October 10 AP Biology - John D. O'Bryant School of Math & Science

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AP Biology
John D. O’Bryant School of
Mathematics and Science
October 10, 2012
AP Biology
Agenda
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Do Now (Quiz)
Nobel Prize in Chemistry
Lactose Intolerance video
Experimental Design: Lactose Intolerance, etc.
AP Biology
Do Now (Quiz)
1. Which of the following statements is true concerning
catabolic pathways?
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A) They combine molecules into more energy-rich
molecules.
B) They are usually coupled with anabolic pathways to
which they supply energy in the form of ATP.
C) They are endergonic.
D) They are spontaneous and do not need enzyme
catalysis.
E) They build up complex molecules such as protein from
simpler compounds.
AP Biology
Do Now (Quiz)
 2. When chemical, transport, or mechanical work is done by
an organism, what happens to the heat generated?
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A) It is used to power yet more cellular work.
B) It is used to store energy as more ATP.
C) It is used to generate ADP from nucleotide precursors.
D) It is lost to the environment.
E) It is transported to specific organs such as the brain.
AP Biology
Do Now (Quiz)
 3. During a laboratory experiment, you discover that an
enzyme-catalyzed reaction has a △G of -20 kcal/mol. If you
double the amount of enzyme in the reaction, what will be
the △G for the new reaction?
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A) -40 kcal/mol
B) -20 kcal/mol
C) 0 kcal/mol
D) +20 kcal/mol
E) +40 kcal/mol
AP Biology
Do Now (Quiz)
 4. According to the induced fit hypothesis of enzyme
catalysis, which of the following is correct?
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A) The binding of the substrate depends on the shape of
the active site.
B) Some enzymes change their structure when activators
bind to the enzyme.
C) A competitive inhibitor can outcompete the substrate for
the active site.
D) The binding of the substrate changes the shape of the
enzyme's active site.
E) The active site creates a microenvironment ideal for the
reaction.
AP Biology
Do Now (Quiz)
 5. Which of the following is likely to lead to an increase in
the concentration of ATP in a cell?
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A) an increase in a cell's anabolic activity
B) an increase in a cell's catabolic activity
C) an increased influx of cofactor molecules
D) an increased amino acid concentration
E) the cell's increased transport of materials to the
environment
AP Biology
Do Now (Quiz)
 6. The mechanism in which the end product of a metabolic
pathway inhibits an earlier step in the pathway is known as
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A) metabolic inhibition.
B) feedback inhibition.
C) allosteric inhibition.
D) noncooperative inhibition.
E) reversible inhibition.
AP Biology
Do Now (Quiz)
 7. If an enzyme solution is saturated with substrate, the
most effective way to obtain a faster yield of products is to
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A) add more of the enzyme.
B) heat the solution to 90°C.
C) add more substrate.
D) add an allosteric inhibitor.
E) add a noncompetitive inhibitor.
AP Biology
Metabolism & Enzymes
AP Biology
2007-2008
Factors that Affect Enzymes
AP Biology
2007-2008
Factors Affecting Enzyme Function
 Enzyme concentration
 Substrate concentration
 Temperature
 pH
 Salinity
 Activators
 Inhibitors
AP Biology
catalase
Enzyme concentration
reaction rate
What’s
happening here?!
enzyme concentration
AP Biology
Factors affecting enzyme function
 Enzyme concentration
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as  enzyme =  reaction rate
 more enzymes = more frequently collide with
substrate

reaction rate levels off
reaction rate
 substrate becomes limiting factor
 not all enzyme molecules can find substrate
AP Biology
enzyme concentration
Substrate concentration
reaction rate
What’s
happening here?!
substrate concentration
AP Biology
Factors affecting enzyme function
 Substrate concentration

as  substrate =  reaction rate
 more substrate = more frequently collide with
enzyme

reaction rate levels off
reaction rate
 all enzymes have active site engaged
 enzyme is saturated
 maximum rate of reaction
AP Biology
substrate concentration
Temperature
reaction rate
What’s
happening here?!
37°
temperature
AP Biology
Factors affecting enzyme function
 Temperature

Optimum T°
 greatest number of molecular collisions
 human enzymes = 35°- 40°C
 body temp = 37°C
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Heat: increase beyond optimum T°
 increased energy level of molecules disrupts
bonds in enzyme & between enzyme & substrate
 H, ionic = weak bonds
 denaturation = lose 3D shape (3° structure)
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Cold: decrease T°
 molecules move slower
 decrease collisions between enzyme & substrate
AP Biology
Enzymes and temperature
 Different enzymes function in different
organisms in different environments
reaction rate
human enzyme
hot spring
bacteria enzyme
37°C
AP Biology
temperature
70°C
(158°F)
How do ectotherms do it?
AP Biology
pH
What’s
happening here?!
trypsin
reaction rate
pepsin
pepsin
trypsin
0
AP Biology
1
2
3
4
5
6
pH
7
8
9
10
11
12
13
14
Factors affecting enzyme function
 pH

