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ENZYMES AND
VITAMINS
Catalysis by Enzymes
Classification of Enzymes
Enzymes Regulation
Vitamins and Minerals
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Enzymes
• is a compound, usually a
protein, that acts as a catalyst
for a biochemical reaction.
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Enzyme Structure
• Simple Enzyme – composed
only of protein (amino acid
chain)
• Conjugated Enzyme – has a
nonprotein part in addition to a
protein part
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Enzyme Structure
•Apoenzyme – protein part of a
conjugated enzyme
•Cofactor – nonprotein part of a
conjugated enzyme
•Holoenzyme – is the biochemically
active conjugated enzyme produced
from apoenzyme and cofactor
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Catalysts
• accelerate the rates of
chemical reactions but at the
end of the reaction have
undergone no change
themselves
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NOMENCLATURE AND
CLASSIFICATION
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Enzyme Naming Process

1. the suffix –ase identifies a
substance as enzyme
2. type of reaction catalyzed by
an enzyme is often noted
with a prefix.
ex. oxidase - catalyzes oxidation reaction
hydrolase - catalyzes hydrolysis reaction
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Enzyme Naming Process

3. The identity of the substrate
is often noted in addition to
the type of reaction
Ex. glucose oxidase,
pyruvate carboxylase,
succinate dehydrogenase
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CLASSIFICATION OF
ENZYMES
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Oxidoreductases
catalyze oxidation–reduction reactions of
substrate molecules, most commonly
addition or removal of oxygen or hydrogen
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Main Classes and

Subclasses of Enzymes
Selected Type of Reaction
Main Class
Subclass Catalyzed
Oxidases • oxidation of a substrate
Reductases • reduction of a substrate
Dehydrogenases • Introduction of double
bond by removal of two
Oxidoreductases
H atoms from a
substrate, with H being
accepted by a
coenzyme
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Transferases
catalyze transfer of a group from one
molecule to another
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Main Classes and

Subclasses of Enzymes
Selected Type of Reaction
Main Class
Subclass Catalyzed
Transaminase • Transfer of amino group
between substrates
Transferase Kinases • Transfer of a phosphate
group between
substrates
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Hydrolases
• catalyze the hydrolysis of
substrates—the breaking of
bonds with addition of water
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Main Classes and

Subclasses of Enzymes
Selected Type of Reaction
Main Class
Subclass Catalyzed
Lipases • Hydrolysis in ester
linkages in lipids
Proteases • Hydrolysis of amides
linkages in protein
Nucleases • Hydrolysis of sugar-
Hydrolase phosphate ester bond
in carbohydrate
Carbohydrases • Hydrolysis of glycosidic
bonds on carbohydrate
Phosphatases • Hydrolysis of phosphate
ester bond
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Main Classes and

Subclasses of Enzymes
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Lyases
• (from the Greek lein, meaning “to break”) catalyze
the addition of a molecule such as H2O or CO2 to
a double bond or the reverse reaction in which a
molecule is eliminated to leave a double bond
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Main Classes and

Subclasses of Enzymes
Selected Type of Reaction
Main Class
Subclass Catalyzed
Dehydratases • Removal of H2O from a
substrate
Decarboxylases • Removal of CO2 from a
substrate
Lyases Deaminases • Removal of NH3 from a
substrate
Hydratases
• Addition of H2O from a
substrate
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Main Classes and

Subclasses of Enzymes
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Isomerases
catalyze the isomerization (rearrangement of
atoms) of a substrate in reactions that have
but one substrate and one product
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Main Classes and

Subclasses of Enzymes
Selected Type of Reaction
Main Class
Subclass Catalyzed
Racemases • Conversion of D-isomer
to L-isomer or vice
versa
Isomerases Mutase • Transfer of functional
group from one position
to another in the same
molecule
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Main Classes and

Subclasses of Enzymes
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Ligases
• (from the Latin ligare, meaning “to
tie together”) catalyze the bonding
together of two substrate
molecules
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Main Classes and

