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Why do allosteric enzymes have two types of binding sites?
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19. Enzymes
Enzyme Regulation: Allosteric Control
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Isoleucine can attach to the enzyme threonine deaminase and can decrease its activity. Isoleucine can be classified as:
A
Positive allosteric regulator
B
Negative allosteric regulator
Guida verificata passo dopo passo1
Understand the role of allosteric regulators: Allosteric regulators are molecules that bind to an enzyme at a site other than the active site, causing a change in the enzyme's activity.
Differentiate between positive and negative allosteric regulators: Positive allosteric regulators increase enzyme activity, while negative allosteric regulators decrease enzyme activity.
Identify the effect of isoleucine on threonine deaminase: The problem states that isoleucine decreases the activity of threonine deaminase.
Classify isoleucine based on its effect: Since isoleucine decreases the enzyme's activity, it acts as a negative allosteric regulator.
Conclude the classification: Isoleucine is a negative allosteric regulator because it binds to threonine deaminase and decreases its activity.
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