Enzymes. Characteristics of Enzymes 1.Proteins 1.Monomer is: _______ ______ 2.Catalysts a.Start or...
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Transcript of Enzymes. Characteristics of Enzymes 1.Proteins 1.Monomer is: _______ ______ 2.Catalysts a.Start or...
![Page 1: Enzymes. Characteristics of Enzymes 1.Proteins 1.Monomer is: _______ ______ 2.Catalysts a.Start or speed up chemical reactions without being used up.](https://reader036.fdocuments.us/reader036/viewer/2022062422/56649f315503460f94c4cf2c/html5/thumbnails/1.jpg)
Enzymes
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Characteristics of Enzymes
1. Proteins 1. Monomer is: _______ ______
2. Catalystsa. Start or speed up chemical reactions without
being used up
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In case you wondered…How do enzymes work?
1. Lower Activation Energy to speed up rates of reactiona. Reactions require energy to begin…
enzymes lower the amount of energy required.
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Naming
1. Often end in “–ase”
2. Usually relates to the reaction they help start
a. Examples: lactase, sucrase,
protease, carboxypeptidase
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Catalyzing Process
1. A unique 3-D shape of an enzyme determines which chemical reaction it catalyzes
2. Important Vocab:a. SUBSTRATE: A specific reactant that
an enzyme acts on is called a substrate of the enzyme.
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2. Important Vocab (cont.):b. ACTIVE SITE: A substrate fits into a
region of the enzyme called an active site.1. An active site is typically a pocket or
groove on the surface of the enzyme.
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3. The enzyme and substrate form a complex
substrate
enzyme
Active site
Enzyme-substrate complex
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Lock and Key Model
+ +
Enzyme + Substrate ES complex Enzyme + Products
S
P
P
S
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Enzymes can be used to break down molecules
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Enzymes can also be used to bond two substrates into one product
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In this lab- there are three reagents: Turnip peroxidaseHydrogen peroxide
Guiacol
Which is the enzyme? Which is the substrate?
What is the other reagent then?!?
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What kind of reaction is being started in this reaction (breaking
down or building up?)
What are the products of this reaction?
H2O2 H20 + O
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How will we know if the reaction occurred?
H2O2 H20 + O
Guiacol turns brown when oxidized. (and it gets more and more brown as
more of the guiacol is oxidized).
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How do we quantify “how brown” it is?
With a spectrophotometer!
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Structure1. If an enzyme’s shape is changed so that
it is no longer able to catalyze reactions, we call it…
DENATURED
– What kinds of things do you think could denature a protein?
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Denaturation
a. Disruption of protein structure by1. Heat: Break apart H bonds and disrupt
hydrophobic attractions 2. Acids/ bases: Break H bonds between polar
R groups and ionic bonds3. Heavy metal ions: React with S-S bonds to
form solids4. Agitation: Stretches chains until bonds
break
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Applications of Denaturation
a. Hard boiling an egg
b. Wiping skin with alcohol swab for injection
c. Cooking food to destroy E. coli
d. Autoclave sterilizes instruments
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Think about it
Tannic acid is used to form a scab on a burn. An egg becomes hard boiled when placed in hot water. What is similar about these two events?
Solution
Acid and heat cause a denaturation of protein. They both break bonds in the structure of protein.
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Factors Affecting Enzyme Action
1. Temperature affects molecular motion
a. An enzyme’s optimal temperature produces the highest rate
b. Most human enzymes work best at 35-40 ºC.
WATCH OUT!!!If the temperature gets too high, the enzyme may be
denatured!
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Temperature (cont.)
Optimum temperature
ReactionRate
Low High Temperature
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2. Ions: Salt concentration & pH influence enzyme activity.
a. SALT: The salt ions interfere with some of the chemical bonds that maintain protein structure
b. pH: The same is true of the extra hydrogen ions at very low pH
1. Optimal pH for most enzymes near neutral
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3. Substrate Concentrationa. Increasing substrate concentration
increases the rate of reaction initially (enzyme concentration is constant) Why?
b. Maximum enzyme activity will be reached when all of enzyme combines with substrate.
c. What would a graph of the above look like?
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Substrate Concentration (cont.)
Maximum activity
Reaction
Rate
substrate concentration
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Enzyme Inhibition
1. Inhibitors: cause a loss of catalytic activity
a. May change the protein structure of an enzyme
b. May be competitive or noncompetitive
c. Some effects are irreversible
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2. Competitive Inhibition
a. A competitive inhibitor1. Has a structure similar to substrate2. Occupies active site
a. “Competes” with substrate for active site
3. Effects can be reversed by increasing substrate concentration
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Competitive Inhibition Image
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3. Noncompetitive Inhibition
a. A noncompetitive inhibitor
1. Does not have a structure like substrate
2. Binds to the enzyme (not at active site) & changes the shape of enzyme & active site
a. Substrate cannot fit altered active site
3. No reaction occurs
4. Effect is not reversed by adding substrate
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Noncompetitive Inhibition Image