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Please pick up your lab notebooks from the table by the door.
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Overall 1st Quarter Grades (AVG) (updated w/ Unit 2 Test included)
• 1st period: 85%
• 2nd period: 89%
• 3rd period: 86%
• 4th period: 88%
• 6th period: 90%
• 8th period: 86%
• WOW!!!
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Pre-Lab Preparation!!!• Go to “Labs & Lab Notebook” link on my website.• Click on “LabBench” link.• Click on “Lab 1: Diffusion & Osmosis.”• Read through Concepts #1-5, Design Exercises
#1-2, and Self-Quiz ?s #1-3 of the Pre-Lab.• Answer the general questions COMPLETELY that
are listed on your Lab Notebook Guidelines sheet.– Remember to ignore the “Water Potential”
section and calculations– Due on Friday!!!
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1. What is metabolism?• All of an organisms chemical processes
2. What are the different types of metabolism?• Catabolism – releases energy by breaking down complex
molecules• Anabolism – use energy to build up complex molecules• Catabolic rxns – hydrolysis – break bonds• Anabolic rxns – dehydration – form bonds
3. How is metabolism regulated?
Chapter 8: An Introduction to Metabolism
Enzyme 1 Enzyme 2 Enzyme 3
A B C DReaction 1 Reaction 2 Reaction 3
Startingmolecule
Product
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4. What are the different forms of energy?
- Kinetic – energy from molecules in motion
- Potential – energy based on location or structure
- water behind a dam
- bonds in gas/oil
- Chemical energy – bio speak for potential energy that can be released in a catabolic rxn
Chapter 8: An Introduction to Metabolism
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Figure 8.2 Transformation between kinetic and potential energy
On the platform, a diverhas more potential energy.
Diving converts potentialenergy to kinetic energy.
Climbing up converts kinetic
energy of muscle movement
to potential energy.
In the water, a diver has less potential energy.
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5. What are the 2 laws of thermodynamics?
- 1st law – Energy is constant. It can be transferred or transformed but it cannot be created or destroyed.
- 2nd law – Every transfer or transformation of energy increases the entropy (disorder) of the universe.
Chapter 8: An Introduction to Metabolism
(a) First law of thermodynamics: Energy can be transferred or transformed but neither created nor destroyed. For example, the chemical (potential) energy in food will be converted to the kinetic energy of the cheetah’s movement in (b).
Second law of thermodynamics: Every energy transfer or transformation increasesthe disorder (entropy) of the universe. For example, disorder is added to the cheetah’ssurroundings in the form of heat and the small molecules that are the by-productsof metabolism.
(b)
Chemicalenergy
Heatco2
H2O+
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6. What is the difference between exergonic & endergonic rxns?
- Exergonic – releases energy
- Endergonic – require energy
- Catabolic rxns – hydrolysis – break bonds – exergonic
- Anabolic rxns – dehydr. syn. – form bonds – endergonic
7. Where does the energy come from to drive rxns in the body?
- ATP
Chapter 8: An Introduction to Metabolism
CH–O O O O CH2
H
OH OH
H
N
H H
O
NC
HC
NC
C
N
NH2Adenine
Ribose
O–
O O
O–
O
O–
P P P
Phosphate groups
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8. How does ATP provide energy?
- hydrolysis of ATP
Chapter 8: An Introduction to Metabolism
P
Adenosine triphosphate (ATP)
H2O
+ Energy
Inorganic phosphate Adenosine diphosphate (ADP)
PP
P PP i
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Figure 8.10 Energy Coupling: Use an exergonic reaction to fuel an endergonic reaction!!!
Endergonic reaction (dehydration synthesis of NH2 and Glu): ∆G is positive, reaction is not spontaneous
∆G = +3.4 kcal/molGlu Glu
∆G = –7.3 kcal/molATP H2O+
+ NH3
ADP +
NH2
Glutamicacid
Ammonia Glutamine
Exergonic reaction (hydrolysis of ATP): ∆ G is negative, reaction is spontaneous
P
Coupled reactions: Overall ∆G is negative; together, reactions are spontaneous ∆G = –3.9 kcal/mol
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Figure 8.11 How ATP drives cellular work
+
P
Motor protein
P i
Protein moved
(a) Mechanical work: ATP phosphorylates motor proteins
Membraneprotein
ATP
Solute
P P i
P i
ADP+
Solute transported
(b) Transport work: ATP phosphorylates transport proteins
GluGlu
NH3
NH2
P i
P
+
(c) Chemical work: ATP phosphorylates key reactants
Reactants: Glutamic acid and ammonia
Product (glutamine)made
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ATP synthesis from ADP + P i requires energy (endergonic)
ATP
ADP + P i
Energy for cellular work (such as dehydration synthesis!)
Energy from catabolism(breaking down food molecules via hydrolysis)
ATP hydrolysis to ADP + P i yields energy (exergonic)
Figure 8.12 The ATP cycle
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9. What is an enzyme?
