Loading presentation...

Present Remotely

Send the link below via email or IM

Copy

Present to your audience

Start remote presentation

  • Invited audience members will follow you as you navigate and present
  • People invited to a presentation do not need a Prezi account
  • This link expires 10 minutes after you close the presentation
  • A maximum of 30 users can follow your presentation
  • Learn more about this feature in our knowledge base article

Do you really want to delete this prezi?

Neither you, nor the coeditors you shared it with will be able to recover it again.

DeleteCancel

Make your likes visible on Facebook?

Connect your Facebook account to Prezi and let your likes appear on your timeline.
You can change this under Settings & Account at any time.

No, thanks

Enzyme inhibitors

No description
by

Rure Manyika

on 22 May 2016

Comments (0)

Please log in to add your comment.

Report abuse

Transcript of Enzyme inhibitors

.
While the inhibitor is attached to the enzyme, the enzyme's function is blocked.
This is reversible because if the inhibitor leaves the enzyme, its
shape is restored
and the enzyme can now accept substrate.
Comparing Enzyme affinities
V-Max
Measuring how well an enzyme performs by finding the theoretical maximum rate (V-max) of the reaction it catalyzes is, a key step to allowing the comparability of affinities.
At V-max ,
all the enzyme molecules are bound to substrate molecules.

Some more V-max
Example of competitive inhibition
.
Non-competitive inhibition
This is when a substance reduces the rate of activity of an an enzyme by
binding to areas of the enzyme molecule other than the active site
.
While the inhibitor is bound to the enzyme, it seriously disrupts the normal arrangement of
hydrogen bonds and hydrophobic interactions
holding the enzyme in its 3-D shape.
Competitive, reversible inhibition
The active site of an enzyme fits one particular substrate. However, it is possible for some other molecule to bind to an enzyme's active site if it is very similar in shape to the enzyme's substrate.
The molecule will be called an
inhibitor
.
Enzyme inhibitors Among Other things
Explanation
While the inhibitor is bound to the active site, it prevents a substrate molecule from occupying that site. So,
inhibitors reduce the rate of the reaction
.
.
The resulting distortion ripples across the molecule to the active site, making the enzyme
unsuitable for the substrate
.

How V-max is measured; The reaction rate is measured at different substrate concentrations while keeping the enzyme concentration constant. As substrate concentration is increased, reaction rate rises until the reaction reaches its maximum rate.

Due to this inhibition being reversible, the
same quantity of product is formed
.
This is because the substrate continues to
use any enzyme that is unaffected by the inhibitor
.
NOTE: The enzyme is not denatured when the inhibitor leaves, hence the reversibility of the process.
Km
Km is the substrate concentration at which an enzyme works at
half its maximum rate
(1/2V-max). At km, half the active sites are occupied by substrate.
So,
the higher the affinity of the enzyme for the substrate, the lower the substrate concentration needed for 1/2 V-max to be reached.
Thus, the Michaelis-Menten (Km) constant is a measure of the affinity of the enzyme for its substrate.
Immobilizing enzymes
Enzymes can be immobilized- for example, by trapping them in jelly (alginate) beads. This is commercially used because the
enzyme can be re-used
and the
product is separate from (uncontaminated by) the enzyme
.
Full transcript