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 KEY CONCEPTS
• Enzymes differ from ordinary chemical catalysts in
reaction rate, reaction conditions, reaction specificity,
and control.
• The unique physical and chemical properties of the
active site limit an enzyme’s activity to specific
substrates and reactions.
• Some enzymes require metal ions or organic cofactors.
Enzyme
• Enzymes – biocatalysts
• Enzymology – the study of enzymes
• All enzymes are protein but not ribozymes
• Ribozyme – have enzyme activity (include ribosomal RNA)
• Active site – the region of enzyme where catalysis occurs
What is an enzyme?
• Almost all enzymes are proteins that act as biological catalysts that speeds up
chemical reactions or biological chemical reactions.
• Enzymes are highly specific to a type of reaction.
• Enzymes must maintain their specific shape in order to function.
• Any alteration in the primary, secondary, tertiary, or quaternary forms of the
enzyme are detrimental.
General Properties of Enzymes
1. Higher reaction rates.
• The rates of enzymatically catalyzed reactions are typically 106 to 1012 times greater
than those of the corresponding uncatalyzed reactions and are at least several orders
of magnitude greater than those of the corresponding chemically catalyzed reactions.
2. Milder reaction conditions.
• Enzymatically catalyzed reactions occur under relatively mild conditions:
temperatures below 100°C, atmospheric pressure, and nearly neutral pH. In contrast,
efficient chemical catalysis often requires elevated temperatures and pressures as
well as extremes of pH.
3. Greater reaction specificity.
• Enzymes have a vastly greater degree of specificity with respect to the identities of
both their substrates (reactants) and their products than do chemical catalysts; that is,
enzymatic reactions rarely have side products.
 Function of enzy
mes
• Enzymes have many jobs.
• Break down nutrients into useable
molecules.
• Store and release energy (ATP).
• Create larger molecules from smaller
ones.
• Coordinate biological reactions between
different systems in an organism.

Enzyme function. Image Credit: Designua / Shutterstock

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Enzyme action overview

• Enzymes are Biological Catalysts.
• They increase the rate of Metabolic reactions.
• Almost all Biological Reactions involve Enzymes.
• All enzymes are Globular Proteins with a specific Tertiary Shape.
• They are usually specific to only one reaction.
• The part of the Enzyme that acts a Catalyst is called the Active Site.
• The rest of the Enzyme is much larger and is involved in maintaining the specific shape of the
Enzyme.
• The active site reacts with the desired substance, called the substrate.
• The substrate may need an environment different from the mostly neutral environment of the
cell in order to react.
• When a reaction involving an Enzyme occurs, a Substrate is turned into a Product.
• The Substrate can be one or more molecules.
• The Active Site of an Enzyme is Complementary to the Substrate it catalyses.
Enzymes Acts on Specific Substrates

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Classification of Enzyme
• Commonly named by suffix –ase to the name of the enzyme’s substrate or to a
phrase describing the enzyme’s catalytic action
• Urease : Catalyzes the hydrolysis of urea
• Alcohol dehydrogenase : Catalyzes the oxidation of primary and secondary
alcohols to their corresponding aldehydes and ketones by removing hydrogen
• Lactase: Breaks down Lactose into Glucose and Galactose.
• Catalase: Breaks Hydrogen Peroxide down into Water and Oxygen.
• Glycogen Synthase: Catalyses the formation of Glycosidic Bonds between
Glucose molecules.
• ATP-ase: Breaks down ATP into ADP, producing energy.
• Classified and named according to the nature of the chemical reactions they
catalyze
 TABLE - Enzyme Classification According to Reaction Type

Classification Type of Reaction Catalyzed

1. Oxidoreductases Oxidation–reduction reactions

2. Transferases Transfer of functional groups
3. Hydrolases Hydrolysis reactions
4. Lyases Group elimination to form double bonds
5. Isomerases Isomerization
6. Ligases Bond formation coupled with ATP hydrolysis
 Models of Enzyme Function
• A substrate-binding site consists of an indentation or cleft on the surface of an enzyme
molecule that is complementary in shape to the substrate (geometric complementarity)
• The amino acid residues that form the binding site are arranged to specifically attract the
substrate (electronic complementarity)
• The complementarity between enzymes and their substrates is the basis of the “lock-
and-key” model of enzyme function
• Molecules that differ in shape or functional group distribution from the substrate cannot
productively bind to the enzyme.
• X-Ray studies indicate that the substrate-binding sites of most enzymes are largely
preformed
• But undergo some conformational change on substrate binding (a phenomenon called
induced fit)
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The Lock-and-key Hypothesis
• The Lock-and-key Hypothesis is a model of how Enzymes catalyse Substrate
reactions. It states that the shape of the Active Sites of Enzymes are exactly
Complementary to the shape of the Substrate.
• When a substrate molecule collides with an enzyme whose Active Site shape is
complementary, the substrate will fit into the Active Site and an Enzyme-
Substrate Complex will form.
• The enzyme will catalyse the reaction, and the products, together with the
enzyme, will form an Enzyme-Product Complex. According to this model, it is
possible for an enzyme to catalyse a reverse reaction.

