kDeeksha Marla

Mr. Didden
AP Bio
Chapter 8: An Introduction to Metabolism
Metabolism: Emergent property of life that arises from orderly interactions between
molecules
1. Metabolic Pathways
1. Metabolic pathways> begins with a specific molecules, resulting in a certain
product,
3. Catabolic pathways=degradative that releases energy by breaking down
molecules, complex to simple
1. Cellular respiration
4. Anabolic pathways=consume energy to build complex molecules from simpler
molecules
5. used to drive anabolic
2.
1.
2.
3.

Energy Forms
Capacity to cause change
Some form can be used to do work
Heat or thermal E: Kenergy associated with random movement of atoms or
molecules
8. Molecules in Cat. Path. are high in chemical energy
3. Energy Transformation
1. Study of energy transformations that occur in a collection of matter:
thermodynamics
3. Isolation system: unable to exchange energy or matter w surroundings
4. Open system: able to
5. Organisms> open systems, absorb energy in form of organic molecules, and
release heat and metabolic waste products to surroundings
4.
1.
2.
3.
5.
2.

First Law of Thermodynamics

Energy of the universe in constant
Can be transformed or transferred, but not created or destroyed
Conservation of E
2nd Law
During any energy transfer or transformation, more usable forms are
transformed to heat> how it is lost
3. energy is only converted to heat when it not utilized

4.
6.
7.
8.

Entropy: disorder of randomness, more random, more entropy

Spontaneous process: a process that does not require input of E
Nonspontaneous: Cannot occur on its own, no energy needed
For a process to occur spontaneously, it must increase the entry of the universe

1. Free-Energy Change, Delta G

1. Free Energy: proportion of a systems energy that can perform work when
temperature and pressure are uniform throughout the system, as in a living cell
2. H symbolizes change in systems enthalpy, total energy
3. S change in systems entropy
4. T temp in Kelvin
5. -G is spontaneous reaction, spontaneous process decreases systems free
energy
2. Free Energy, Stability, and Equilibrium
1. Spontaneous: loss of free energy
2. Unstable systems (higher G) change in such a way that they become more
stable (lower G)
3. Equilibrium: maximum stability
4. Most chem reactions are reversible, forward and back at same rate, net
change= 0
5. More equilibrium= less G, lowest possible state
6. A process is spontaneous and can perform work only when it is moving toward
equilibrium
3. Free Energy and Metabolism
4. Exergonic and Endergonic Reactions in Metabolism
1. Exergonic reaction: proceeds with a net release of free energy, chemical mixture
loses G, G is negative in exergonic reaction, occur spontaneously (energetically
favorable)
2. Magnitude of delta G for an exergonic reaction represents the maximum amount
of work the reaction can perform
3. Greater decrease in free energy, greater amount of work can be done
4. Breaking of bonds does not release energy, requires energy, energy stored in
bonds potential energy that can be released when new bonds are formed after
original bonds break, products are of lower G than reactants
5. Endergonic reaction: absorbs G from surroundings
1. Stores G in molecules, G is pos
2. Non spontaneous

3. Magnitude of G is the quantity of energy to drive the reaction

4. Using energy instead of releasing
5.
1.
2.
3.
4.

Equilibrium and Metabolism

Metabolism is never at equilibrium in a living cell, can do no work
Catabolic pathway is exergonic reaction (Cell resp.)
Product becomes reactant in next reaction (kept out of equilibrium)
Organisms are open systems

3 main types of work by cell:

1. Chemical work: Non Spontaneous endergonic reactions such as poly to mono
2. Transport work: Pumping of substances across membranes against dir. of
spontaneous movement, active transport
3. Mechanical work: cilia
4. Energy coupling> use of an exergonic process to drive an endergonic one,
ATP
5. The Structure and Hydrolysis of ATP
1. ATP: Sugar ribose, nitrogenous base adenine, 3 phosphate groups
2. Bonds can be broken by hydrolysis
3. ATP + H2O= ADP + P
4. Exergonic rxn, -7.3kcal /mol (standard cond.) cellular conditions = higher G
release
5. High energy phosphate bonds> release of energy does not come from but
from conversion of ATP which is high energy to ADP which is low energy and
going from H to L energy state u release E
6. ATP releases more energy than other molecules
7. Triphosphate tail is unstable bc they are negative
6. How the Hydrolysis of ATP performs work
1. Release of ATP heats surroundings, in cell used for chemical, mech, and trans
work
2. Uses energy to drive chem rxns that by themselves are endergonic
3. If G of endergonic rxn is less than amt of energy released by ATP hydrolysis,
then two rxns can be coupled so that the coupled reactions are exergonic,
transfer of phosphate group from ATP to some other molecule such as the
reactant.
4. Recipient w the phosphate group covalently bonded to it is called
phosphorylated intermediate > less stable than original
7. The Regeneration of ATP
1. Organism at work uses ATP continuously

