Human Physiology, An Integrated Approach

8th Edition energy

ATP
groups
4

f
Chapter 4
Energy and Cellular
Metabolism

show us harch 2
chemicals breakdown to
make energy
How much energy its
giving me
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About This Chapter
4.1 Energy in Biological Systems
4.2 Chemical Reactions
4.3 Enzymes
4.4 Metabolism

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Table 4.1 Properties of Living Organisms
TABLE 4.1 Properties of Living Organisms

1. Have a complex structure whose basic unit of organization is

the cell

2. Acquire, transform, store, and use energy

3. Sense and respond to internal and external environments

4. Maintain homeostasis through internal control systems with

feedback

5. Store, use, and transmit information

6. Reproduce, develop, grow, and die

7. Have emergent properties that cannot be predicted from the

simple sum of the parts

8. Individuals adapt and species evolve

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4.1 Energy in Biological Systems
• All living organisms need a source of energy
• Plants
– Trap radiant energy from the sun
– Store energy in chemical bonds
• Animals
– Must import energy through ingestion of plants or other animals

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 Figure 4.1 Energy transfer in the
environment world
threadmedl breaking
Hot
Plants trap radiant
energy from the
energy Animals eat the
plants and either glucose sugar
I
sun and store it use the energy
in the chemical or store it.
bonds of Sun
biomolecules.
Heat Energy lost
energy to environment KEY

Transfer of radiant
or heat energy
Radiant
energy Transfer of energy
in chemical bonds

argestion O2 O2 Energy for work

0 491 +

real
Photosynthesis Respiration
CO2 takes place in Energy stored in takes place in Energy stored
plant cells, yielding: biomolecules human cells, yielding: in biomolecules

purist
+
H2O CO2

effve H2O

N2 Llycoga
starch
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Energy is Used to Perform Work
• Energy is the capacity to do work
• Chemical work
– Making and breaking of chemical bonds
• Transport work
– Moving ions, molecules, and larger particles
– Useful for creating concentration gradients
• Mechanical work
– Moving organelles, changing cell shape, beating flagella and cilia
– Contracting muscles

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Energy Comes in Two Forms: Kinetic and
Potential
• Kinetic energy is the energy of motion
• Potential energy is stored energy
– In concentration gradients and chemical bonds
• Energy Can Be Converted From One Form to Another
Transformation efficiency

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Figure 4.2 Kinetic and potential energy

(a) Work is used to push a ball up a (b) The ball sitting at the top of (c) The ball rolling down the ramp is converting the
ramp. Kinetic energy of movement up the ramp has potential energy, potential energy to kinetic energy. However, the
the ramp is being stored in the the potential to do work. conversion is not totally efficient, and some energy is lost
potential energy of the ball’s position. as heat due to friction between the ball, ramp, and air.

Kinetic energy Potential energy Kinetic energy

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Thermodynamic Is the Study of Energy
Use
conserved
• First law of thermodynamics is
energy out or stued
– Law of conservation of energy make seething get snowhone
– Total amount of energy in the universe is constant
• Second law of thermodynamics
– Processes move from state of order to randomness or disorder
(entropy)
disorder
Order

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4.2 Chemical Reactions
• Bioenergetics is the study of energy flow through biological systems
• Chemical reactions
– Reactants become products
– Reaction rate
• Free energy
• Activation energy gets reactions started

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 Energy Is Trapped or Released during
Reactions
• Free energy change of the reaction

oxo – Exergonic reactions – energy producing creates heat

out
end – Endergonic reactions – energy utilizing creates heat in
– Coupling endergonic and exergonic reactions
• Net free energy change determines reaction reversibility
– Reversible vs. irreversible reaction

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 together
things
Adding
Table 4.2 Chemical Reactions
TABLE 4.2 Chemical Reactions

Reactants
Reaction Type (Substrates) Products

Combination A+B → C

Decomposition C → A+B
pygmy
Single L + MX → LX + M
displacement*

Double LX + MY → LY+MX
displacement*

*X and Y represent atoms, ions, or chemical groups.

