ENZYMES

Biochem (Lab)
(Nursing) (116) | (Alexander Dominic S. Liban) | SEM 1 2022

● Some enzymes retain their original

trivial names, which give no hint of
Enzymes
the associated enzymatic reaction
○ Are biological catalysts that alters ● • Pepsin; trypsin
the rate of chemical reaction
CLASSIFICATION OF ENZYME
○ Increase the rate of a reaction by a ● 1. Oxidoreductases
factor of 10^9 to 10^20 over an - catalyze oxidation-reduction
uncatalyzed reaction reactions. Requires a coenzyme
○ In the absence of enzymatic that is oxidized or reduced
catalysis, most biochemical
reactions are so slow ● 2. Transferases
- catalyze transfer of C-, N-, or P
○ Reactions that would not occur containing groups. Subtypes are
under the mild conditions of transaminase and kinase
temperature and pressure that are
compatible with life ● 3. Hydrolases -
catalyze cleavage of bonds by
ENZYME STRUCTURE addition of water
(hydrolysis). Includes important
● Simple Enzyme digestive enzymes (lipase,
○ Composed only of protein (amino protease)
acid chains)
● 4. Lyases
● Conjugated Enzyme - catalyze cleavage of C–C,
○ Has a nonprotein part in addition to C–S and certain C–N bonds to
a protein part. form a double bond.

● Apoenzyme: Protein part of a ● 5. Isomerases - catalyze

conjugated enzyme. racemization of optical or
geometric isomers
● Cofactor: Nonprotein part of a
conjugated enzyme. ● 6. Ligases
- catalyze formation of bonds
● A holoenzyme is the between carbon and O, S, N
biochemically active conjugated coupled to hydrolysis of
enzyme high-energy phosphates (ATP)

ENZYME NOMENCLATURE
ENZYME SPECIFICITY
● Glucosidase-hydrolyzes
glycosides ● Absolute specificity: catalyzes
the reaction of one unique
● Urease – hydrolyzes urea substrate to a particular product

● Lactate dehydrogenase – ○ Example: Catalase is an enzyme

catalyzes conversion of lactate to with absolute specificity for
pyruvate, and vice versa hydrogen peroxide

● Adenylyl cyclase – catalyzes

formation of cyclic AMP

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ENZYMES
Biochem (Lab)
(Nursing) (116) | (Alexander Dominic S. Liban) | SEM 1 2022

2. Irreversible inhibition: binds to

E tightly, permanently blocks the
enzyme;
● Group specificity: Enzyme will covalent alterations in the E
act only on molecules that have a Suicide inactivators
specific functional group (mechanism-based inactivators)

○ Example: Carboxypeptidase REGULATION OF ENZYME

cleaves amino acids, one at a time, ACTIVITY
from the carboxyl end of the
peptide chain ● Feedback Control - •
Process in which activation
● Stereospecificity: catalyzes a or inhibition of the first
reaction in which one stereoisomer reaction in a reaction
is reacted or formed in preference sequence is controlled by a
to all others that might be reacted product of the reaction
or formed sequence

○ Example: ʟ-amino-acid oxidase ➢ Regulators of an allosteric enzyme

will only catalyze the oxidation of may be:
the ʟ-form of an amino acid but not ○ • Products of different
its ᴅ-form pathways of reaction within
the cell
● Linkage specificity: Enzyme will ○ • Compounds produced
act on a particular type of chemical outside the cell (hormones)
bond, rest of the molecular
structure is not considered
● Allosterism: Enzyme regulation
○ Example: Phosphatases hydrolyze based on an event occurring at a
phosphate–ester bonds in all types place other than the active site but
of phosphate esters that creates a change in the active
site.
ENZYME INHIBITION ● Allosteric enzymes often have
multiple polypeptide chains.
• Enzyme inhibitors are molecular
agents that interfere with catalysis, ○ Regulator: A substance that binds
slowing or halting enzymatic to an allosteric enzyme to produce
reactions an effect:
• There are two broad classes of ➢ • Negative modulation: Inhibition
enzyme inhibition: ➢ • Positive modulation: Stimulation

1. Reversible inhibition: binds

with the E through noncovalent
interactions

(1) Competitive inhibition

(2) Uncompetitive inhibition
(3) Mixed inhibition (a special case:
Noncompetitive inhibition)

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ENZYMES
Biochem (Lab)
(Nursing) (116) | (Alexander Dominic S. Liban) | SEM 1 2022

● Zymogems: Mechanism of
induces a conformational
regulation by production of
change that results in a
proteolytic enzymes in
complementary fit
inactiveforms
○ •Proteolytic enzyme: Catalyzes
• The rate of an enzyme-
the breaking of peptide bonds
catalyzed reaction is
affected by:
○
• Zymogens (pro-enzymes):
• Enzyme concentration
Turned on at the appropriate
• Substrate concentration
● time and place
• Temperature
● • Example: Most digestive and
• pH
● blood-clotting enzymes are
proteolytic enzymes
• First-order kinetics: reaction rate
dependent on an increase [S]
Covalent Modification:
• Zero order kinetics: reaction rate
Process in which enzyme activity is
independent on increase [S]; reached
altered by covalently modifying the
saturation point
structure of the enzyme
• Saturation point: S are bound to all
• Involves adding or removing a
available active sites of the E; reaction
chemical group within an enzyme
rate proceeds at max rate (Vmax);
↑[S] will not affect reaction rate
• Common covalent modification –
Addition and removal of phosphate
group (phosphorylation and
desphosphorylation)

HEADING 2
● Keyword
○ Definition, Notes
● Notes
● Notes
● Notes

IMPORTANT INFO

• Substrate – biomolecule
acted upon by the enzyme

• Active site – specific

region of the enzyme that
creates a 3D surface
complementary to the
substrate.

• Lock-and-key model: substrate binds

to that portion of the enzyme with a
complementary shape
• Induced fit model:
binding of the substrate