Metabolism and Enzymes. Metabolism- the total of all chemical reactions done in an organism to store...
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Transcript of Metabolism and Enzymes. Metabolism- the total of all chemical reactions done in an organism to store...
![Page 1: Metabolism and Enzymes. Metabolism- the total of all chemical reactions done in an organism to store or release energy. (the number of molecules built.](https://reader036.fdocuments.us/reader036/viewer/2022070401/56649f1b5503460f94c301b8/html5/thumbnails/1.jpg)
Metabolism and Enzymes
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• Metabolism- the total of all chemical reactions done in an organism to store or release energy. (the number of molecules built vs. the amount of molecules broken down) ex. Digestion or building muscle.
• A metabolic pathway begins with a specific molecule and ends with a product and is carried out by enzymes.
Metabolism
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• Catabolic pathways release energy by breaking down molecules into simpler compounds.
• Ex. Cellular respiration, the breakdown of glucose to release energy in humans.
Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings
Catabolic Pathways
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• Anabolic pathways use energy to build molecules.
• The synthesis of protein from amino acids to be used in muscles is an example of anabolism.
Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings
Anabolic Pathways
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Thermodynamics• Thermodynamics is the study of energytransformations
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The First Law of Thermodynamics• 1st Law – energy cannot not by created or
destroyed, just transformed.
Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings
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The Second Law of Thermodynamics• 2nd Law- Every energy transfer increases the
entropy (disorder) of the universe and makes things unstable. (energy will seek to get back into a stable form or equilibrium)
Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings
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Free Energy• free energy - energy available to do work• ∆G = change in free energy• If ∆G is negative energy was released (becomes
more stable) • If ∆G is positive energy was stored (becomes less
stable)
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Spontaneous Change• Releasing free energy is known as a spontaneous
change. The energy released in a spontaneous change can be harnessed to do work.
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Fig. 8-5
(a) Gravitational motion (b) Diffusion (c) Chemical reaction
• More free energy (higher G)• Less stable• Greater work capacity
In a spontaneous change• The free energy of the system decreases (∆G < 0)• The system becomes more stable• The released free energy can be harnessed to do work
• Less free energy (lower G)• More stable• Less work capacity
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• An endergonic reaction absorbs free energy from its surroundings and is nonspontaneous. (Anabolic)
Energy in Cells
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Energy in Cells• An exergonic reaction proceeds with a net
release of free energy and is spontaneous. (Catabolic)
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Energy Coupling • energy coupling - the use of an exergonic process to
drive an endergonic one
• Most energy coupling in cells is done by ATP (the cells energy molecule).
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ATP • ATP (adenosine triphosphate) - ATP made of
ribose (a sugar), adenine (a nitrogenous base), and three phosphate groups.
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• ATP powers cells by breaking off a phosphate group. This lowers free energy and releases energy. (exergonic)
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ATP at Work
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ATP at Work• The released phosphate combines with a reactant
(phosphorylation) to make it unstable.• This endergonic reaction makes the recipient
molecule unstable with extra stored energy and able to do work.
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Fig. 8-11
(b) Mechanical work: ATP binds noncovalently to motor proteins, then is hydrolyzed
Membrane protein
P i
ADP+
P
Solute Solute transported
Pi
Vesicle Cytoskeletal track
Motor protein Protein moved
(a) Transport work: ATP phosphorylates transport proteins
ATP
ATP
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Fig. 8-12
P iADP +
ATP + H2O
Energy Coupling • Dephosphorylation (exergonic)
• Phosphorylation (endergonic)
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Enzymes• catalyst - is a chemical agent that speeds up a
reaction (can be reused)• An enzyme is a catalytic proteinEx. Hydrolysis of sucrose by the enzyme sucrase
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Activation Energy• activation energy (EA) -The initial energy needed
to start a chemical reaction
• Activation energy can by supplied in the form of heat from the surroundings
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Fig. 8-14
Progress of the reaction
Products
Reactants
∆G < O
Transition state
Fre
e en
erg
y EA
DC
BA
D
D
C
C
B
B
A
A
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Enzymes Lower the EA• Enzymes catalyze reactions by lowering the EA
barrier*
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Substrate Specificity of Enzymes• substrate -reactant that an enzyme acts on enzyme-• substrate complex – enzyme and substrate together• active site – part of the enzyme the substrate binds to• Induced fit – “lock and key” matching shape of
enzyme and substrate
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How EA is lowered • The active site can lower an EA barrier by
– Orienting substrates correctly
– Straining substrate bonds
– Providing favorable pH
– Covalently bonding to the substrate
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Fig. 8-17
Substrates
Enzyme
Products arereleased.
Products
Substrates areconverted toproducts.
Active site can lower EA
and speed up a reaction.
Substrates held in active site by weakinteractions, such as hydrogen bonds andionic bonds.
Substrates enter active site; enzyme changes shape such that its active siteenfolds the substrates (induced fit).
Activesite is
availablefor two new
substratemolecules.
Enzyme-substratecomplex
5
3
21
6
4
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Enzyme Denature• An enzyme’s activity can be affected by general
environmental factors, such as temperature, pH, salinity, and solute concentration.
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Cofactors• Cofactors - are nonprotein enzyme helpers
• Coenzyme - An organic cofactor (ex. Vitamins)
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Enzyme Inhibitors• Competitive inhibitors bind to the active site of
an enzyme, competing with the substrate• Noncompetitive inhibitors bind to another part of
an enzyme, causing the enzyme to change shape and making the active site less effective
• Examples of inhibitors include toxins, poisons, pesticides, and antibiotics
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Allosteric Regulation of Enzymes• Enzyme activity is controlled to regulate metabolism.• Allosteric regulation - occurs when a regulatory
molecule binds to a protein at one site and affects the protein’s function at another site.
• Inhibitors make enzymes inactive • Activators make enzymes active
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Cooperativity• Cooperativity is a form of allosteric regulation
where the presence of the substrate makes the enzyme active.
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Feedback Inhibition• In feedback inhibition, the end product of a metabolic pathway shuts down the pathway.Ex. thermostat.
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You should now be able to:
1. Distinguish between the following pairs of terms: catabolic and anabolic pathways; exergonic and endergonic reactions
2. In your own words, explain the laws of thermodynamics.
3. Explain in general terms how cells obtain the energy to do cellular work
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4. Explain how ATP performs cellular work
5. Explain why an investment of activation energy is necessary to initiate a spontaneous reaction
6. Describe the mechanisms by which enzymes lower activation energy
7. Describe how allosteric regulators may inhibit or stimulate the activity of an enzyme
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