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Figure 4.3 Activation energy in exergonic
and endergonic reactions
(a) Activation energy
(a) Activation energy is the “push” needed to start a reaction.

Activation energy

Reactants

Starting free
energy level

Products

Final free energy level

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 Figure 4.3b-c Activation energy in
exergonic and endergonic reactions
(b) Exergonic reactions, (c) Endergonic
reactions
(b) Exergonic reactions release energy because the (c) Endergonic reactions trap some activation energy in the
products have less energy than the reactants. products, which then have more free energy than the reactants.

KEY KEY
Reactants Reactants
Activation

Free energy of molecule

energy Activation Activation
of reaction G+H
Free energy of molecule

Activation energy of reaction

Reaction Reaction
A+B process E+F process

Products Net free Products

Net free
energy change
energy
change

C+D
Time
Time

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Figure 4.4 Energy in biological reactions

Energy released by exergonic reactions can be trapped

in the high-energy electrons of NADH,FADH2, or
NADPH. Energy that is not trapped is given off as heat.

Nucleotides capture
and transfer energy
Exergonic reactions release energy. Heat energy and electrons. Endergonic reactions will not
occur without input of energy.

ENERGY
A+B C+D +
released
NADPH

High-energy
ENERGY + E+F G+H
NADH
electrons
ATP

FADH2

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Figure 4.5 Some reactions have large
activation energies
KEY
Reactants

Activation
of reaction
Free energy of molecule

Activation A+B Reaction

energy process

Products
Net free
energy
change

C+D

Time

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 8mW
ose ase

4.3 Enzymes reaction

Protons speed up
done a
• Enzymes speed up the rate of chemical reactions reaction
– Catalysts
– Reactants are called substrates
• Enzymes are proteins (or RNA)
• Isozymes
– Catalyze same reaction, but under different conditions or in
different tissues

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4.3 Enzymes
• Reaction rates are variable
– Amount of substrate or enzyme, temperature
– Reversible reactions go to a state of equilibrium
• Enzymes may be activated, inactivated, or modulated
– Proenzymes or zymogens
– Coenzymes - many vitamins are coenzyme precursors
– Chemical factors, temperature and pH
• Enzymes lower the activation energy of reactions

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 enzyme adds an phosphate
its called tenase
phosphate

Table 4.3 Diagnostically Important When enzyme

takes away a
Enzymes phosphate its
TABLE 4.3 Diagnostically Important Enzymes called
Elevated blood levels of these enzymes are suggestive of the phosphatase
on pathologies listed.

modtisoder Enzyme Related Diseases

a
Acid phosphatase* Cancer of the prostate

corner Alkaline phosphatase Diseases of bone or liver

Homeostatic attend
mm Amylase Pancreatic disease
too
dong told
phosphate
Creatine kinase (CK) Myocardial infarction
(heart attack), muscle
disease
becomes
Lactate dehydrogenase (LDH) Tissue damage to heart,
liver, skeletal muscle, red
blood cells

*A newer test for a molecule called prostate specific antigen (PSA) has
replaced the test for acid phosphatase in the diagnosis of prostate cancer.

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Figure 4.6 pH affects enzyme activity
Most enzymes in humans have optimal activity
near the body's internal pH of 7.4.
Rate of enzyme activity

5 6 7 8 9
pH
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Figure 4.7 Enzymes lower the activation
energy of reactions
Activation energy
without enzyme KEY
Lower activation
Reactants
energy in presence
of enzyme
Activation
of reaction

Reaction
process
Free energy of molecule

A+B
Products

C+D

Time

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Enzymatic Reactions Can Be Categorized
• Phosphorylation – addition of a phosphate group
• Oxidation-reduction reactions
– Reduced – gains electrons
– Oxidized – loses electrons
• Hydrolysis-dehydration reactions
– Dehydration reactions – water is a product
– Hydrolysis reactions – with addition of water
breaks down w water

