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Enzymes
1
What Are Enzymes?
•Enzymes are Proteins
•Proteins are folded in specific shapes.
•Enzymes act as biological Catalysts.
Catalysts speed up chemical reactions
•The enzyme is not permanently changed in
the process. Animation
2
3
Enzymes
•Are specific for the
substrate they will
catalyze
•Are Reusable, which
means they are not
used up in the reaction.
•End in –ase
-Sucrase
-Lactase
-Maltase
4
How do enzymes Work?
Enzymes work by
weakening chemical
bonds, which lowers
the activation energy.
Molecules can be built
up or broken down by
the body.
5
Enzymes
6
Free
Energy
Progress of the
reaction
Reactants
Products
Free energy of activation
Without Enzyme
With Enzyme
Enzyme-Substrate Complex
The substance (reactant) an enzyme
acts on is the substrate
The lock and key analogy is that the
enzyme is the lock and the
substrate is the key.
7
Enzyme
Substrate Joins
Enzyme
Active Site
•Where the substrate
temporarily fits into the active
site during the metabolic
reaction..
8
Substrate
Active
Site
Induced Fit
• A change in the
shape of an
enzyme’s active
site
• Induced by the
substrate
• The lock and
key analogy is
that the enzyme
is the lock and
the substrate is 9
Induced Fit
•A change in the configuration of an
enzyme’s active site (H+ and ionic bonds
are involved).
•Induced by the substrate.
10
Enzyme
Active Site
substrate
induced fit
What Affects Enzyme Activity?
•Three factors:
1. Environmental Conditions
2. Cofactors and Coenzymes
3. Enzyme Inhibitors
11
1. Environmental Conditions
1. Extreme Temperature are the most
dangerous
- high temps may denature (unfold) the
enzyme. When an enzyme becomes
denatured, it is essentially deactivated.
2. pH (most like 6 - 8 pH near neutral)
3. Ionic concentration (salt ions)
12
What is pH?
Water molecules naturally dissociate into a
hydrogen ion(H+) and a hydroxide ion (OH-)
Ions are charged particles.
H2O ⇄ H+ + OH-
Hydrogen Ion Hydroxide Ion
Acid
Base
13
The pH scale
● Indicates the concentration of H+ ions.
● The scale ranges from 0-14.
● 7 is neutral pH
● 0-6 is an acid
● 8-14 is a base
14
What do buffers have to do with pH?
Buffers are weak acids or bases that
react with strong acids or bases to
prevent sharp, sudden changes in pH.
These buffering systems are integral to
maintaining homeostasis in organisms.
Homeostasis means to maintain stable
internal conditions.
15
2. Cofactors and Coenzymes
•Inorganic substances (zinc, iron) and
vitamins (respectively) are sometimes
needed for proper enzymatic activity.
•Example:
Iron must be present in the quaternary
structure - hemoglobin in order for it to pick
up oxygen.
16
Two examples of Enzyme Inhibitors
a. Competitive inhibitors: are
chemicals that resemble an
enzyme’s normal substrate and
compete with it for the active site.
17
Enzyme
Competitive inhibitor
Substrate
Inhibitors
18
b. Noncompetitive inhibitors:
Inhibitors that do not enter the
active site, but bind to another part of
the enzyme causing the enzyme to
change its shape, which in turn
alters the active site.
Enzyme
active site
altered
Noncompetitive
Inhibitor
Substrate
Enzyme videos
19
Amoeba sisters enzyme video
Crash course Enzyme video
Enzyme animation
20

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Enzymes Topic - Power Point Presentation

  • 2. What Are Enzymes? •Enzymes are Proteins •Proteins are folded in specific shapes. •Enzymes act as biological Catalysts. Catalysts speed up chemical reactions •The enzyme is not permanently changed in the process. Animation 2
  • 3. 3
  • 4. Enzymes •Are specific for the substrate they will catalyze •Are Reusable, which means they are not used up in the reaction. •End in –ase -Sucrase -Lactase -Maltase 4
  • 5. How do enzymes Work? Enzymes work by weakening chemical bonds, which lowers the activation energy. Molecules can be built up or broken down by the body. 5
  • 6. Enzymes 6 Free Energy Progress of the reaction Reactants Products Free energy of activation Without Enzyme With Enzyme
  • 7. Enzyme-Substrate Complex The substance (reactant) an enzyme acts on is the substrate The lock and key analogy is that the enzyme is the lock and the substrate is the key. 7 Enzyme Substrate Joins
  • 8. Enzyme Active Site •Where the substrate temporarily fits into the active site during the metabolic reaction.. 8 Substrate Active Site
  • 9. Induced Fit • A change in the shape of an enzyme’s active site • Induced by the substrate • The lock and key analogy is that the enzyme is the lock and the substrate is 9
  • 10. Induced Fit •A change in the configuration of an enzyme’s active site (H+ and ionic bonds are involved). •Induced by the substrate. 10 Enzyme Active Site substrate induced fit
  • 11. What Affects Enzyme Activity? •Three factors: 1. Environmental Conditions 2. Cofactors and Coenzymes 3. Enzyme Inhibitors 11
  • 12. 1. Environmental Conditions 1. Extreme Temperature are the most dangerous - high temps may denature (unfold) the enzyme. When an enzyme becomes denatured, it is essentially deactivated. 2. pH (most like 6 - 8 pH near neutral) 3. Ionic concentration (salt ions) 12
  • 13. What is pH? Water molecules naturally dissociate into a hydrogen ion(H+) and a hydroxide ion (OH-) Ions are charged particles. H2O ⇄ H+ + OH- Hydrogen Ion Hydroxide Ion Acid Base 13
  • 14. The pH scale ● Indicates the concentration of H+ ions. ● The scale ranges from 0-14. ● 7 is neutral pH ● 0-6 is an acid ● 8-14 is a base 14
  • 15. What do buffers have to do with pH? Buffers are weak acids or bases that react with strong acids or bases to prevent sharp, sudden changes in pH. These buffering systems are integral to maintaining homeostasis in organisms. Homeostasis means to maintain stable internal conditions. 15
  • 16. 2. Cofactors and Coenzymes •Inorganic substances (zinc, iron) and vitamins (respectively) are sometimes needed for proper enzymatic activity. •Example: Iron must be present in the quaternary structure - hemoglobin in order for it to pick up oxygen. 16
  • 17. Two examples of Enzyme Inhibitors a. Competitive inhibitors: are chemicals that resemble an enzyme’s normal substrate and compete with it for the active site. 17 Enzyme Competitive inhibitor Substrate
  • 18. Inhibitors 18 b. Noncompetitive inhibitors: Inhibitors that do not enter the active site, but bind to another part of the enzyme causing the enzyme to change its shape, which in turn alters the active site. Enzyme active site altered Noncompetitive Inhibitor Substrate
  • 19. Enzyme videos 19 Amoeba sisters enzyme video Crash course Enzyme video Enzyme animation
  • 20. 20