1 MC-2 LECTURE: ENZYMES

BSN – 1C – 1ST SEMESTER – MIDTERMS

S.Y. 2022-2023
IMPORTANCE OF ENZYMES TERMS TO UNDERSTAND
BIOCHEMICAL NATURE OF ENZYMES
- All biochemical reactions are enzyme
catalyzed in the living organism - Active site – the area on the enzyme
- Plays a role in metabolism, diagnosis, where the substrate or substrates is/are
and therapeutics attached to
o Level of enzyme in blood are of o Enzymes are usually very large
diagnostic importance i.e., good proteins, and the active sites is just a
indicator in disease such as small region of the enzyme molecule
myocardial infarction - Substrate – the reactant in the chemical
o Digestive enzymes as therapeutic reaction
DEFINITION
- Enzymes are biological catalysts
o Catalyze nearly all the chemical
reactions taking place in the body
o Proteins that increase the rate of
reaction by looking for an alternative
pathway that has a low energy of
activation - Apoenzyme – the enzyme without its
CHARACTERISTICS non-protein moiety is termed as
apoenzyme and it is inactive
- Not altered or consumed during reaction
- Holoenzyme – active enzyme with its
- Reusable
non-protein component
- Shows specificity to the reaction they
control
- Are sensitive to their environment so
they can be controlled by adjusting the
temperature, the pH or the substrate
concentration
STRUCTURE
- Globular shape
- Complex 3D structure - Cofactor – non protein chemical
STRUCTURE OF ENZYMES compound that is bound either tightly or
loosely to an enzyme and is required for
catalysis
- Types of cofactors
o Coenzymes – examples: vitamins.
Compound derived from vitamins
o Prosthetic group – Zinc,
manganese, iron
NAMING ENZYMES
- In many cases ends in -apse
o Sucrase – catalyze the hydrolysis of
sucrose

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2 MC-2 LECTURE: ENZYMES
BSN – 1C – 1ST SEMESTER – MIDTERMS
S.Y. 2022-2023
- Name describes the function of the - Examples: glucose oxidase, Peroxidase,
enzyme Catalase, Phenylalanine Hydroxylase
o Oxidases- catalyze oxidation
TRANSFERASES
reactions
- Sometimes common names are used, - Catalyze group transfer reactions
especially for digestion enzymes
o Pepsin and trypsin
- Some names describe both the
substrate and the function
o Alcohol dehydrogenase oxidizes
ethanol
CLASSIFICATION OF ENZYMES
- Examples: Transaminases (ALT and
- 6 functional classes (EC number AST), Phosphotransferases (Kinases),
classification) by the International Union Transmethylases, Transpeptidases,
of Biochemist based on the types of Transacylases
reactions that they catalyze
o EC 1 – Oxidoreductase HYDROLASES
o EC 2 – Transferases - Catalyze hydrolysis reactions where
o EC 3 – Hydrolases water is the acceptor of the transferred
o EC 4 – Lyases group
o EC 5 – Isomerases
o EC 6 – Ligases
PRINCIPLE OF INTERNATIONAL
CLASSIFICATION
- Each enzyme has classification number
- Examples: Protein hydrolyzing enzymes
- consisting of 4 digits (example: EC:
(peptidases), Carbohydrates (Amylase,
(2,7,1,1) Hexokinase
Maltase, Lactase), Lipid hydrolyzing
o 2 is class – transferase
enzymes (Lipase), Deaminases,
o 7 is subclass – transfer of phosphate
Phosphatases
o 1 is sub-sub class – alcohol is
phosphate acceptor LYASES
o 1 is specific name
- Cleave various bonds by means other
- Specific name of Hexokinase is ATP, D-
than hydrolysis and oxidation
Hexose-6-Phosphotransferase
- Add water, ammonia or carbon dioxide
(Hexokinase)
across double bonds, or remove these
OXIDOREDUCTASE elements to produce double bonds
- Catalyze oxidation-reduction reactions