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 Enzymatic Reactions Can Be Categorized
• Addition-subtraction-exchange reactions
– Addition reaction – adds a functional group
– Subtraction reaction – removes a functional group
– Exchange reaction – functional groups are exchanged
– Kinases – add a phosphate group

Free
– Deamination – remove an amino group
– Amination – add an amino group
– Transamination – transfer an amino group
sniff • Ligation reactions
– Synthases join two molecules together

T
brings molecules together
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Table 4.4 Diagnostically Important
Enzymes
TABLE 4.4 Classification of Enzymatic Reactions
Reaction Type What Happens Representative Enzymes

1. Oxidation-reduction Add or subtract electrons Class:* oxidoreductase

(a) Oxidation Transfer electrons from donor to oxygen Oxidase
Remove electrons and H+ Dehydrogenase
(b) Reduction Gain electrons Reductase

2. Hydrolysis-dehydration Add or subtract a water molecule Class:* hydrolase

(a) Hydrolysis Split large molecules by adding water Peptidases, saccharidases, lipases
(b) Dehydration Remove water to make one large molecule from Dehydratases
several smaller ones

3. Transfer chemical groups Exchange groups between molecules Class:* transferases

Add or subtract groups Class:* lyases
(a) Exchange reaction Phosphate Kinase
Amino group (transamination) Transaminase
(b) Addition Phosphate (phosphorylation) Phosphorylase
Amino group (amination) Aminase
(c) Subtraction Phosphate (dephosphorylation) Phosphatase
Amino group (deamination) Deaminase

4. Ligation Join two substrates using energy from ATP Class:* ligases
Synthetase

*Enzyme classes as defined by the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology.

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 breakdown
4.4 Metabolism
• All chemical reactions that take place in an organism
• Catabolism – energy-releasing breakdown
• Anabolism – energy-utilizing synthesis
• Kilocalories – energy released from or stored in chemical bonds
acids
• Molecules in pathways are intermediates fatty
famous stoord
ex
much energy builder
you that body steroids
give
type of in yourbody
you inject if its anabolic
understand
catabolic

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Figure 4.8 Metabolic pathways resemble a
road map
(a) Section of Road Map (b) Metabolic Pathways Drawn Like a Road Map

Seligman Glycogen
Flagstaff
40
Williams 40 Winslow

Sedona
17 Holbrook Glucose Glucose 6-phosphate
Prescott

Fructose 6-
17
Payson phosphate
Wickenburg
Carefree
Ribose 5-
Fructose Fructose 1-phosphate phosphate
10 Glendale Scottsdale Fructose 1,6-
Mesa Globe
PHOENIX bisphosphate
Tempe Superior
Maricopa
Gila Bend 10 Florence
Casa
8
Grande Glycerol
10 DHAP
Glucose 3-phosphate
Ajo
Tucson
Three Points
DHAP = dihydroxyacetone phosphate

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Cells Regulate Their Metabolic Pathways
1. Controlling enzyme concentrations
2. Producing modulators that change reaction rates
– Feedback inhibition
3. Using different enzymes to catalyze reversible reactions
4. Compartmentalizing enzymes within organelles
5. Maintaining optimum ratio of ATP to ADP

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Figure 4.9 Feedback inhibition

enzyme 1 enzyme 2 enzyme 3

A B C Z

Feedback inhibition

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Figure 4.10 Enzymes control reversibility
of metabolic reactions

Reversible Reactions Irreversible Reactions

(a) Some reversible reactions (b) Reversible reactions requiring (c) Irreversible reactions lack
use one enzyme for both two enzymes allow more the enzyme for the reverse
directions. control over the reaction. direction.

