ENZYMES

Enzymes Identity of substrate and type of reaction

 It is a compound usually a protein, that acts as catalyzed:
a catalyst for a biochemical reaction.  Ex. Glucose oxidase, pyruvate
 Cause cellular reaction to occur millions of carboxylase, succinate dehydrogenase
times faster.
 Not consumed during the reaction but merely
help the reaction occur more rapidly. Classification of Enzymes
 Mostly, are globular proteins. Oxidoreductase  Catalyzes an oxidation -
reduction reaction.
Enzyme Structure  Requires a coenzyme that
Simple Enzyme – Composed only of protein. is oxidized or reduced as
Conjugated Enzyme - Has a non –protein part in the substrate is reduced
addition to a protein part. or oxidized.
Transferase  Catalyzes the transfer of
Apoenzyme Protein of the conjugated a functional group from
enzyme. one molecule to another.
Cofactor Has a non-protein part of
the conjugated enzyme.  Transaminases
Holoenzyme  Biochemically active - Catalyzes the transfer
conjugated enzyme of amino group from
produced from an one molecule to
apoenzyme and a another
cofactor.  Kinases
 Combined apoenzyme - Catalyzes the transfer
and cofactor entity. of phosphate group
Coenzyme Serves as a cofactor in a from ATP to give ADP
conjugated enzyme. and a phosphorylated
product.
Hydrolase  Catalyzes the hydrolysis
reaction.
Nomenclature and Classification of Enzymes
 Central to the process of
 Named about the function of the enzyme, type digestion.
of reaction catalyzed and the substrate identity.  Carbohydrases,
 Substrate Proteases, and Lipases.
 Reactant in an enzyme – catalyzed Lyase  Catalyzes the addition of
reaction a group to a double bond
or the removal of a group
3 Important Aspects in the Naming Process to form a double bond in
of Enzymes a manner that does not
Suffix  most enzymes end in the suffix “ase”. involve hydrolysis or
 Ex. Urease, Sucrase, Lipase oxidation.
Exception: Digestive enzymes Isomerase  Catalyzes the
 Ex. Trypsin, Chymotrypsin, Pepsin isomerisation of a
substrate in a reaction
Type of reaction catalyzed by an enzyme is often converting it to a
used as a prefix: molecule isomeric with
 Ex. Oxidase - oxidation reaction itself.
 Hydrolase - hydrolysis reaction

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 One reactant and one Induced - Fit Model

product in reactions.  Enzyme’s active site is not rigid and static.
Ligase  Catalyzes the bonding  There’s a constant change in shape
together of two molecules  Allows for changes in the shape or geometry
into one with the of the active site of an enzyme to
participation of ATP. accommodate a substrate.
 Result of the enzyme’s flexibility; it adapts the
incoming substrate.
Models of Enzyme Action
 Enzyme Active Site
 Small part of an enzyme’s structure that is
actually involved in catalysis.
 A three-dimensional entity formed by groups
that come from different parts of the protein
chains

 Enzyme-Substrate Complex
Enzyme Specificity
 The intermediate reaction species that is
 Extent to which an enzymes activity is
formed when a substrate binds to the active site
of an enzyme. restricted to a specific substrate, a specific
group of substrate, a specific type of chemical
bond, or a specific type of chemical reaction.
 Degree of specificity is determined by the
active site.

Types of Enzyme Specificity

Absolute  Catalyze only one reaction
Specificity  Most restrictive of all
specificities
 Catalase - enzyme with
absolute specificity
Group  Act only on molecules that
Lock - and - Key Model Specificity have a specific functional
 Active site in the enzyme has the fixed, rigid group, such a hydroxyl,
geometrical conformation. amino or phosphate
 Substrate with a complementary geometry groups.
can be accommodated.  Carboxylpeptidase is
group specific.
Linkage  Act on the particular type
Specificity of bond, irrespective to the
rest of the molecular
structure.
 Phosphatases hydrolyze
phosphate - ester bonds in
all types of phosphate
esters.
 Most general of the
common species.
Stereochemical  Act on a particular isomer.
Specificity

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Factors that Affect Enzyme Activity - Operates in the small intestines, function
 Enzyme Activity best at pH 8.0
- Measures the rate at which an enzyme
converts substrate to products in a
biochemical reaction.
 Temperature
 pH
 Substance Concentration
 Enzyme Concentration

Temperature
 Measure of kinetic energy of molecules.
 Higher temperatures mean molecules are
moving faster and colliding more frequently.
 Optimum temperature
- Temperature at which an enzyme exhibits Substrate Concentration
maximum activity.
 Increased concentration of substrate will
obtain the enzyme activity.
 Turnover Number
- Number of substrate molecules
transformed per minute by one molecule
of enzyme under optimum conditions of
temperature, pH and saturation.
Enzyme Concentration
 Kept in a low number because enzymes are
not consumed in the reaction.
 The greater the Enzyme concentration, the
greater the reaction rate.

