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What properties of enzymes give rise to their ability to distinguish one substrates from another?
Enzymes have specific active sites that can only bind to complementary substrates, based on size, shape, and chemical properties. The binding of substrates to the active site induces a conformational change in the enzyme that stabilizes the transition state for the reaction with that particular substrate. Additionally, enzymes may undergo induced fit where the active site reshapes to better accommodate the specific substrate.
What is it about enzymes that determines which reaction they catalyse?
Enzymatic reactions depend on the concentration of the substrate. Once all active sites become filled, the output of product obviously depends on something else. This could be the pH of the solution, the temperature of the solution, or many other factors. Usually, higher temperature means high kinetic energy (motion) of molecules and faster reaction times. However, too hot of a temperature can denature the enzymes active site. Also, different enzymes work more or less efficiently in different pH levels. Also, the overall affinity for the substrate by the enzyme influences the rate. Inhibitors can also affect rates.
Why is the shape of H2O2 important to the enzyme catalase?
it is important because the shape of h2o2 must be complementary to the shape of the active site of the calase enzyme. Enzyme substarate complex can be formed and enzyme product complex can then be formed. If h202 shape was not complementary of the shape of the active site of catalase h202 could not be broken down into water and oxygen. Without the enzyme present it would take days for the h202 to break down. It would eventually break but it would take a long time. So the shape is important because without h202 would not be able to bind with the active site.
What do acids and bases do to enzymes?
Acids and bases can denature enzymes by disrupting their shape and changing the active site where substrates bind. This alteration can prevent enzymes from catalyzing reactions effectively. pH changes can also affect the ionization of amino acid side chains, influencing enzyme activity.
What happens during allosteric inhibition?
Allosteric (noncompetitive) inhibition results from a change in the shape of the active site when an inhibitor binds to an allosteric site. When this occurs the substrate cannot bind to its active site due to the fact that the active site has changed shape and the substrate no longer fits. Allosteric activation results when the binding of an activator molecule to an allosteric site causes a change in the active site that makes it capable of binding substrate.
Does the shape of an enzyme protein determine specificity?
Shape of an enzyme specifically shape of its active site determines enzyme specificity .
What characteristics of enzymes makes them specific for substrate?
shape of their active site make them specific for the substrates
How the genetic codes affects an enzyme function?
The gene sequence determines the codon, which in turn determines the aminoacid, which in turn determines the tridimensional shape on the protein, which in turn determines the shape of the active site, which in turn determines what it'll be catalysing.
How does an enzymes active site relate to its substrate?
An enzyme's active site is where the substrate binds and undergoes a chemical reaction. The active site has a specific shape that complements the substrate's shape, allowing for a precise fit. This interaction facilitates the enzyme to catalyze the chemical reaction efficiently.
Substrate molecules bind to enzymes where?
The bind in the active site.
Why must a molecule have a specific shape if it is to be a substrate of an enzyme?
Active sites of enzymes (where the substrates fit in) are substrate specific, and are complementary to the shape of the molecule (substrate). In this way, enzymes can only act on a specific substrate, since that is the only shape that it will accommodate in the active site.
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 enzymes have an attachment site called the active site for what to join?
Active site.
What is the attachment site of enzymes called?
Active site.
Does the active site of an enzyme have a shape that is specfic for its given substrate?
Yes all enzymes have an active site where substance are temporarily bound. All enzymes have shape that may change during catalysis. The active site of an enzyme orients its substrate molecules, thereby promoting interaction of their reactive parts.
How does an enzymes active site relate to it's substrate?
The substrate binds to the active site.
Do uncompetitive inhibitors bind to the active site of enzymes?
No, uncompetitive inhibitors do not bind to the active site of enzymes. They bind to a different site on the enzyme, causing a conformational change that prevents the substrate from binding to the active site.
