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Enzyme Inhibitors

Enzyme inhibitors are molecules that impede enzyme-catalyzed reactions, with two main types: competitive and non-competitive inhibition. Competitive inhibitors, like sucralose, compete with substrates for the enzyme's active site, blocking the reaction, while non-competitive inhibitors bind to a different site, altering the enzyme's shape and reducing its activity. These mechanisms illustrate how inhibitors can disrupt normal enzymatic functions, impacting biological processes.

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136 views3 pages

Enzyme Inhibitors

Enzyme inhibitors are molecules that impede enzyme-catalyzed reactions, with two main types: competitive and non-competitive inhibition. Competitive inhibitors, like sucralose, compete with substrates for the enzyme's active site, blocking the reaction, while non-competitive inhibitors bind to a different site, altering the enzyme's shape and reducing its activity. These mechanisms illustrate how inhibitors can disrupt normal enzymatic functions, impacting biological processes.

Uploaded by

Angelica Edwards
Copyright
© © All Rights Reserved
We take content rights seriously. If you suspect this is your content, claim it here.
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Enzyme Inhibitors

Enzyme inhibitors are molecules that slow down or block


enzyme-catalyzed reactions. Enzymes are biological
catalysts that speed up chemical reactions in cells.

1. Competitive Inhibition: The inhibitor competes with the


substrate (the molecule the enzyme acts upon) for the
enzyme's active site.
Example: Sucrose (table sugar) vs. Sucralose (artificial
sweetener)
{Imagine a nightclub with a bouncer (enzyme) and a
specific guest list (substrate binding site). Sucrose would
be the invited guest(substrate) and the sucralose would
be a party crasher or someone who wasn't
invited(inhibitor) to the club. They both have similar ID’s
(molecular shape). Now sucralose comes along and
competes with sucrose as to which should enter the club
(bind to the enzymes active site).
When sucralose binds to the enzyme's active site, it
blocks sucrose from entering. The enzyme can't catalyze
the reaction because the "wrong guest" (sucralose) is
occupying the space.
To sum this up:
- Enzyme (bouncer) controls access to the reaction
(club)
- Sucrose (invited guest) binds to the enzyme's
active site
- Sucralose (party crasher) competes with sucrose,
blocking access
- Competitive inhibition occurs when sucralose
occupies the active site

Further Explanation
{Think of it like a parking lot: The substrate and inhibitor
compete for the same parking spot (active site). When
the inhibitor occupies the spot, the substrate can't park
and the reaction can't happen.}
OR
{Think of a lock: A lock needs a key to open it right? Well
if you put a fake key in it and try to open it lets say this
key broke in the lock. The actual key for this lock won't
be able to open the lock because it is already has a key
stuck in it.}

2. Non-Competitive Inhibition: The inhibitor binds


to a different site on the enzyme, altering its shape
and reducing activity.
Example: Some antibiotics work by non-competitively
inhibiting bacterial enzymes.
{Imagine a switch placed on a machine, it turns the
machine on or off. Let’s say the machine is on imagine a
troublesome kid who comes along and decides to turn
the machine off.}
OR
{Imagine you are given a question(enzyme) and this
question has two answers one right (active site) and the
other wrong(Allosteric site). You are to tick the answer
(catalizing and binding of inhibitor to enzyme) which is
correct in order for you to get the question correct. You
are not sure which is the answer and end up placing the
tick in the wrong box. You end up getting a zero on that
question.

To sum this up:


- The two answers were the sites for binding.
- However, the tick being the inhibitor got placed
in a different site.
- This causes the question to be wrong which also
means it causes the enzyme not to be able to work
efficiently.

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