2. G required to phosphorylate ADP comes from exergonic breakdown run

(catabolism) in cell
3. ATP + h2o = ADP + P + energy from cellular rxns, ADP + P + energy from
catabolic rxn = ATP + h2o
4. Regeneration of ATp from ADP and P is endergonic
5. energy is used, catabolic reactions provide E

1. The Activation energy Barrier

1. changing =ing on molecule into another involves making starting molecule
unstable
2. Activation Energy> the initial investment of energy required to contort the
reactant molecules so the bonds can break, Ea
3. Push to top of uphill barrier (heat i.e.)
4. Transition state: unstable position of reactant
5. Endergonic to exergonic
6. Reaction will occur at noticeable rate only if reactants are heated, more often
2. How Enzymes Lower the Ea Barrier
1. High temp denatures, kills proteins, heat would speed up all reactions
2. Enzyme catalyses by lowering Ea barrier, specific for reactions
3. Substrate Specificity of Enzymes
1. Substrate: reactant an enzyme acts on, binds to it to form enzyme-substrate
complex, converts substrate to products
2. Enzymes have 3D configurations, specificity is determined by AA sequence
3. Only portion that binds to substrate= active site
5. Enzyme changes shape due to interactions bw substrates chemical groups and
chem groups of side chains of the amino acids that form the active site
6. Induced fit: brings chemical groups of active site into positions that enhance
ability to catalyze chem run
4. Catalysis in the Enzyme's Active Site
1. Occurs very rapidly w multiple substrates at same time
2. Reversible
1. Four mechanisms enzymes create catalysis
1. Provides a template for substrate
4. Direct participation of active site in chem rxn (i.e. brief covalent bonding)
5. Restore side chains to orig state so that active site is the same, reversible

3. Rate is a function of initial conc., more substrate molecules, more frequently

they access active sites, saturated> no more enzyme available, more than
substrate, add more enzymes to increase rate
5. Effects of Local Conditions on Enzyme Activity
1. Affect the activity of enzyme
1. Temperature
2. pH
1. Rate of an enzymatic reaction increases w heat
2. Substrates collide more frequently
3. Hotter than specific heat disrupts hydrogen and ionic bonds causing
molecule to denature
4. 35-40 deg C for humans
3. Chemicals
1. Cofactors: nonprotein helpers for catalytic activity, bound to enzyme or
substrate
2. Coenzyme: organic cofactor
3. Enzyme Inhibitors
1. Irreversible or reversible depending on strength of Binding
2. Competitive Inhibitors: resembling substrate and compete w substrate
for active site, increase more substrate to deny
3. Noncompetitive Inhibitors: bind to another part of enzyme to make
active site less functional by changing shape
1.
1.
2.
3.

Allosteric Regulation of Enzymes

Reversible noncompetitive inhibitors
Change an enzymes shape by nonequivalent interaction
Any case in which a proteins function at one site is affected the binding of a
regulatory molecule to a separate site, and may result in either inhibition or
stimulation of activity
4. Oscillates bw 2 diff shapes, one catalytically active and other inactive
5. Join to create an allosteric site
6. Activator==> stabilizes shape that has functional active sites
7. Inhibitor> stabilizes inactive form of enzyme
8. Affects site of ALL subunits
9. ATP binds to several catabolic enzymes allosterically, lowering affinity for
substrate and thus inhibiting activity
10. ADP functions as activator of same enzymes
11. ATP hydrolysis is controlled by allosteric enzyme activity
12. Rate of run is driven by amt of ATP, ADP accumulates and activates enzymes,
producing more ATP, ATP bind to same enzymes, inhibiting them

13. Cooperativity: Substrate binding to one site in a multisubunit enzyme, triggering

shape change in all subunit and thus increase catalytic activity
2. Identification of Allosteric Regulators
1. Bind to enzyme at low affinity and hard to isolate
2. Distinct bw enzymes, higher specificity
3. Feedback Inhibition
1. A metabolic pathway is switched off by inhibitory binding of its end product to an
enzyme that act early in pathway
4. Specific Location of Enzymes within the Cell
1. Compartmentalized, cellular structures bring order to metabolic pathways,
apartment, mitochondria