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 The Induced-Fit Hypothesis
• A more recent model, which is backed up by evidence ,and is widely accepted as
describing the way enzymes work, is the Induced-Fit Hypothesis.
• It states that the shape of Active Sites are not exactly Complementary, but change
shape in the presence of a specific substrate to become Complementary.
• When a substrate molecule collides with an enzyme, if
its composition is specifically correct, the shape of the enzyme’s Active Site will
change so that the substrate fits into it and an Enzyme-Substrate Complex can form.
• The reaction is then catalysed and an Enzyme-Product Complex forms.

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Some Enzymes Require Cofactors
• The functional groups of proteins participate in acid–base reactions,
• Form certain types of transient covalent bonds, and
• Take part in charge–charge interactions.
• They are, however, less suitable for catalyzing oxidation–reduction reactions and
many types of group-transfer processes.
• Although enzymes catalyze such reactions, they can do so only in association with
small cofactors, which essentially act as the enzymes’ “chemical teeth”
Image credit to owner
• Cofactors may be metal ions, such as Cu2+, Fe3+ or Zn2+
• The essential nature of these cofactors explains why organisms require trace
amounts of certain elements in their diets.
• It also explains, in part, the toxic effects of certain heavy metals.
• For example, Cd2+ and Hg2+ can replace Zn2+ (all are in the same group of the
periodic table) in the active sites of certain enzymes, including RNA polymerase,
and thereby render these enzymes inactive.
• Cofactors may also be organic molecules known as coenzymes.
• Some cofactors are only transiently associated with a given enzyme molecule, so
that they function as cosubstrates.
• Nicotinamide adenine dinucleotide (NAD+) and nicotinamide adenine
dinucleotide phosphate (NADP+)
• Prosthetic groups, are permanently associated with their protein, often by covalent
bonds.
• For example, a heme prosthetic group is tightly bound to proteins known as
cytochromes through extensive hydrophobic and hydrogen-bonding interactions
together with covalent bonds between the heme and specific protein side chains.
• A catalytically active enzyme–cofactor complex is called a holoenzyme.
• The enzymatically inactive protein resulting from the removal of a holoenzyme’s
cofactor is referred to as an apoenzyme; that is,
Image credit to owner
Coenzymes Must Be Regenerated.
• Coenzymes are chemically changed by the enzymatic reactions in which they
participate.
• In order to complete the catalytic cycle, the coenzyme must return to its original
state.
• For a transiently bound coenzyme (cosubstrate), the regeneration reaction may be
catalyzed by a different enzyme as we have seen to be the case for NAD.
• However, for a prosthetic group, regeneration occurs as part of the enzyme
reaction sequence.
Enzymes in the Real World
• Since Enzymes are Proteins, which are effected by their environment, organisms that live in
varying conditions have adapted by producing Enzymes more suitable to their
environments. Endotherms (animals that maintain their body temperature) keep
the temperature of the Enzymes within their bodies constant to ensure optimum rates of reaction.
• Enzymes are used for a wide variety of purposes, such as in digestion. The action of an Enzyme
may be Intracellular (the Enzymes are attached to the cell membrane or are in the Cytoplasm, and
reactions occur inside the cell) or Extracellular (Enzymes work outside cells, and their products
may be absorbed into the cell)
• Enzymes are also used in protection against Pathogens. They can be used to destroy invading
Microorgansims. For example, Phagocytes engulf Pathogens and the Endocytosed Vesicle then fuses
with Lysosomes which contain enzymes that destroy the Pathogen’s cell membrane.
Credit to Sam Adam-Day
 CHECK POINTS
• What properties distinguish enzymes from other catalysts?
• Describe how different enzymes are classified and named.
• What factors influence an enzyme’s substrate specificity?
• Why are cofactors required for some enzymatic reactions?
• What is the relationship between cofactors, coenzymes, cosubstrates,
and prosthetic groups?