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3 MC-2 LECTURE: ENZYMES
BSN – 1C – 1ST SEMESTER – MIDTERMS
S.Y. 2022-2023
- Examples: Fumarase, Carbonic ENZYMES LOWER A REACTION’S
anhydrase, Hydralase, Dehydratase ACTIVATION ENERGY
ISOMERASE
- Catalyze isomerization reaction

- Carry out many kinds of isomerization:

o L to D isomerization
o Mutase reactions (shift of chemical
groups)
- Examples: Isomerase, Mutase
ENZYME-SUBSTRATE BONDING
ENZYMATIC ACTION
2 Models for the enzyme-substrate formation
- Chemical reactions need an initial output
of energy - Lock-and-key model
o Activation energy o Active site has a rigid shape
- During this part of the reaction, the o Substrates with matching shape can
molecules are said to be in a transition fit
state o Substrate is a key that fits the lock of
the active site

- Biological systems are very sensitive to

temperature changes
- Enzymes can increase the rate of
reactions without increasing the
temperature
- They do this by lowering the activation
energy. They look for new reaction
pathway – shortcut
- Enzyme controlled reactions proceed
10^8 to 10^11 times faster than
corresponding non-enzymatic reactions
- Induced-fit model
o Active site is flexible, not rigid. Can
change its conformation
o Shape of enzyme, active site, and
substrate adjust to maximize the fit.
Which improves catalysis
o Greater range of substrate specificity