CO2 + H2O Glucose + PO4 Glucose + PO4

Carbonic Carbonic glucose 6- hexokinase

hexokinase
anhydrase anhydrase phosphatase

Carbonic acid Glucose 6-phosphate Glucose 6-phosphate

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ATP Transfers Energy between Reactions
• High-energy phosphate bond
• Aerobic metabolism
– One glucose molecule can yield 30-32 ATP
• Anaerobic metabolism makes two ATP
• Catabolic pathways produce ATP
– Glycolysis
– Citric acid cycle
– Electron transport system

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glucose
 cytoplasm g
Glycolysis
blood individual cell cytoplasm cytoplasm
breakdown glucose
energy mitochondria
Figure 4.11 ATP Production o
Glucose
The catabolic pathways that extract

Siii
energy from biomolecules and
transfer it to ATP are summarized NAD+
G
in this overview figure of aerobic L
respiration of glucose. Y NADH
Glycerol
C
O
L ADP
Jejunum Amino
Y
metamin intestines
Duodenum acids S
I
ATP
NAVIGATOR
S
small
hfm
Glycolysis and the citric acid cycle Glucose
belly produce small amounts of ATP
directly, but their most important Amino Pyruvate
units contributions to ATP synthesis are acids Cytosol
down high-energy electrons carried by
NAD+
break NADH and FADH2 to the electron
Pyruvate
transport system in the mitochondria.
hose NADH Mitochondrion Acetyl CoA

g brought whereveryouneed Fatty acids Acetyl CoA Citric acid

sugar mitochondria cycle

cell cytoplasm High-energy

electrons

ADP ETS

Amino
CITRIC
acids ACID ATP
This icon represents the
CYCLE different steps in the
metabolic summary
figure. Look for it in the
figures that follow to help
Aerobic Metabolism of Glucose CO2 you navigate your way
The energy production from one through metabolism.
glucose molecule can be summarized
in the following two equations. High-energy electrons
and H+

Glucose + O2 + ADP + Pi CO2 + H2O + ATP

ELECTRON TRANSPORTSYSTEM
ADP
outside cell
ATP
30–32 ADP + Pi 30–32 ATP

C6H12O6 + 6 O2 6 CO2 + 6 H2O O2 H2O

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 have to use ATP

group A pagain
Figure 4.12 Glycolysis phosphate
carbon group
distension
During glycolysis, one molecule of 16 Transfer carbon
76
glucose is converted by a series
of enzymatically catalyzed GLUCOSE
reactions into two pyruvate
molecules, producing a
net release of energy. ATP
group
1 Glucose is phosphorylated to
ADP P
glucose 6-phosphate. (The “6”
in glucose 6-phosphate tells
phosphate
itself Srmg
you that the phosphate group
Glucose 6-phosphate
has been attached to carbon 6
of the glucose molecule.)
NAVIGATOR

rearrange
Glucose
P
2
so its homeostatic
a
Key Features of Glycolysis
Fructose 6-phosphate

ATP • In glycolysis, one 6-carbon

3 molecule of glucose becomes two
3-carbon pyruvate molecules.
Pyruvate
attachment ADP P P

Fructose 1,6- • Two steps of glycolysis require

bisphosphate energy input from ATP. Other step
strap energy in ATP and the

howm
high-energy electrons of NADH.
4
P

Ekins
• Glycolysis does not require

PEPYS
Dihydroxyacetone
oxygen. It is the common pathway
phosphate
for aerobic and anaerobic catabo-
lism of glucose.

move
looklike fiae
2 Glyceraldehyde 3-phosphate2
P te group energy
through
I P
NAD +

NADH
5 Steps 5–9 occur twice for each
glucose that begins the
dam this
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pathway.
Takesmitochondria
teamingto sand
P
2 1,3-Bisphosphoglycerate

ATPwet
2

wyygf.fm
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much
6
ATP
Phosphatening

KEY
2 3-Phosphoglycerate
2
P
make
stiffestwww.yahoo.ipnospnate.AE
= Carbon 7
= Oxygen
P
P = Phosphate group
2 2-Phosphoglycerate
2
(side groups not shown)

tophosphategroup

dggngyyyyy
H2 O
P
2 Phosphoenol
pyruvate 2

ADP
9 Pyruvate is the branch point for
aerobic and anaerobic
ATP
metabolism of glucose.

qgii.gg
magggy yyggygggg.gg
2 Pyruvate 2

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characteristic
 P
II pyruvatesend product of
glycolysis

