Chapter 2: Enzyme: Activation Energy

3/4/2018
Chapter 2: Enzyme
Lecturer: Dr. Vu Tran Khanh Linh

Department of Food Technology
Email: linhvtk@hcmute.edu.vn
Activation Energy
Transition state:
a fleeting molecular moment
in which events such as bond
breakage, bond formation,
and charge development have
proceeded to the precise point
at which decay to either
substrate or product is equally
likely
a high-energy state
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Activation energy and reaction rate

Activation energies are energy barriers to chemical reactions.
These barriers are crucial to life itself.
The higher the activation energy, the ……….. the chemical
reaction will be
Many reactions have such high activation energies that they
basically don't proceed at all without an input of energy
Activation energy and reaction rate

The activation energy of most chemical reactions taking place
in cells is too high for the reactions to proceed significantly at
ambient temperature.
the process of speeding up a reaction by reducing its
activation energy:
the factor added to lower the activation energy (without
being a reactant):
biological catalysts:
Over the course of evolution, enzymes have developed to

lower activation energies selectively for reactions that are
needed for cell survival.
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An Introduction to Enzymes
Enzymes:
the most remarkable and highly specialized proteins
have extraordinary catalytic power
have a high degree of specificity for their substrates,
are central to every biochemical process:
The study of enzymes has immense practical importance.

Enzymes are also important practical tools in
………………………………………………………………………………………….
History of Enzyme Research

late 1700s: Biological catalysis was first recognized and
described in studies on the digestion of meat by secretions of
the stomach
1800s: examinations of the conversion of starch to sugar by
saliva and various plant extracts
1850s: Louis Pasteur concluded that fermentation of sugar into
alcohol by yeast is catalyzed by “ferments.” He postulated that
these ferments were inseparable from the structure of living
yeast cells
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History of Enzyme research

1987:
Eduard Buchner discovered that yeast extracts could
ferment sugar to alcohol fermentation was promoted by
molecules that continued to function when removed from
cells.
Frederick W. Kühne later gave the name enzymes (from the
Greek enzymos, “leavened”) to the molecules detected by
Buchner.
1926: James Sumner postulated that all enzymes are proteins
Most Enzymes are Proteins

All enzymes are proteins (exception: )
Their catalytic activity depends on the integrity of their native

protein conformation:
catalytic activity is usually lost If an enzyme is denatured or
dissociated into its subunits.
the primary, secondary, tertiary, and quaternary structures
of protein enzymes are essential to their catalytic activity.
Molecular weights: 12,000 – 1,000,000
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Enzyme cofactors:
either one or more inorganic ions, such as Fe2+, Mg2+, Mn2+,
or Zn2+
coenzymes:
non-protein organic molecules
act as transient carriers of specific functional group
Most are derived from vitamins
Some enzymes require both a coenzyme and one or more

metal ions for activity
prosthetic group: a coenzyme or metal ion that is very tightly
or even covalently bound to the enzyme protein
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Apoenzyme/Apoprotein Cofactor Holoenzyme

(protein portion), (nonprotein portion), (whole enzyme),
inactive activator active
holoenzyme : a complete, catalytically active enzyme

together with its bound coenzyme and/or metal ions
apoenzyme or apoprotein : the protein part of such an
enzyme
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Enzymes Are Classified by the Reactions They Catalyze

Many enzymes have been named by adding the suffix “-ase” to
the name of their substrate or to a word or phrase describing
their activity
Urease
DNA polymerase
Other enzymes were named by their discoverers for a broad
function, before the specific reaction catalyzed was known.
E.g. pepsin, lysozyme
Sometimes the same enzyme has two or more names, or two
different enzymes have the same name
International Classification of Enzymes
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System for naming and classifying enzymes:
This system divides enzymes into six classes, each with
subclasses, based on the type of reaction catalyzed
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Each enzyme is assigned a four part classification number
and a systematic name, which identifies the reaction it
catalyzes
A complete list and description of the thousands of known
enzymes is maintained by the Nomenclature Committee of
the International Union of Biochemistry and Molecular
Biology
www.chem.qmul.ac.uk/iubmb/enzyme
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Formal systematic name:

