occur and requiring much less energy for the substrates to locate and approach one another.
Can the enzyme be reused or is it destroyed in the reaction?
Yes. Enzymes are pretty much known as catalysts, and the definition of a catalyst is "a substance that increases the rate of a chemical reaction, without being consumed or produced by the reaction." So thus we see the enzyme being active in a reaction but not destroyed. There are exceptions to this, though. If an enzyme is kept in hot, unfavorable temperatures, it will change shape or become "denatured" and may become useless in a very short time.
What fits with an enzyme to make a reaction occur?
The substrate fits into the enzyme, much the way a key fits in a lock. Sometimes there are other "modulators" that also fit in the enzyme.
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?
How does a enzyme increase the rates of reactions?
An enzyme increases the rate of the reaction by lowering the activation energy needed for the reaction. The secret is that enzymes weaken the bonds in the substrate so that products are formed much faster. Enzymes are catalysts or substances that speed up the reaction (without being consumed in it). An enzyme increases the rate of reaction by lowering the energy of activation or (Ea). Enzymes achieve that by attaching to the substrate in the active site and forming an enzyme substrate complex in which the enzyme disturbs the covalent bond of the substrate. This causes it to enter the transitional state, which is the most energetic and unstable state. The enzyme then breaks apart, and the substrate goes into an exorganic reaction to form the product.
What determines an enzyme's function and how many unctions does one enzyme have?
The arrangement of it's active site. Some enzymes just provide a place where two reactants can be in a protected environment for the reaction, some enzymes stress bonds of reactant to lower the reaction activation energy and some enzymes have catalytic properties due to the arrangement of the various amino acid R groups in their active site. One enzyme, one substrate(s) and one function. So, many different classes of enzymes. Very much so
How do enzyme activators affect enzymes?
Enzymes speed up chemical reactions by lowering the activation energy. The activation energy is the amount of energy needed to start a reaction and if this is lowered the reaction can occur more rapidly.
What is better more substrates or more enzymes?
Depends on how much substrate the enzyme can process. Most enzymes can process more than one molecule of substrate without denaturing or becoming unusable. However, in the terms of your question. More substrate is better. Too many enzymes would mean the reaction would be cut short, because they would all react the substrate at once. So for a prolonged, efficient reaction more substrate would be proper.
What conditions affects the function of enzymes?
The activity of an enzyme is affected by temperature, pH and the concentration of the substrate.
What happens to the rate of enzyme reaction when you increase the enzyme concentration?
As the enzyme concentration increases, the rate of reaction will increase because there are many more enzymes present to aid break down the substrate. However, a point will be reached when no matter how much enzyme is present, the reaction will not occur any quicker. This is equilibrium. This happens because all the substrate is being broken down by the exact same amount of enzyme, so enzymes will be present which have no substrate to break down.
What are two ways you can increase the rate of a chemical reaction?
The most effective way to increase the rate of reaction is to increase the temperature. This is effective up to a certain temperature (depending on the specific reaction and enzyme). Above that point the reaction may slow down (drastically) or stop entirely. Note that enzymes speed up a chemical reaction by physically binding with a substrate (or substrates) and causing the appropriate change (breaking apart a large molecule into two or more pieces, combining two substrates into one molecule, etc.) A substrate is a material (chemical, element, compound, whatever) that is undergoing a reaction. It is changed by the reaction. If the materials that are reacting are heated past an enzyme's tolerance, the enzyme undergoes what is known as "denaturation." This means that the molecule physically alters, losing the specific shape that allows it to function as an enzyme. As a reminder, heat is defined as random kinetic energy. That is, heat causes atoms, molecules, proteins, etc. to move around in a random fashion. Heat can speed up a reaction because it moves around the substrate and enzyme molecules faster, allowing them to "bump into" each other more often. By the same token, this random movement will, if great enough, shake up a molecule so much that molecule falls apart or alters in some way. High heat denatures the molecule. Another technique is to increase the amount of substrate and/or enzyme. Increasing the substrate or enzyme increases the rate of reaction because the two materials will bump into each other more quickly and frequently.
Lock and key method?
In biology the lock and key method states that an enzyme and it's substrate are complementary and only the correct substrate can bind with the enzyme, this is due to the folding in the protein structure. However this theory is outdated and the inducted fit method is a much better representation.
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.
Enzymes are affected by?
There are several factors that affect enzyme itself. 1. Temperature As the shape specificity of the enzyme's active site is vital for any enzyme reaction, therefore an optimal temperature is important for enzymes. Enzymes will be inactive under low temperatures since it has too low kinetic energy to start the reaction or quickens the reaction. Alternatively, enzyme's structure and the shape of active site will changed in high temperature. Eventually, enzymes are denature and never can be used again. 2. pH value As mentioned, the structure of enzyme is highly sensitive to the external environment, therefore pH value of the environment also has an effect on enzymes. Again, the shape of enzymes changed outside the range of pH value that suits particular enzymes. For instance, the optimum pH value for enzymes in stomach is around pH 2 whereas most are pH 7. 3. Presence of inhibitor There are 2 types of inhibitor, one is non-competition inhibitor. These inhibitors will bind to the allosteric site (alternative site) of the enzymes that alters the shape of active site, therefore preventing the substrate from binding the enzymes and having reactions.
