Textbook Question
Why do allosteric enzymes have two types of binding sites?
19. Enzymes
Enzyme Regulation: Allosteric Control
Struggling with GOB Chemistry?
Join thousands of students who trust us to help them ace their exams!Watch the first videoMultiple Choice
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
Verified step by step guidance1
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.
2:57mWatch next
Master Allosteric Control Concept 1 with a bite sized video explanation from Jules
Start learningRelated Videos
Related Practice
Enzyme Regulation: Allosteric Control practice set
Problem sets built by lead tutorsExpert video explanations