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to Metabolism
Chemical
energy
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
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
Reactants
Amount of
energy
released
Free energy
(G 0)
Energy
Products
Products
Amount of
energy
required
Free energy
(G 0)
Energy
Reactants
G 0 G 0
G 0
G 0
G 0
Phosphate groups
Ribose
Energy
(c) Free-energy
change for NH3 NH2
ATP ADP Pi
coupled Glu Glu
reaction
GGlu = +3.4 kcal/mol
GATP = 7.3 kcal/mol
+ GATP = 7.3 kcal/mol
ATP ADP Pi
P Pi
Solute transported
(a) Transport work: ATP phosphorylates transport proteins.
ATP ADP Pi
ATP
Sucrase
C D
Transition state
A B
Free energy
EA
C D
Reactants
A B
G O
C D
Products
Reactants
Course of G is unaffected
reaction by enzyme
with enzyme
Products
Active site
Enzyme Enzyme-substrate
complex
(a) (b)
Catalysis in the Enzyme’s Active Site
• In an enzymatic reaction, the substrate binds to
the active site of the enzyme
• The active site can lower an EA barrier by
– Orienting substrates correctly
– Straining substrate bonds
– Providing a favorable microenvironment
– Covalently bonding to the substrate
Substrates
Enzyme-substrate
complex
Active
site
Enzyme
Figure 8.15-2
1 Substrates enter active site.
2 Substrates are held
in active site by weak
interactions.
Substrates
Enzyme-substrate
complex 3 Active site can
lower EA and speed
up a reaction.
Active
site
Enzyme
4 Substrates are
converted to
products.
Figure 8.15-3
1 Substrates enter active site.
2 Substrates are held
in active site by weak
interactions.
Substrates
Enzyme-substrate
complex 3 Active site can
lower EA and speed
up a reaction.
6 Active
site is
available
for two new
substrate
molecules.
Enzyme
Rate of reaction
bacteria (77°C)
0 60
20 80 40 100 120
Temperature (°C)
(a) Optimal temperature for two enzymes
0 1 5 2 3 4 6 7 8 9 10
pH
(b) Optimal pH for two enzymes
Cofactors
• Cofactors are nonprotein enzyme helpers
• Cofactors may be inorganic (such as a metal in
ionic form) or organic
• An organic cofactor is called a coenzyme
• Coenzymes include vitamins
Active
site
Competitive
inhibitor
Enzyme
Noncompetitive
inhibitor
The Evolution of Enzymes
• Enzymes are proteins encoded by genes
• Changes (mutations) in genes lead to changes
in amino acid composition of an enzyme
• Altered amino acids in enzymes may alter their
substrate specificity
• Under new environmental conditions a novel
form of an enzyme might be favored
Regulatory
site (one
Activator Stabilized active
of four) Inactive form
Active form Stabilized active form form
Oscillation
Non- Inhibitor
Inactive form Stabilized inactive
functional
active site form
• Cooperativity is a form of allosteric regulation
that can amplify enzyme activity
• One substrate molecule primes an enzyme to
act on additional substrate molecules more
readily
• Cooperativity is allosteric because binding by a
substrate to one active site affects catalysis in
a different active site
Enzyme 1
(threonine
Isoleucine
deaminase)
used up by
cell
Intermediate A
Active site of Feedback
enzyme 1 is inhibition Enzyme 2
no longer able
to catalyze the
Intermediate B
conversion
of threonine to Enzyme 3
intermediate A;
pathway is Intermediate C
switched off. Isoleucine
binds to Enzyme 4
allosteric
site. Intermediate D
Enzyme 5
End product
(isoleucine)
Specific Localization of Enzymes Within
the Cell
• Structures within the cell help bring order to
metabolic pathways
• Some enzymes act as structural components
of membranes
• In eukaryotic cells, some enzymes reside in
specific organelles; for example, enzymes for
cellular respiration are located in mitochondria
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