pH
 The charge on acidic and basic amino acids
located at the active site depends on pH
 Small pH changes can result in enzyme
denaturation and subsequent loss of catalytic
activity.
 Biochemical buffers help maintain the
optimum pH for an enzyme. Extremozymes
 Can also affect substrate, causing either  A microbial enzyme active at a conditions
protonation or deprotonation of groups on the that would inactivate human enzymes as well
substrate. as enzymes present in other types of higher
 Optimum pH organisms.
- pH at which an enzyme exhibits maximum  Extremophile
activity  Microorganisms that thrives in extreme
- physiological pH ranges from 7.0 7.5 environments.
 Pepsin  Acidophiles
- Active in the stomach, functions best at pH - Optimal growth at pH levels of 3.0
2.0 or below.
 Trypsin

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 Alkaliphiles the catalytic groups at the active site from

- Optimal growth at pH levels of 9.0 properly effecting their catalyzing action.
or above.
 Hyperthermophile
- Temperature between 80C and
122C needed to thrive.
 Halophiles
 Cryophiles

Enzyme Inhibition
 Enzyme Inhibitor
- Substance that slows or stops the normal Irreversible Inhibition
catalytic function of an enzyme by binding Irreversible Enzyme Inhibitor
to it.  Molecule that inactivates enzyme by forming
a strong covalent bond to an amino acid side
 Reversible Competitive Inhibition
chain group at the enzymes active site.
 Reversible Non-Competitive Inhibition
 Do not have structures similar to that of the
 Irreversible Inhibition enzyme’s normal substrate.

Reversible Competitive Inhibition

Competitive Enzyme Inhibitor
 Molecule that sufficiently resembles an
enzyme substrate in shape and charge
distribution that it can compete with the
substrate for occupancy of the enzymes
active site.
 Remains in changed as it binds to the
enzymes’s active site. Regulation of Enzyme Activity
 Reversible process because it is maintained 1. A cell that continually produces large amount of
but weak interactions. enzyme for which substrate concentration is
 Can be reduced but increasing the always very low wasting energy. The production
concentration of the substrate. of the enzyme needs to be “turned off”.
2. A product of an enzyme Catalyzed reaction
that is present in plentiful amounts in a cell is a
waste of energy if the enzyme continues to
catalyze the reaction that produces the
product. The enzyme needs to be turned off.

Allosteric Enzyme
1. Have Quaternary Structure; (2 or more protein
chains).
2. Have 2 kinds of binding sites (for substrates and
for regulators).
3. Active and regulatory binding sites are distinct
from each other in both location and shape.
4. Binding of a molecule at the regulatory site
Reversible Non-Competitive Inhibition causes changes in the overall three-
Non-Competitive Enzyme Inhibitor dimensional structure of the enzyme, including
 Molecule that decreases enzyme activity by structural changes at the active site.
binding to a site on an enzyme other than the
active site.
 Presence of this causes a change in the
structure of the enzyme sufficient to prevent

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Proteolytic Enzymes and Zymogens

Proteolytic  Catalyzes the breaking of
Enzymes peptide bonds that maintain
the primary structure of
protein.
 Generated in an inactive form
and converted to active form
when they are needed.
Zymogens  Inactive precursor of a
proteolytic enzyme.
 Activation of a zymogen
requires an enzyme -
controlled reaction that moves
some part of the zymogen
structure which changes the 3-
dimensional structure of
zymogen, which affects active
site conformation.

Covalent Modification of Enzyme

 Process in which enzyme activity is altered by
covalently modifying the structure of the
enzyme through attachment of a chemical
group or removal of a chemical group from a
particular amino acid within the enzyme
Enzyme with two or more Protein Chains structure.
and 2 Kinds of Binding Sites
Regulators  Substance that bind at the Phosphorylation Process of addition of the
regulatory sites of allosteric phosphate group to the
enzymes. enzyme by protein kinases.
Positive  Increase enzyme activity Dephosphorylation Removal of the phosphate
Regulators  The shape of the active site is group from the enzyme by
changed such that it can phosphatases.
more readily accept
substrate.
Negative  Decrease enzyme activity Medical Uses of Enzymes
Regulators  Changes to the active site are  Used to diagnose certain diseases.
such that substrate is less  Appearance of these enzymes in the blood
readily accepted. often indicates that there is tissue damage in an
organ and that cellular contents are spilling out
into the bloodstream.
Feedback Control
 Used in the treatment of disease.
 A process in which activation or inhibition of the
first reaction in a reaction sequence is
controlled by a product of reaction sequence.
 Negative Feedback

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