Figure 4.13 Pyruvate, Acetyl CoA, and the

Citric Acid Cycle onlyhogy Pffganoughfromsuch
2x pyruvate

KM Pyruvate
Cytosol
1 If the cell has adequate
oxygen, pyruvate is
transported into the

aoanaaee.f.netifif
1

thirteen
mitochondria.

refortified Pyruvate

2
Mitochondrial
matrix
2 Pyruvate reacts with
coenzyme A to produce
acetyl CoA, one NADH,

of
NAD+ and one CO2.

presence
NADH
within oxygenffy
to
3

dontlike
Acetyl CoA has two
CoA 4 parts: a 2-carbon acyl
CO2 unit, derived from
pyruvate, and

Aerobffporton Acetyl CoA

3 bitaminteraces
coenzyme A.
CoA
more breathing canbecome
20mm 4 Coenzyme A is made
from the vitamin efficient
oxygentodryyourself
NAVIGATOR Acyl unit getsrecycled pantothenic acid.
Coenzymes, like

breathdeeplyqualityoxygen
enzymes, are not
changed during

fee
reactions and can be

takeyoutothislevel
5
reused.
Citrate (6C)

sagging
0 if
6
Oxaloacetate (4C) 5 The 2-carbon acyl unit
Pyruvate enters the cycle by
combining with a

IE
Acetyl CoA 4-carbon oxaloacetate
NADH molecule.

Citric acid

Trait
NAD+

www.gfhnafe
cycle
6 The 6-carbon citrate
Malate (4C)
molecule goes through
NAD+ 7

www.teddd
High-energy a series of reactions
electrons until it completes the
CITRIC ACID CO2 cycle as another

Taffeta
NADH
CYCLE oxaloacetate molecule.

want
H2O

wet
NADH Fumarate (4C)
FADA
molecule  Ketoglutarate (5C)
7 Two carbons are
removed in the form
of CO2.

888d
NAD+ CO2
FADH2

8 NADH 8 Most of the energy

notever CO mÑ
FAD
ADP
ATP
CoA
released is captured as
high-energy electrons
on three NADH and one
pH
FADH2. Some energy
Succinate (4C) Succinyl CoA (4C)
goes into the
GTP CoA high-energy phosphate
GDP + Pi bond of one ATP. The
remaining energy is
KEY

Treat
given off as heat.
= Carbon CoA = Coenzyme A CoA

= Oxygen (Side groups not shown)

recycled
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ridofCoA
CoA be aplaceholder
 pyruvate

2ATP 2x NADH
notento cycle wo
present
Mitochondria oxygen

Tpyruvate acetyl CoA DADH

2xcitricakivaple6KNAD.IQ
2AP
TCAmeanscitricacidcycle FADAN
2
 Figure 4.14 The Electron Transport System
1 NADH and FADH2 2 Energy released when 3 By the end of 4 Each pair of 5 As H+ move down their concentration
release high- pairs of high-energy the ETS, the electrons released gradient through a protein known as
energy electrons electrons pass along the electrons have by the ETS ATP synthase, the synthase
and H+ to the ETS. transport system is used given up their combines with two transfers their kinetic energy to the
NAD+ and FAD are to concentrate H+ from the stored energy. H+ and an oxygen high-energy phosphate bond of ATP.
coenzymes that mitochondrial matrix in the atom, creating a
recycle. intermembrane space. molecule of water, • Each 3 H+ that shuttle through the
The H+ concentration H2O. ATP synthase make a maximum of
gradient is a source of 1 ATP.
potential energy.
• A portion of the kinetic energy is
released as heat.