Subclasses of Enzymes
Selected Type of Reaction
Main Class
Subclass Catalyzed
Synthetase • Formation of new bond
between two
substrates, with
participation of ATP
Ligase Carboxylase • Formation of a new
bond between a
substrate and CO2 with
participation of ATP
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Main Classes and

Subclasses of Enzymes
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MODELS OF ENZYME
ACTIONS
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Active site
•pocket in an
enzyme with the
specific shape
and chemical
make up
necessary to
bind a substrate
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Substrate
•reactant in an
enzyme
catalyzed
reaction.
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Enzyme-Substrate
Complex
•is the intermediate
reaction species
that is formed
when a substrate
binds to the active
site of an enzyme
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Lock-and-Key Model
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Induced-Fit Model
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Specificity
•limitation of the
activity of an
enzyme to a
specific substrate,
specific reaction,
or specific type of
reaction.
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Absolute Specificity
•the enzyme will catalyze only
one reaction
Group Specificity
•the enzyme will act only on a
specific functional group
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Linkage Specificity
•Will act on a particular type of
chemical bond
Stereochemical Specificity
•will only act on a particular
stereoisomer
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Turnover number
maximum number of substrate molecules
acted upon by one molecule of enzyme per
unit time
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Cofactor
•A nonprotein part of an enzyme that
is essential to the enzyme’s catalytic
activity; a metal ion or a coenzyme.
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Coenzyme
• organic molecule that acts as
an enzyme cofactor.
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HOW ENZYMES WORK

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Induced-fit model
• A model of enzyme action in which
the enzyme has a flexible active
site that changes shape to best fit
the substrate and catalyze the
reaction
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enzymes act as catalysts because of their ability to

1. Bring substrate(s) and catalytic sites together

(proximity effect)
2. hold substrate(s) at the exact distance and in
the exact orientation necessary for reaction
(orientation effect)
3. provide acidic, basic, or other types of groups
required for catalysis (catalytic effect)
4. lower the energy barrier by inducing strain in
bonds in the substrate molecule (energy
effect)
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Substrate Concentration
• If the substrate concentration
doubles, the rate doubles (a
directly proportional relationship).
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Enzyme Concentration
• If the substrate concentration
doubles, the rate doubles (a
directly proportional relationship).
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Effect of Temperature on Enzyme Activity

• reaction rate increases

with increasing
temperature until a
temperature is
reached at which the
enzyme begins to
denature; then the rate
decreases rapidly.
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Effect of pH on Enzyme Activity

• pepsin, which initiates

protein digestion in the
highly acidic environment
of the stomach
• chymotrypsin, an
enzyme that aids
digestion of proteins in
the small intestine
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ENZYME REGULATION:
FEEDBACK
AND ALLOSTERIC CONTROL
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Activation (of an enzyme)

• Any process that initiates or
increases the action of an enzyme.

Inhibition (of an enzyme)

• Any process that slows or stops the
action of an enzyme.
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Feedback Control
• Regulation of an enzyme’s activity
by the product of a reaction later in
a pathway.
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Allosteric Control
• The binding of a molecule (an allosteric
regulator or effector) at one site on a
protein affects the binding of another
molecule at a different site
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Allosteric enzyme
• An enzyme whose activity is
controlled by the binding of an
activator or inhibitor at a location
other than the active site.
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The inhibition of an enzyme can be

reversible or irreversible.
In reversible inhibition, the inhibitor
can leave, restoring the enzyme to its
uninhibited level of activity.
In irreversible inhibition, the inhibitor
remains permanently bound and the
enzyme is permanently
inhibited.
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VITAMINS AND MINERALS

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Vitamin
• An organic molecule, essential in trace
amounts that must be obtained in the
diet because it is not synthesized in
the body.
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Vitamin
• An organic molecule, essential in trace
amounts that must be obtained in the
diet because it is not synthesized in
the body.
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Antioxidant
• A substance that prevents oxidation by
reacting with an oxidizing agent.

• Free radicals, highly reactive

molecular fragments with unpaired
electrons (for example, superoxide
ion,  O2-)
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Minerals