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4 MC-2 LECTURE: ENZYMES
BSN – 1C – 1ST SEMESTER – MIDTERMS
S.Y. 2022-2023
ENZYME SPECIFICITY
FACTORS AFFECTING ENZYME
ACTIVITY
- Environmental conditions
o Temperature
o pH
o Substrate concentration
o Enzyme concentration
- Cofactors and Coenzymes
- Allosteric regulation
o Positive regulation
o Negative regulation
- Enzyme inhibitors
EFFECTS OF TEMPERATURE
- Increases enzyme activity up to its
optimum temperature
o Optimum temperature is at which
enzymatic reaction occur fastest
- 40 degrees centigrade – optimum
temperature for most enzymes
- Many are at lower, cold-water fish will
die at 30 degrees Celsius because their
enzymes denature
- Few bacteria can withstand high
temperature (up to 100 degrees Celsius)
- Most enzymes full denature at 70 degrees
Celsius
EFFECTS OF PH
- If pH is slightly different from the
enzyme’s optimum value, there will be
small changes in the charges of the
enzymes and its’s substrate’s molecule
- Change in ionization will affect the
binding of the substrate with the active
site
- Different optimum pH when enzyme
activity is at its highest
- Extreme changes in pH can cause
denaturation
EFFECT OF SUBSTRATE
CONCENTRATION
- Rate of reaction increases as substrate
concentration increases (at constant
enzyme concentration)
- Maximum activity occurs when the
enzyme is saturated (when all enzymes
are bound to the substrate). – called
saturation point
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5 MC-2 LECTURE: ENZYMES
BSN – 1C – 1ST SEMESTER – MIDTERMS
S.Y. 2022-2023
- If you alter the concentration of the
enzyme, then Vmax will change too.
EFFECT OF ENZYME CONCENTRATION
- Reaction rate increases with increasing
enzyme concentration, assuming
enzyme concentration is much lower
than that of substrate
COFACTORS
- Additional non-protein molecule that is
needed by some enzymes for proper
functioning.
- Main role is to assist
- Prosthetic groups – tightly bound
cofactors
- Coenzyme – cofactors that are bound and
released easily to the apoenzyme
- Many vitamins are coenzymes. They are
not specific to which enzyme they assist
EXAMPLES OF METAL COFACTORS
- Cu2+= assists in cytochrome oxidase, last
enzyme in the respiratory electron
transport chain
- Fe2+ and Fe3+ - helps catalase, converts
hydrogen peroxide to water and oxygen
- Mg2+ - assists Hexokinase in transferring
phosphate to glucose, forming glucose-6-
phosphate in glycolysis
- Mn2+- helps arginase, the final enzyme in
urea cycle
- Zn2+ - assists alcohol dehydrogenase
together with NAD+ to convert alcohol
to aldehyde and carboxylic acid
IMPORTANT COENZYME
- FADH (Vitamin B2) – flavin adenine
dinucleotide – reducing agent in cellular
respiration and donates electrons to the
electron transport chain
- NADH (Vitamin B3) – nicotinamide
adenine dinucleotide – capable of
carrying and transferring electrons and
functions as oxidizing agent in redox
reactions
- Quinone – fully conjugated aromatic
rings that acts as pigment in bacteria,
fungi, and certain plants
- CoA (synthesized from Vitamin B5) –
acyl group carriers
OTHER COENZYMES
- Vitamin C – ascorbic acid – co-substrate
with iron in formation of collagen in the
body, helper of other vitamins (E and B9)
to remain active
- TPP (Vitamin B1) – thiamin
pyrophosphate – needed in CAC –
transfer of carboxyl group
- Vitamin B6 compounds (6) –
coenzymes for the transfer of amino
groups
- Biotin (Vitamin B7 or Vitamin H) –
transfer of carboxyl group
- THF (Vitamin B9) – tetrahydrofolate –
needed in methylation reactions
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6 MC-2 LECTURE: ENZYMES
BSN – 1C – 1ST SEMESTER – MIDTERMS
S.Y. 2022-2023
- Cobalamin (Vitamin B12) – transfer of o Distorts the shape of the enzyme
methyl groups when it Is bound to it, thus enzyme
- Vitamin A and K cannot bind the substrate
o These are not influenced by the
FIVE GROUP-TRANSFER
concentration of the substrate
COENZYMES
o Inhibits by binding irreversibly or
reversibly to the enzyme but not at
the active site
- Uncompetitive Inhibition
o Has a structure different from the
substrate
o Inhibition happens only when
enzyme is already bound to the
substrate
o Concentration of the substrate is
reduced at the same time the rate of
enzymatic action (substrate binds
longer in the enzyme)
o Inhibits by binding irreversibly to
FACTORS AFFECTING ENZYME the enzyme but not at the active site
ACTIVITY
APPLICATION OF INHIBITORS
Poisons: Snake bite, plant alkaloids and nerve
gases
Medicine: antibiotics, sulphonamides, sedatives,
and stimulants
Examples:
- Aspirin: inhibit the synthesis of
GENERAL CHARACTERISTICS OF
prostaglandins which are at least partly
VITAMINS
responsible for the aches and pains of
arthritis
- Methotrexate: cancer chemotherapy to
semi-selectively inhibit DNA synthesis
of malignant cells
- Sulfa Drugs: inhibit the folic acid
synthesis that is essential for the
metabolism and growth of disease-
causing bacteria
ALLOSTERIC REGULATOR
FACTORS AFFECTING ENZYME
ACTIVITY - Negative Regulator – inhibitor
o Substances that decrease the rate of
- Non-competitive inhibition enzymatic reaction
o Has a structure different from the o Changes the active site such that
substrate substrate is less readily accepted

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7 MC-2 LECTURE: ENZYMES
BSN – 1C – 1ST SEMESTER – MIDTERMS
S.Y. 2022-2023
- Positive Regulator – activator
o Substances that increase the rate of
enzymatic reaction
o The shape of the active site is
changes such that it can more
readily accept substrate
▪ Examples: fructose-2,6-
biphosphate which activates
phosphofructokinase1 and
increases the rate of glycolysis in
response to the hormone insulin.
▪ Hexokinase-1
▪ Glucokinase

ANOTHER TYPE OF REGULATION

- Feedback Control
o Is a process in which activation or
inhibition of the first reaction in a
reaction sequence is controlled by a
product of the reaction sequence

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