ATP
CITRIC
ACID
Mitochondrial matrix
ftp.fffasenesy
CYCLE electrons
2 H2O 4 O2 + Matrix pool of H+
e–

Innerprotein capture
synthesize ATP
ATP
H
1
–
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energy to
–
–
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High-energy electrons –
+
– +
ATP
synthase +
+
– +
–
– +
– H+
– 3
– 2 – +
– – – +
– – +
+ H+
H+

III
+ H+
+ +
+ + +
+
+ +

H+ H+
H+ H+

quicker H+
H+

energy
H+
Inner

take ATP mitochondrial

membrane

drove quickly
energy passed High-energy electrons
Outer
mitochondrial
membrane
standates from glycolysis
Cytosol

electron ATP
make
to
ATP Mfhqffn startATP synthase
µ Copyright © 2019, 2016, 2013 Pearson Education, Inc. All Rights Reserved
 Glycolysis
www.MEEERGY.wegmxsfmfe
71 1 211 says
ATP

Figure 4.15 Energy yields from catabolismKHEIMET

of one glucose molecule 5k GNADHX2si
Is.oAt Z APHxI.SATP
(a) Anaerobic Metabolism C6H12O6 2 C3H5O3– + 2 H+ (b) Aerobic Metabolism C6H12O6 + 6 O2 6 CO2 + 6 H2O

wkf.gghy
One glucose metabolized One glucose metabolized aerobically through
anaerobically yields only 2 ATP. the citric acid cycle yields 30–32ATP.

Elisa
1 Glucose NADH FADH2 ATP CO2 1 Glucose NADH FADH2 ATP CO2
G G

MT
L L
Y Y

am C
O
L
2
4 C
O
L
2*
+4
–2 sina.IE
Y –2 Y
S S
I I
S
2 Pyruvate
S
2 Pyruvate
Meat'Tered
–2 2 2
2 Lactate 2 Acetyl CoA

TOTALS 0
NADH
2
ATP
Citric
acid
cycle
6 2 2 4 IÑÉMet
count
bitney
NADH 2 SK 6 O2
High-energy electrons
and H+

faithful're
T FADHQ
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SYSTEM

TOTALS 6
26–28

30–32 6
true
H2O ATP CO2
capture
* Cytoplasmic NADH sometimes yields only
1.5 ATP/NADH instead of 2.5 ATP/NADH.
energy
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Figure 4.16 Aerobic and anaerobic
metabolism
Pyruvate is the branch point between aerobic
and anaerobic metabolism of glucose.

NAD+ NADH
glycolysis no oxygen
Anaerobic Aerobic
Pyruvate

Tooxygnamates lactateYOU LOSE

Lactate

Pyruvate

NADH
Cytosol
Sue pushoutlactic acid
CoA
no room to doglycolysis
Mitochondrial saeness beataway
Acetyl CoA
matrix
CoA
lactic acid
produe on
hr of respiratics

mitochondria
building
Acyl unit
up
CITRIC ACID doingthingsprogressive
CYCLE
do a littlebiteveryday

KEY AdjustingI
= Carbon CoA = Coenzyme A tryto getsystem in
= Oxygen H and –OH not shown shape
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 thanhow to digest sugars no

Proteins Are the Key Role to Cell Function

chickentofu fishbeef
• Variability and specificity
• The protein “alphabet”
– 20 amino acids
– Sequence & number of amino acids give rise to different proteins
– Codon – three bases encoding one amino acid

Proton syntheers

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 essential lookat an acids 4 possibilities its ex.by
thatmpater
Ala
needpossible combinations to getthatammoacid
Figure 4.17 The genetic code as it appears in
the codons of mRNA male protons

ftp.go.amstornd The three-letter abbreviations to the right of the

brackets indicate the amino acid each codon
unstable blogger.is 5
vac.im RNAcovid
represents. The start and stop codons are also marked.

expose
Second base of codon iffthirsase
U C A G
nts
U
How is m that.TT
setralmpatn ffems
UUU
Phe
UCU UAU
Tyr
UGU
Cys
C
U UUC UCC UAC UGC

