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What else can I help you with?
What can prohibit enzymes from working in the body?
the various inhibitory molecules such as allosteric inhibitors, poisons, other ihhibitory molecules
Why allosteric enzymes do not obey michealis menten kinetics?
Allosteric enzymes do not obey Michaelis-Menten kinetics because their activity is regulated by the binding of effector molecules at sites other than the active site, leading to a conformational change in the enzyme. This results in a sigmoidal (S-shaped) reaction rate curve rather than the hyperbolic curve typical of Michaelis-Menten kinetics. Additionally, allosteric enzymes often exhibit cooperative binding, meaning the binding of substrate to one active site affects the binding properties of other sites, further deviating from the assumptions of Michaelis-Menten kinetics.
What statement is characteristic of allosteric effectors?
Allosteric effectors may not resemble the enzyme's substrates.
Why will increasing the substrate concentration not decrease the effect of a non competitive inhibitor?
Because you will still have the same number of enzymes inhibited. For example, you have 20 enzymes and 10 non-competitive inhibitors. Regardless of substrate concentration, at any one time, there will only be 10 enzymes available to accept a substrate. Increasing the substrate concentration does not affect this.
What is conjugated enzymes?
Conjugated enzymes are proteins that have a non-protein component attached to them, such as a metal ion or a coenzyme. This non-protein component is necessary for the enzyme to function properly and can help in catalyzing chemical reactions. Examples of conjugated enzymes include heme-containing enzymes like cytochrome c and flavoproteins like succinate dehydrogenase.
What is the difference between an allosteric enzyme and a non-allosteric enzyme?
An allosteric enzyme has multiple binding sites that can be used to modulate its activity through the binding of effectors or ligands, whereas a non-allosteric enzyme typically only has one active site. Allosteric enzymes can exhibit cooperativity, meaning that binding at one site affects binding at another site, while non-allosteric enzymes do not show this behavior.
What kind of regulation exist for enzymes?
Allosteric regulation and Reversaeble regulation :)
How do noncompetitive and allosteric inhibitors differ in their mechanisms of action on enzymes?
Noncompetitive inhibitors bind to a site on the enzyme that is not the active site, causing a change in the enzyme's shape and preventing substrate binding. Allosteric inhibitors bind to a different site on the enzyme, causing a conformational change that affects the active site's ability to bind substrate.
How does allosteric inhibition differ from competitive inhibition in terms of their mechanisms of action on enzymes?
Allosteric inhibition and competitive inhibition are two ways enzymes can be regulated. Allosteric inhibition occurs when a molecule binds to a site on the enzyme that is not the active site, causing a change in the enzyme's shape and reducing its activity. Competitive inhibition, on the other hand, occurs when a molecule binds to the active site of the enzyme, blocking the substrate from binding and inhibiting the enzyme's activity. In summary, allosteric inhibition affects enzyme activity by binding to a site other than the active site, while competitive inhibition affects enzyme activity by binding to the active site directly.
What functions do allosteric enzymes serve in reaction sequences?
Enzyme reaction rates can be decreased by various types of enzyme inhibitors. ... Enzymes serve a wide variety of functions inside living organisms
What can prohibit enzymes from working in the body?
the various inhibitory molecules such as allosteric inhibitors, poisons, other ihhibitory molecules
How do allosteric inhibition and noncompetitive inhibition differ in their mechanisms of action on enzymes?
Allosteric inhibition occurs when a molecule binds to a site on an enzyme that is not the active site, causing a change in the enzyme's shape and reducing its activity. Noncompetitive inhibition, on the other hand, involves a molecule binding to the enzyme at a site other than the active site, which does not change the enzyme's shape but still reduces its activity.
What are the 3 conditions required for enzymes to do their job properly?
temperature, pH, and allosteric inhibition (at least that's what I said on my bio essay)
How do cells regulate enzymes?
Cells regulate enzymes through various mechanisms such as allosteric regulation, post-translational modifications (e.g. phosphorylation, acetylation), and gene expression control. Allosteric regulation involves molecules binding to specific sites on enzymes to alter their activity. Post-translational modifications can activate or inhibit enzymes by changing their structure or function. Gene expression control involves regulating the amount of enzyme produced by the cell.
Allosteric enzymes are most effective when the substrate concentration is?
low, as they can exhibit cooperative binding of substrates and activators at low concentrations. At high substrate concentrations, the active site may become saturated, reducing the impact of allosteric regulation.
How can enzymes be regulated to optimize their activity and function?
Enzymes can be regulated to optimize their activity and function through various mechanisms such as allosteric regulation, competitive and non-competitive inhibition, post-translational modifications, and gene expression control. These regulatory processes help maintain enzyme activity at the right level for efficient biological processes.
Why allosteric enzymes do not obey michealis menten kinetics?
Allosteric enzymes do not obey Michaelis-Menten kinetics because their activity is regulated by the binding of effector molecules at sites other than the active site, leading to a conformational change in the enzyme. This results in a sigmoidal (S-shaped) reaction rate curve rather than the hyperbolic curve typical of Michaelis-Menten kinetics. Additionally, allosteric enzymes often exhibit cooperative binding, meaning the binding of substrate to one active site affects the binding properties of other sites, further deviating from the assumptions of Michaelis-Menten kinetics.
