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Biology IB HL - 8.1 Metabolism Part 2

Biology20 CardsCreated about 1 month ago

This flashcard deck covers key concepts of enzyme activity, including competitive and non-competitive inhibition, and examples of inhibitors in medicine and agriculture.

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How does the active site bind with the substrate? Do any changes need to occur?

When binding occurs, the active site undergoes a conformational change to optimally interact with the substrate (induced fit)
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Key Terms

Term
Definition
How does the active site bind with the substrate? Do any changes need to occur?
When binding occurs, the active site undergoes a conformational change to optimally interact with the substrate (induced fit)
What is the role of the conformational change of the active site?
This conformational change destabilises chemical bonds within the substrate, lowering the activation energy
What is the result of enzyme-substrate interaction?
As a consequence of enzyme interaction, the substrate is converted into product at an accelerated rate
What does competitive inhibition involve?
Competitive inhibition involves a molecule, other than the substrate, binding to the enzyme’s active site
What is the competitive inhibitor's relation to the active site?
The molecule (inhibitor) is structurally and chemically similar to the substrate (hence able to bind to the active site)
How does the competitive inhibitor inhibit enzyme activity?
The competitive inhibitor blocks the active site and thus prevents substrate binding
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Biology IB HL - 8.1 Metabolism Part 2
TermDefinition
How does the active site bind with the substrate? Do any changes need to occur?
When binding occurs, the active site undergoes a conformational change to optimally interact with the substrate (induced fit)
What is the role of the conformational change of the active site?
This conformational change destabilises chemical bonds within the substrate, lowering the activation energy
What is the result of enzyme-substrate interaction?
As a consequence of enzyme interaction, the substrate is converted into product at an accelerated rate
What does competitive inhibition involve?
Competitive inhibition involves a molecule, other than the substrate, binding to the enzyme’s active site
What is the competitive inhibitor's relation to the active site?
The molecule (inhibitor) is structurally and chemically similar to the substrate (hence able to bind to the active site)
How does the competitive inhibitor inhibit enzyme activity?
The competitive inhibitor blocks the active site and thus prevents substrate binding
How can the effects of a competitive inhibitor be reduced?
As the inhibitor is in competition with the substrate, its effects can be reduced by increasing substrate concentration
What does non-competitive inhibition involve?
Non-competitive inhibition involves a molecule binding to a site other than the active site (an allosteric site)
What does the binding of a non-competitive inhibitor cause? Where does it bind?
The binding of the inhibitor to the allosteric site causes a conformational change to the enzyme’s active site
How does a non-competitive inhibitor inhibit enzymatic activity?
As a result of this change, the active site and substrate no longer share specificity, meaning the substrate cannot bind
What can mitigate the effects of a non-competitve inhibitor?
NOTHING As the inhibitor is not in direct competition with the substrate, increasing substrate levels cannot mitigate the inhibitor’s effect
What are the (general) purposes of enzyme inhibition?
Enzyme inhibitors can serve a variety of purposes, including in medicine (to treat disease) and agriculture (as pesticides)
What is an example of a use of a competitive inhibitor?
An example of a use for a competitive inhibitor is in the treatment of influenza via the neuraminidase inhibitor, RelenzaTM
What is an example of a use of a non-competitive inhibitor?
An example of a use for a non-competitive inhibitor is in the use of cyanide as a poison (prevents aerobic respiration)
What is relenza?
Relenza is a synthetic drug designed by Australian scientists to treat individuals infected with the influenza virus
What is released from infected cells which is harmful?
Virions are released from infected cells when the viral enzyme neuraminidase cleaves a docking protein (haemagglutinin)
How does Relenza prevent infected cells from releasing virions?
Relenza competitively binds to the neuraminidase active site and prevents the cleavage of the docking protein
What is the final result of reflenza treatment?
Consequently, virions are not released from infected cells, preventing the spread of the influenza virus
What is cyanide? What does it do?
Cyanide is a poison which prevents ATP production via aerobic respiration, leading to eventual death
What does cyanide bind to?
It binds to an allosteric site on cytochrome oxidase – a carrier molecule that forms part of the electron transport chain