enzymes situated at key steps in metabolic pathways are modulated by allosteric effectors
these effectors are usually produced elsewhere in the pathway
effectors may be feed-forward activators or feedback inhibitors
kinetics are sigmoid ("S-shaped")
Feedback inhibition, allosteric regulation, and covalent modification are all examples of regulatory mechanisms that control enzyme activity in living organisms. These mechanisms help maintain homeostasis and ensure that metabolic pathways are operating efficiently.
When an enzyme in a pathway is inhibited by the product of the reaction sequence, feedback inhibition occurs. The product molecule "feeds back" to stop the reaction sequence when the product is abundant.
Cells can control enzymatic activity through post-translational modifications such as phosphorylation, allosteric regulation, and feedback inhibition. They can also regulate enzyme synthesis and degradation, as well as by compartmentalizing enzymes in specific organelles or cellular locations.
An allosteric enzyme is one in which the activity of the enzyme can be controlled by the biniding of a molecule to the "allosteric site". This really just means somewhere other than the active site. Thus allosteric control of an enzyme can be classed in two ways. A positive allosteric modification is the binding of a molecule to the enzyme which increase the rate of reaction. Sort of like catalysing the catalysing effect of an enzyme. Obviously the opposite is true of negative allosteric modification. A good example for this is the activity of phosphofructokinase, which is promoted by a high AMP concentration, and inhibited by a high ATP concentration. This should make sense if you think about the action of a kinase etc.
Feedback inhibition is typically noncompetitive because the end product of a metabolic pathway binds to an allosteric site on the enzyme rather than the active site. This binding alters the enzyme's conformation, reducing its activity without directly competing with the substrate for the active site. As a result, the substrate can still bind, but the overall rate of the reaction decreases, allowing for fine-tuned regulation of metabolic pathways. This mechanism ensures that the pathway's activity is modulated based on the levels of the final product, preventing overproduction.
an accumulation of effectors slows the pathway.
In allosteric enzyme regulation, the regulator molecule binds to a site other than the active site, called the allosteric site. This binding alters the enzyme's activity by inducing a conformational change in the enzyme structure. This can either activate or inhibit the enzyme's function, depending on the nature of the allosteric regulator.
Feedback inhibition, allosteric regulation, and covalent modification are all examples of regulatory mechanisms that control enzyme activity in living organisms. These mechanisms help maintain homeostasis and ensure that metabolic pathways are operating efficiently.
When an enzyme in a pathway is inhibited by the product of the reaction sequence, feedback inhibition occurs. The product molecule "feeds back" to stop the reaction sequence when the product is abundant.
The process you are referring to is known as negative feedback regulation. In negative feedback regulation, the product of a system acts to decrease its own production or activity, maintaining a balance within the system. This helps to prevent excessive build-up of the product and maintain stability in the system.
Cells can control enzymatic activity through post-translational modifications such as phosphorylation, allosteric regulation, and feedback inhibition. They can also regulate enzyme synthesis and degradation, as well as by compartmentalizing enzymes in specific organelles or cellular locations.
An allosteric enzyme is one in which the activity of the enzyme can be controlled by the biniding of a molecule to the "allosteric site". This really just means somewhere other than the active site. Thus allosteric control of an enzyme can be classed in two ways. A positive allosteric modification is the binding of a molecule to the enzyme which increase the rate of reaction. Sort of like catalysing the catalysing effect of an enzyme. Obviously the opposite is true of negative allosteric modification. A good example for this is the activity of phosphofructokinase, which is promoted by a high AMP concentration, and inhibited by a high ATP concentration. This should make sense if you think about the action of a kinase etc.
Feedback inhibition is typically noncompetitive because the end product of a metabolic pathway binds to an allosteric site on the enzyme rather than the active site. This binding alters the enzyme's conformation, reducing its activity without directly competing with the substrate for the active site. As a result, the substrate can still bind, but the overall rate of the reaction decreases, allowing for fine-tuned regulation of metabolic pathways. This mechanism ensures that the pathway's activity is modulated based on the levels of the final product, preventing overproduction.
Feedback regulation of metabolic pathways involves the inhibition of an enzyme by the end product of the pathway. This helps maintain homeostasis by preventing the overproduction of metabolites. This process is important for ensuring that a cell or organism does not waste resources on unnecessary synthesis.
feedback inhibition. Feedback inhibition is a regulatory mechanism where the end product of a biosynthetic pathway inhibits the activity of the enzyme catalyzing the initial step, thereby regulating the overall rate of the pathway.
Feedback inhibition at the beginning of a metabolic pathway allows for rapid control of the pathway by regulating the initial enzyme activity, helping to prevent unnecessary accumulation of intermediates. This control mechanism is more efficient and direct compared to inhibiting enzymes in the middle of the pathway, which may lead to wasteful buildup of metabolites before regulation occurs.
feedback inhibition