ygKodos
Ser
UUA UCA UAA UGA Stop A
Leu Stop
UUG UCG UAG UGG Trp G

U
mutation
CUU CC U CAU CGU
indicatestop
First base of codon

His C
CUC CCC CAC CGC

Third base of codon

codons C
stop CUA
Leu
CCA Pro CAA CGA
Arg
A
transcription CUG CC G CAG Gln CGG
G Paturalprotection
amino
AUU ACU AAU AGU
U central
AUC IIe Asn Ser C
A AUA ACC
Thr
AAC AGC acid
ACA AAA AGA A
AUG Met Lys AGG Arg
addthis.ME eftafdfne
ACG AAG G
Start
U
WOBBLE THEORY
88
GUU GCU GAU GGU
Asp C
G GUC Val
GCC
Ala
GAC GGC
Gly
GUA GCA GAA GGA A
Glu
GUG GCG GAG GGG G no matter codon

whathappens codeforthe
Copyright © 2019, 2016, 2013 Pearson Education, Inc. All Rights some ammo
Reserved acid
genetic code
 know how to
Lets make a proton
mRNA 3

FAUC AUG AGG GGG GAU UAG AAAA

1
www.www I
FEW A 57080

In exons giveyou MRNA wobbletheory

mistakes
make protem anytime make

yonysorceofpantshaetrytgho trytoph.cn
hard because only rare
very
in plants

of
all 20 implements
amino acid
to complete
synthesis
protein

make sure eating

complements haltrytophan
Unlocking DNA’s Code
• Gene – region of DNA  RNA
– Constitutively active genes continuously converted to RNA
Regulated genes are turned on (induced) and off (repressed)
• Transcription – DNA  RNA
– Synthesis of messenger RNA (mRNA), transfer RNA (tRNA),and
ribosomal RNA (rRNA)
• Translation – mRNA  protein
– Assembly of amino acids into a protein chain
• Post-translational modifications

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Figure 4.18 Overview of Protein Synthesis
The major steps required to convert the
genetic code of DNA into a functional protein.

Gene Regulatory proteins

1
GENE ACTIVATION

Constitutively Regulated
active activity

Induction Repression

2 TRANSCRIPTION
(see Fig. 4.19)

siRNA
mRNA

3 mRNA PROCESSING Alternative

splicing Interference
(see Fig. 4.20)

mRNA “silenced”
Processed
mRNA

Nucleus

Cytosol
• rRNA in ribosomes
• tRNA
• Amino acids
4 TRANSLATION
(see Fig. 4.21)

Protein chain

5 POSTTRANSLATIONAL
MODIFICATION Folding and Cleavage into Addition of groups: Assembly into
cross-links smaller peptides • sugars polymeric proteins
• lipids
• –CH3
• phosphate

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DNA Guides the Synthesis of RNA
• Production of mRNA
– DNA template strand
– RNA polymerase
– Promoter
– Transcription factors

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Alternative Splicing Creates Multiple
Proteins from One DNA Sequence
• mRNA processing
– RNA interference
– Alternative splicing
▪ Exons encode proteins
▪ Introns are noncoding segments of genes

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Figure 4.19 Transcription Double
bonded DNA
proteins
tomake
A gene is a segment of DNA that can produce a functional ready
piece of RNA, which in turn can make a protein. Base RNA
pairing is the same as in DNA synthesis, except that the polymerase
base uracil (U) substitutes for thymine (T).

1 RNA polymerase bindsto DNA.

50mopenDNA only onestrandactslikely

2 The section of DNA that contains
the gene unwinds.

RNA bases

make RNAmake a cham 8keepleading

stand gene 3 RNA bases bind to DNA,
creating a single strand of mRNA.

Template
strand Site of
nucleotide assembly

Kafka DNA

DNA
buk
crops
Lengthening
mRNA strand

around
NUCLEUS
mRNA
transcript
RNA
polymerase gene foisted
4 mRNA and the RNA polymerase
detach from DNA, and the
mRNA goes to the cytosol after
processing.
DNA isoesbacktogether
RNA
polymerase
mRNA strand
released

