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What are the molecules that enzymes act on called?
The molecule upon which an enzyme acts is called the substrate.
What is better more substrates or more enzymes?
It depends on the specific reaction and conditions. Increasing the amount of substrate can increase the rate of reaction up to a certain point, but adding more enzymes can also enhance reaction rates by increasing the chance of substrate-enzyme collisions. Overall, the optimal balance of substrates and enzymes is critical for maximizing reaction efficiency.
Does a substrate molecule need and enzyme molecule?
Yes, a substrate molecule typically needs an enzyme molecule to catalyze a specific chemical reaction. Enzymes help by lowering the activation energy required for the reaction to occur, making it more efficient. Without enzymes, many biological reactions would proceed too slowly to sustain life.
How enzyme structure makes an enzyme very specific?
Enzymes are proteins, which are made up of amino acids. Each enzyme has a different sequence of amino acids and changing even one amino acid will mean that the tertiary structure of the enzyme will be lost and so will it's active site. As enzymes are substrate specific, only a certain substrate will bind to its active site, due to its amino acid sequence determining the shape of the active site.
What happens if the enzyme concentration is low?
If the enzyme concentration is low, the rate of the enzymatic reaction will be slower because there are fewer enzymes available to catalyze the reaction. This can lead to a longer time required for the reaction to reach completion or for the substrate to be converted into the product. Additionally, the enzyme-substrate complex formation may be less frequent, resulting in lower overall reaction efficiency.
What are the molecules that enzymes act on called?
The molecule upon which an enzyme acts is called the substrate.
What is better more substrates or more enzymes?
It depends on the specific reaction and conditions. Increasing the amount of substrate can increase the rate of reaction up to a certain point, but adding more enzymes can also enhance reaction rates by increasing the chance of substrate-enzyme collisions. Overall, the optimal balance of substrates and enzymes is critical for maximizing reaction efficiency.
Does a substrate molecule need and enzyme molecule?
Yes, a substrate molecule typically needs an enzyme molecule to catalyze a specific chemical reaction. Enzymes help by lowering the activation energy required for the reaction to occur, making it more efficient. Without enzymes, many biological reactions would proceed too slowly to sustain life.
What happens when you halved the amount of enzymes in a reaction?
It would take a longer amount of time for the substrate to be fully broken down into its final products.
How enzyme structure makes an enzyme very specific?
Enzymes are proteins, which are made up of amino acids. Each enzyme has a different sequence of amino acids and changing even one amino acid will mean that the tertiary structure of the enzyme will be lost and so will it's active site. As enzymes are substrate specific, only a certain substrate will bind to its active site, due to its amino acid sequence determining the shape of the active site.
What is The function of enzymes in plants?
Enzymes in plants are involved in various biochemical reactions that are essential for plant growth, development, and response to environmental stimuli. They act as catalysts to accelerate these reactions, such as photosynthesis, respiration, and synthesis of essential molecules like proteins and hormones. Enzymes play a crucial role in regulating plant metabolism and overall physiological functions.
What happens if the enzyme concentration is low?
If the enzyme concentration is low, the rate of the enzymatic reaction will be slower because there are fewer enzymes available to catalyze the reaction. This can lead to a longer time required for the reaction to reach completion or for the substrate to be converted into the product. Additionally, the enzyme-substrate complex formation may be less frequent, resulting in lower overall reaction efficiency.
How do inhibitors regulate enzymes?
Competitive inhibition: Where an inhibitor, which has a similar molecular shape to the enzyme's substrate, competes with substrate to fit to the enzymes active site. In the end all substrate can be broken down because the competitive inhibitors are not permanently bonded to the enzymes active site. If there is a higher concentration of substrate the amount of time it will take for all the substrate to be broken down will be less than if there is a higher concentration of inhibitor. Non-competitive inhibition: Where the inhibitor attaches itself to the enzyme at a site which is NOT the active site. This causes the enzymes shape to be changed slightly which would mean that the substrate is unable to fit to the active site. Non-competitive inhibitors do no compete with the substrate for the active site, hence their name. Non-competitive inhibitors may be permanent or not. Because the inhibitor and substrate are not competing for the same site an incrase in substrate concentration does not decrease the inhibitors effect.
How are substrates like keys and enzymes like locks?
Substrates are molecules that fit into the active site of an enzyme, much like a key fits into a lock. The active site of the enzyme has a specific shape that only allows substrates with a complementary shape to bind, similar to how a lock only opens with the correct key. This specificity ensures that enzymes only catalyze specific reactions with specific substrates.
What do most enzymes end in?
Some thing then ase. So if the substrate was called B the enzyme would B+ase, Base. Or substrate Z, the enzyme would be Z+ase, Zase. Some examples, amylase, maltase, catalase, sucrase. That is the most common naming, but it is not ALWAYS the case.
Describe the chemical compositions and configuration of enzymes and discuss the factors that modify enzymes structure and function?
Enzymes are composed of amino acids, and have different bonds such as a hydrogen bond which maintains the enzyme's shape. Factors such as temperature and pH have an effect upon the enzymes structure. Enzymes have slower rates of reaction when the temperature is below the enzymes optimum temperature. This is due to the fact that hydrogen bonds are stronger at lower temperatures meaning that the enzyme is less flexible and so, using the induced fit theory, this means that the substrate is less able to fit into the enzymes active site meaning less substrate is broken down therefore the rate of reaction is much less than it would be at the enzymes optimum temperature. When the temperature also exceeds the enzymes optimum temperature the rate of reaction is again slower that it would be at the optimum temperature, this is due to the high temperature causing the hydrogen bonds to be broken, meaning the enzyme can be denatured, and there is a point where the enzymes are unable to "renature" (when temp is returned to optimum) because too many hydrogen bonds would have been broken. pH is a factor which also affects the enzymes structure, by changing the pH from the enzymes optimum pH you are then causing there to be a change in the enzymes structure and molecular shape. pH can in turn strengthen or weaken the intermolecular forces like the hydrogen bonds. Competitive inhibitors can also alter the enzymes function. Competitive inhibitors have a molecular shape which is similar to the shape of the substrate; This means that they can occupy the enzymes active site meaning that they compete with the substrate for an available active site. The difference between the concentration of the competitive inhibitor and the substrate determines the effect upon the enzyme activity, if the competitive inhibitors concentration is highest the effect of the substrate is lessened. The inhibitor is not permenantly bound to the enzymes active site, so when it leaves another molecule may take its place, either another inhibitor or substrate. Sooner or later all of the substrate will occupy active sites of enzymes, but if the inhibitor concentration is higher this may take some time. Non-competitive inhibitors can also effect the enzyme activity by attaching themselves to the enzyme, but not at the active site. This attachment means the enzyme's active site may under-go a shape change meaning that the substrate may not fit into it, causing the effect of the enzyme to be lowered as less substrate can be broken down. Non-competitive inhibitors may be permanent. Hope this helps you, even if it is very slightly.
The presence of in the circulatory system would be considered abnormal?
Kreb's cycle enzymes