changes in pH
 adds or remove H+
 disrupts bonds, disrupts 3D shape
 disrupts attractions between charged amino acids
 affect 2° & 3° structure
 denatures protein

optimal pH?
 most human enzymes = pH 6-8
 depends on localized conditions
 pepsin (stomach) = pH 2-3
 trypsin (small intestines) = pH 8
AP Biology
0 1 2 3 4 5 6 7 8 9 10 11
Salinity
reaction rate
What’s
happening here?!
salt concentration
AP Biology
Factors affecting enzyme function
 Salt concentration

changes in salinity
 adds or removes cations (+) & anions (–)
 disrupts bonds, disrupts 3D shape
 disrupts attractions between charged amino acids
 affect 2° & 3° structure
 denatures protein

enzymes intolerant of extreme salinity
 Dead Sea is called dead for a reason!
AP Biology
Compounds which help enzymes
Fe in
 Activators
hemoglobin

cofactors
 non-protein, small inorganic
compounds & ions
 Mg, K, Ca, Zn, Fe, Cu
 bound within enzyme molecule
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coenzymes
 non-protein, organic molecules
 bind temporarily or permanently to
enzyme near active site
AP Biology
 many vitamins
 NAD (niacin; B3)
 FAD (riboflavin; B2)
 Coenzyme A
Mg in
chlorophyll
Compounds which regulate enzymes
 Inhibitors
molecules that reduce enzyme activity
 competitive inhibition
 noncompetitive inhibition
 irreversible inhibition
 feedback inhibition

AP Biology
Competitive Inhibitor
 Inhibitor & substrate “compete” for active site
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penicillin
blocks enzyme bacteria use to build cell walls
disulfiram (Antabuse)
treats chronic alcoholism
 blocks enzyme that
breaks down alcohol
 severe hangover & vomiting
5-10 minutes after drinking
 Overcome by increasing substrate
concentration

AP Biology
saturate solution with substrate
so it out-competes inhibitor
for active site on enzyme
Non-Competitive Inhibitor
 Inhibitor binds to site other than active site


allosteric inhibitor binds to allosteric site
causes enzyme to change shape
 conformational change
 active site is no longer functional binding site
 keeps enzyme inactive

some anti-cancer drugs
inhibit enzymes involved in DNA synthesis
 stop DNA production
 stop division of more cancer cells

cyanide poisoning
irreversible inhibitor of Cytochrome C,
an enzyme in cellular respiration
 stops production of ATP
AP Biology
Irreversible inhibition
 Inhibitor permanently binds to enzyme

competitor
 permanently binds to active site

allosteric
 permanently binds to allosteric site
 permanently changes shape of enzyme
 nerve gas, sarin, many insecticides
(malathion, parathion…)
 cholinesterase inhibitors

AP Biology
doesn’t breakdown the neurotransmitter,
acetylcholine
Allosteric regulation
 Conformational changes by regulatory
molecules

inhibitors
 keeps enzyme in inactive form

activators
 keeps enzyme in active form
AP Biology Conformational
changes
Allosteric regulation
Metabolic pathways
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ABCDEFG
5
6
enzyme enzyme enzyme
enzyme enzyme enzyme
enzyme
1
2
3
4
 Chemical reactions of life
are organized in pathways

AP Biology
divide chemical reaction
into many small steps
 artifact of evolution
  efficiency
 intermediate branching points
  control = regulation
Efficiency
 Organized groups of enzymes
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enzymes are embedded in membrane
and arranged sequentially
 Link endergonic & exergonic reactions
Whoa!
All that going on
in those little
mitochondria!
AP Biology
Feedback Inhibition
 Regulation & coordination of production

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product is used by next step in pathway
final product is inhibitor of earlier step
 allosteric inhibitor of earlier enzyme
 feedback inhibition

no unnecessary accumulation of product
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ABCDEFG
1
2
3
4
5
6
X
enzyme enzyme enzyme enzyme enzyme enzyme
AP Biology
allosteric inhibitor of enzyme 1
threonine
Feedback inhibition
 Example
synthesis of amino
acid, isoleucine from
amino acid, threonine
 isoleucine becomes
the allosteric
inhibitor of the first
step in the pathway

 as product
accumulates it
collides with enzyme
more often than
substrate does
AP Biology
isoleucin
e
Don’t be inhibited!
Ask Questions!
AP Biology
2007-2008
Ghosts of Lectures Past
(storage)
AP Biology
2007-2008
Cooperativity
 Substrate acts as an activator


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substrate causes conformational
change in enzyme
 induced fit
favors binding of substrate at 2nd site
makes enzyme more active & effective
 hemoglobin
Hemoglobin
 4 polypeptide chains
 can bind 4 O2;
 1st O2 binds
 now easier for other
O2 to bind
AP3Biology
Lorenzo’s Oil
AP Biology
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