ATP : glucose phosphotransferase
E.C number: EC.2.7.1.1

(2): class name (transferases);
(7): subclass (phosphotransferase)
(1): a phosphotransferase with a hydroxyl group as
acceptor
(1): D-glucose as the phosphoryl group acceptor
Trivial name: hexokinase
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How Enzymes Work

A simple enzymatic reaction might be written:
E: enzyme,
S: substrate
P: product,
ES, EP: transient complexes of E with S and with P.
An enzyme-catalyzed reaction takes place within the
confines of a pocket on the enzyme called the active site
The function of enzymes is to lower the activation energy,
enhancing reaction rates by a factor of 105 – 1017
Catalysts do not affect reaction equilibria.
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How Enzymes Work

Active site:
the region that binds the substrates (and the cofactor, if
any)
formed by groups that come from different parts of the
amino acid sequence
the substrate is held in the active site by weak interactions
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How Enzymes Work

A Few Principles Explain the Catalytic Power and Specificity of
Enzymes:
1. The rearrangement of covalent bonds during an enzyme-
catalyzed reaction
catalytic functional groups on an enzyme (‘’’’’’’’’’’’’’’’’’’’’’’’
’’’’’’’’’’’’’’’’’’’’’’’’’’’’’’’’’’’’’’’’’’’’’’’’’’’’’’’’’’’’’’’’’’’’’’’) may form a
transient covalent bond with a S and activate it for a
reaction, or
a group may be transiently transferred from S to E
Covalent interactions between enzymes and substrates
lower the activation energy by providing an alternative, lower-
energy reaction path.
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How Enzymes Work

A Few Principles Explain the Catalytic Power and Specificity of
Enzymes:
2. the noncovalent interactions between E and S
formation of ES complex release of a small amount of

free energy that stabilizes the interaction (binding energy, ∆GB)
lower the activation energies of the reactions
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Optimal interactions between substrate and

enzyme occur only in the transition state.
FIGURE 6–5 An imaginary enzyme (stickase) designed to catalyze breakage of a metal stick.
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How Enzymes Work

Roles of binding energy:
1. holds the substrates in the proper orientation to react
2. desolvation of the substrate
3. The enzyme usually undergoes a change in conformation
when the S binds, induced by multiple weak interactions with
the substrate induced fit
serves to bring specific functional group on the enzyme into
the proper position to catalyze the reaction.
new enzyme conformation has enhanced catalytic properties.
The important principle is that weak binding interactions

between the enzyme and the substrate provide a substantial
driving force for enzymatic catalysis.
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3/4/2018

Lecturer: Dr. Vu Tran Khanh Linh

Activation energy and reaction rate

Activation energy and reaction rate

Over the course of evolution, enzymes have developed to

The study of enzymes has immense practical importance.

History of Enzyme Research

History of Enzyme research

Most Enzymes are Proteins

Their catalytic activity depends on the integrity of their native

Molecular weights: 12,000 – 1,000,000

Most Enzymes are Proteins

Some enzymes require both a coenzyme and one or more

Most Enzymes are Proteins

Most Enzymes are Proteins

Most Enzymes are Proteins

Apoenzyme/Apoprotein Cofactor Holoenzyme

holoenzyme : a complete, catalytically active enzyme

Enzymes Are Classified by the Reactions They Catalyze

Enzymes Are Classified by the Reactions They Catalyze

Enzymes Are Classified by the Reactions They Catalyze

Enzymes Are Classified by the Reactions They Catalyze

Formal systematic name:

E.C number: EC.2.7.1.1

How Enzymes Work

How Enzymes Work

the substrate is held in the active site by weak interactions

How Enzymes Work

How Enzymes Work

formation of ES complex release of a small amount of

Optimal interactions between substrate and

How Enzymes Work

The important principle is that weak binding interactions

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