Metabolic Pathways
Enzyme 1
A
Enzyme 3
D
B
Reaction 1
Starting
molecule
Enzyme 2
Reaction 2
Reaction 3
Product
3
Metabolic Pathway
Bioenergetics
Bioenergetics is the study of how organisms
manage their energy resources via
metabolic pathways
Catabolic pathways release energy by
breaking down complex molecules into
simpler compounds
Anabolic pathways consume energy to build
complex molecules from simpler ones
Energy
Forms of Energy
to potential energy.
Chemical
energy
10
Heat
co2
H2O
11
12
Living systems
13
Free Energy
14
Exergonic reactions
Free energy
Amount of
energy
released
(G <0)
Energy
Products
15
Endergonic Reactions
Free energy
Energy
Amount of
energy
released
(G>0)
Reactants
16
Product
Energy
must be
supplied.
Reactant
Reactant
Energy is
released.
Product
Endergonic
Exergonic
17
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G = 0
G < 0
19
20
Energy Coupling
Living organisms have the ability to couple
exergonic and endergonic reactions:
Energy released by exergonic reactions is
captured and used to make ATP from ADP
and Pi
ATP can be broken back down to ADP and
Pi, releasing energy to power the cells
endergonic reactions.
21
-O
O
O
O
CH2
Phosphate groups
HC
O
O
NH2
H
OH
CH
Ribose
OH
22
bond is broken
Inorganic phosphate
Energy
Cellular Work
24
ATP
ADP + P
25
26
Motor protein
Protein moved
(a) Mechanical work: ATP phosphorylates motor proteins
Membrane
protein
ADP
ATP
Solute
Solute transported
Glu +
NH3
NH2
Glu
Product (glutamine)
made
27
Activation Energy
Transition state
Free energy
EA
Reactants
G < O
C
Products
Progress of the reaction
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28
Reaction Rates
29
Energy released
Activation
energy
Activation
energy
Reactant
Reactant
Product
Uncatalyzed
Product
Catalyzed
30
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Free energy
EA
without
enzyme
EA with
enzyme
is lower
Reactants
G is unaffected
by enzyme
Course of
reaction
with enzyme
Products
Progress of the reaction
31
32
Almost all enzymes are globular proteins with one or more active sites on their
surface.
The substrate is the reactant an enzyme acts on
Reactants bind to the active site to form an enzyme-substrate complex.
The 3-D shape of the active site and the substrates must match, like a lock and key
Binding of the substrates causes the enzyme to adjust its shape slightly, leading to
a better induced fit.
Induced fit of a substrate brings chemical groups of the active site into positions
that enhance their ability to catalyze the chemical reaction
When this happens, the substrates are brought close together and existing bonds
are stressed. This reduces the amount of energy needed to reach the transition
state.
Substate
Active site
Enzyme
Enzyme- substrate
complex
33
Substrates
Enzyme-substrate
complex
6 Active site
Is available for
two new substrate
Mole.
Enzyme
5 Products are
Released.
Figure 8.17
Products
2 Substrates held in
active site by weak
interactions, such as
hydrogen bonds and
ionic bonds.
3 Active site (and R groups of
its amino acids) can lower EA
and speed up a reaction by
acting as a template for
substrate orientation,
stressing the substrate bonds
and stabilizing the
transition state,
providing a favorable
microenvironment,
participating directly in the
catalytic reaction.
4 Substrates are
Converted into
Products.
34
Bond
H2O
Active site
Enzyme
Fructose
4 Products are
released, and the
enzyme is free to
bind other
substrates.
35
36
Rate of reaction
20
40
Temperature (C)
(a) Optimal temperature for two enzymes
80
100
37
Optimal pH
for trypsin
(intestinal
enzyme)
Rate of reaction
3
4
0
2
1
(b) Optimal pH for two enzymes
Figure 8.18
38
Enzyme Inhibitors
Substrate
Active site
Enzyme
Competitive
inhibitor
40
Enzyme Inhibitors
A noncompetitive
inhibitor binds to the
enzyme away from
the active site, altering
the conformation of
the enzyme so that its
active site no longer
functions.
Noncompetitive inhibitor
(c) Noncompetitive inhibition
41
43
Active site
(one of four)
Regulatory
site (one
of four)
Activator
Active form
Oscillation
Nonfunctional
active
site
Allosteric activater
stabilizes active from
Inactive form
Inhibitor
Stabilized inactive
form
(a) Allosteric activators and inhibitors. In the cell, activators and inhibitors
dissociate when at low concentrations. The enzyme can then oscillate again.
44
Cooperativity
Substrate
Inactive form
46
47
Feedback Inhibition
Active site
available
Initial substrate
(threonine)
Threonine
in active site
Enzyme 1
(threonine
deaminase)
Isoleucine
used up by
cell
Intermediate A
Feedback
inhibition
Active site of
enzyme 1 no
longer binds
threonine;
pathway is
switched off
Enzyme 2
Intermediate B
Enzyme 3
Intermediate C
Isoleucine
binds to
allosteric
site
Enzyme 4
Intermediate D
Enzyme 5
End product
(isoleucine)
48