Leaves nucleus mRNA mousecytad

after processing

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 Figure 4.20 mRNA processing
only setstands
In mRNA processing, segments of the newly
areas body
protegapiomotorsignal that
Gene
wine serfond
gene
created mRNA strand called introns are
removed. The remaining exons are spliced
back together to form the mRNA that Template
codes for a functional protein. strand
RNAPolymerase sensegene ATCGATCGATCGY.IN
UAGC prod
UAGC
melmm RNA UAGC
extake
odutff.ge
The promoter segment of DNA is not
Jhpresented
yntigg.it
GCTAGCTA6Cn f
transcribed into RNA.
why ftp.atmfproter
mmgdefh aff a
Promoter Transcribed section
yft.mfhf.nl DNA a b c d e f g h i
hecanmanipulate

TRANSCRIPTION
nanites
Tyndall
ftp.ffnasettletranscriet matemfrkf
Unprocessed
mRNA A B C D E F G H I

C TRNA
mRNA Processing
D
may produce two H
proteins from one
gene by simmernottesare
Introns removed
alternative splicing. Introns removed
Removing different introns from mRNA
allows a single gene to code for multiple
proteins. For protein #1, introns A, C, G, and
RNAundergochanges
I were removed. For protein #2, segments B,
D, F, and H became the introns.
B D E F H A C E G I
forbody to
Exons for protein #1 Exons for protein #2 change

Eta Rita Introns

remainexons
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nucleus
 S p
transcribed
sense hnRNA
DMA remove interns
Splicing
keep exons

mRNA Translation Links Amino Acids introns removed

• Protein synthesis gametship'isedHartly mRNA

Individualsbornw dont the
– mRNA template e to nmfifhhfgg.org
hair changesplicing
differentpygmisms
– Ribosomes
▪ rRNAs and proteins
– tRNA with anticodon
has gg ralPosfi iiQ
▪ binds to mRNA codon
▪ carries amino acid to peptide chain
– Dehydration synthesis forms peptide bonds
• Protein sorting directs proteins to their destination
– signal sequence

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 3 HMapper
trancoption

nucleus post modification

NUCLEUS
mRNA 7 READYTOLEAVE
sense
DNA
thy mRNA into
move process.in
1
spring extrons
t
many
transcription
zipolyagffin.mg
EE iife'a 9nd3AAphetoil
I'ht
time
io
If acid
bringingamino

hnRNA
affiliation
forfeit.com singleaminoacid

IIEII.IE
aEinfa.maacmnem.artat

To fityouneed3 setsof
codons

jfftp.fffygmgafm
gf ff
ÉÑ
fffffÑff É take OHMMETER

PEPTIDE
NA

codonentersRNA
ftp.t.it eahihiammtf'may b
mRNA
polypeptide

I aiii
at.tn
san
fi iEttntiEet
pf adf.gg bufferactivitt
foodhelps

in ieiittsror
PEE L ftp.igffimEiai iii Tetracycline teeth
yellowyour
tightfisted'ation

TRANSLATION
Apt ER
modification
RERpost translational
Addsugarfats
vitamins
Raedophffin functional
gets Italthffly

ppHTU

invesicks
lysfzyme
p eroxisomes
Figure 4.21 Translation
Translation matches the codons of RNA
with amino acids to create a protein.

DNA

1
Transcription
RNA
polymerase

2 Nuclear
mRNA processing membrane

Processed mRNA leaves the nucleus

and associates with ribosomes.

3 Attachment of
ribosomal subunits

Amino acid
Incoming tRNA
tRNA bound to an
4 amino acid
Translation Growing peptide
chain Lys

Asp

Phe Trp
Outgoing
“empty” tRNA

Anticodon
A A G A C C

G A U A A
U U C U G G A

mRNA Ribosome

mRNA Each tRNA molecule attaches at one end to a specific

5 Termination amino acid. The anticodon of the tRNA molecule pairs
with the appropriate codon on the mRNA, allowing
amino acids to be linked in the order specified by the
Ribosomal Completed mRNA code.
subunits peptide

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BioFlix: Protein Synthesis

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Proteins Undergo Posttranslational
Modification
1. Protein folding
2. Cross-links
3. Cleaved
4. Add other molecules or groups
5. Assemble into polymeric proteins

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Summary
4.1 Energy in Biological Systems
4.2 Chemical Reactions
4.3 Enzymes
4.4 Metabolism

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