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What is a substrate .?
A substrate molecule hydrogen bonds to the active site on an enzyme and causes it to distort. The distortion stresses a bond in the substrate, causing it to break into two product molecules. These are released by the enzyme and drift away.
What is enzyme cooperativity?
Enzyme cooperativity is a phenomenon where the binding of a substrate to one active site of a multi-subunit enzyme increases the affinity of the other active sites for the substrate. This results in a sigmoidal (S-shaped) saturation curve for enzyme kinetics, rather than the typical hyperbolic curve for non-cooperative enzymes. Cooperativity allows for more complex regulation of enzyme activity in response to changes in substrate concentration.
What are the two models that illustrate the binding of the substrate to the enzyme?
The two models are the lock-and-key model, where the substrate fits perfectly into the enzyme's active site like a key in a lock, and the induced fit model, where the active site of the enzyme changes its shape slightly to accommodate the substrate upon binding.
Competitive inhibitors and how they work?
Inhibitors are substances that alter the activity of enzymes by combining with them in a way that influence the binding of substrate and/or its turnover number. Many inhibitors are substances that structurally resemble their enzyme's substrate but either do not react or react very slowly compared to substrate.There are two kinds of inhibitors: a) competitive inhibitors (those compete directly with a normal substrate for an enzyme-binding site), and b) uncompetitive inhibitors (these bind directly to the enzyme-substrate complex but not to the free enzyme).
What are two factors that influence enzyme activity?
Concentration of the enzyme or it's substrate and the temperature.
What is a substrate .?
A substrate molecule hydrogen bonds to the active site on an enzyme and causes it to distort. The distortion stresses a bond in the substrate, causing it to break into two product molecules. These are released by the enzyme and drift away.
What is substrate is?
A substrate molecule hydrogen bonds to the active site on an enzyme and causes it to distort. The distortion stresses a bond in the substrate, causing it to break into two product molecules. These are released by the enzyme and drift away.
What type of enzyme brings reactants closer together?
A ligase enzyme catalyzes the joining of two molecules by forming a chemical bond. This enzyme brings reactants closer together to facilitate the formation of the bond.
What is the substrate of catalase?
Catalase acts on hydrogen peroxide, which is its substrate. It catalyzes the decomposition of hydrogen peroxide into water and oxygen.
What is cooperativity?
If an enzyme has two or more subunits, a substrate molecule causing induced fit in one subunit can trigger the same favorable conformational change in all the other subunits of the enzyme. Essentially, enzyme cooperativity is a mechanism of amplification regarding the response of enzymes to substrates: One substrate molecule primes an enzyme to accept additional substrate molecules more readily.
What is enzyme cooperativity?
Enzyme cooperativity is a phenomenon where the binding of a substrate to one active site of a multi-subunit enzyme increases the affinity of the other active sites for the substrate. This results in a sigmoidal (S-shaped) saturation curve for enzyme kinetics, rather than the typical hyperbolic curve for non-cooperative enzymes. Cooperativity allows for more complex regulation of enzyme activity in response to changes in substrate concentration.
What is the active site of an enzyme?
The active site of an enzyme is a region where the enzyme binds to its substrate and where the catalytic reaction takes place. It is typically a small, specific region of the enzyme that is complementary in shape and charge to the substrate. The active site is crucial for the enzyme's function in speeding up chemical reactions.
What is the function of substrate?
Maltase is an enzyme which works on the substrate maltose. Maltose is a sugar consisting of two glucose subunits.
How does an enzyme recognize its substrate?
An enzyme recognizes its substrate through a specific binding site that complements the shape and chemical properties of the substrate molecule. This interaction allows the enzyme to form a temporary enzyme-substrate complex, which lowers the activation energy required for the reaction to occur. The specificity of this interaction is critical for the enzyme to catalyze the reaction efficiently.
Competitive inhibitors and how they work?
Inhibitors are substances that alter the activity of enzymes by combining with them in a way that influence the binding of substrate and/or its turnover number. Many inhibitors are substances that structurally resemble their enzyme's substrate but either do not react or react very slowly compared to substrate.There are two kinds of inhibitors: a) competitive inhibitors (those compete directly with a normal substrate for an enzyme-binding site), and b) uncompetitive inhibitors (these bind directly to the enzyme-substrate complex but not to the free enzyme).
What are two factors that influence enzyme activity?
Concentration of the enzyme or it's substrate and the temperature.
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.