- biological catalyst made of protein
10. How do enzymes work?
- lower energy of activation (EA)
- EA = energy reactants must absorb before the rxn can start
Chapter 8: An Introduction to Metabolism
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A
C D
A
A
B
B
B
C
C
D
D
Transition state
Products
Progress of the reaction
∆G < O
Reactants
Fre
e en
ergy
EA
The reactants AB and CD must absorbenough energy from the surroundingsto reach the unstable transition state,where bonds can break.
Bonds break and newbonds form, releasingenergy to thesurroundings.
Figure 8.14 Energy profile of an exergonic reaction
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Progress of the reaction
Products
Course of reaction without enzyme
Reactants
Course of reaction with enzyme
EA
withoutenzyme
EA with enzymeis lower
∆G is unaffected by enzyme
Fre
e e
ne
rgy
Figure 8.15 The effect of enzymes on reaction rate.
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11. Some enzyme terms
- substrate – what the enzyme works on – substrate-specific
- active site – where the substrate binds to the enzyme
- induced fit – molecular handshake – when the enzyme binds to the substrate, it wraps around the substrate
Chapter 8: An Introduction to Metabolism
Substrate
Active site
Enzyme
(a) (b)
Enzyme- substratecomplex
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Figure 8.17 The active site and catalytic cycle of an enzyme
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How does it work?
• Variety of mechanisms to lower activation energy & speed up reaction– Dehydration synthesis
• active site orients substrates in correct position for reaction/brings substrates closer together
– Hydrolysis • active site binds substrate & puts stress on
bonds that must be broken, making it easier to separate molecules
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Enzymes in REAL LIFE!• Enzymes named for reaction they catalyze
– sucrase breaks down sucrose
– proteases break down proteins
– lipases break down lipids
– DNA polymerase builds DNA• adds nucleotides
to DNA strand
– pepsin breaks down proteins (polypeptides)
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12. What affects enzyme activity?
- temperature
- pH
Chapter 8: An Introduction to Metabolism
Optimal pH for two enzymes
Ra
te o
f re
act
ion
Ra
te o
f re
act
ion
0 20 40 60 80 100Temperature (Cº)
(a) Optimal temperature for two enzymes
(b) Optimal pH for two enzymespH
Optimal temperature fortypical human enzyme
Optimal temperature for enzyme of thermophilic
Optimal pH for pepsin (stomach enzyme)
Optimal pHfor trypsin(intestinalenzyme)
10 2 3 4 5 6 7 8 9 10
(heat-tolerant) bacteria
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12. What affects enzyme activity?- temperature- pH- cofactors – inorganic non-protein helpersof enzyme activity (Zn, Fe, Cu)
- coenzymes – organic cofactors (vitamins)
- inhibitors- competitive – compete w/ substrate for active site
-PENICILLIN – blocks enzyme that bacteria use to build cell walls
- non-competitive – bind remotely (not to active site, but to secondary site called ALLOSTERIC SITE,) thus changing enzyme shape & inhibiting activity
-CYANIDE – changes shape of enzyme necessary to make ATP during cellular respiration
Chapter 8: An Introduction to Metabolism
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A noncompetitiveinhibitor binds to the
enzyme away fromthe active site, altering
the conformation ofthe enzyme so that its
active site no longerfunctions.
Competitiveinhibitor
(a) Normal binding
(b) Competitive inhibition
A substrate canbind normally to the
active site of anenzyme.
A competitiveinhibitor mimics the
substrate, competingfor the active site.
Substrate
Active site
Enzyme
Noncompetitive inhibitor
(c) Noncompetitive inhibition
Figure 8.19 Inhibition of enzyme activity
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12. What affects enzyme activity?
13. How are enzymes regulated?
- allosteric inhibitors
-keeps enzyme inactive
- allosteric activators
-keeps enzyme active
Chapter 8: An Introduction to Metabolism
Stabilized inactiveform
Allosteric activaterstabilizes active fromAllosteric enyzme
with four subunitsActive site
(one of four)
Regulatorysite (oneof four)
Active formActivator
Stabilized active form
Allosteric inhibiterstabilizes inactive form
InhibitorInactive formNon-functionalactivesite
Oscillation
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12. What affects enzyme activity?
13. How are enzymes regulated?
- allosteric inhibitors
- allosteric activators
Chapter 8: An Introduction to Metabolism
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12. What affects enzyme activity?
13. How are enzymes regulated?
- allosteric inhibitors
- allosteric activators
- feedback inhibition
-final product is inhibitor
of earlier step!
-prevents unnecessary
accumulation of product
Chapter 8: An Introduction to Metabolism
Active siteavailable
Isoleucineused up bycell
Feedbackinhibition
Isoleucine binds to allosteric site
Active site of enzyme 1 no longer binds threonine;pathway is switched off
Initial substrate(threonine)
Threoninein active site
Enzyme 1(threoninedeaminase)
Intermediate A
Intermediate B
Intermediate C
Intermediate D
Enzyme 2
Enzyme 3
Enzyme 4
Enzyme 5
End product(isoleucine)
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