BIOCHEMISTRY LECTURE: Trisha Love M.
dela Cruz
ENZYME PART II
ENZYME INHIBITION
- An enzyme inhibitor is a substance that slows
or stops the normal catalytic function of an
enzyme by binding to it.
Three Modes Of Inhibition:
preventing the substrate at the active site from
1. Reversible competitive inhibition properly effecting action.
- A competitive enzyme inhibitor is a molecule
that sufficiently resembles an enzyme
substrate in shape and charge distribution that
it can compete with the substrate for
occupancy of the enzyme’s active site.
- The formation of an enzyme–competitive
3. Irreversible inhibition
inhibitor complex is a reversible process
because it is maintained by weak interactions - An irreversible enzyme
(hydrogen bonds, etc.).- inhibitor is a molecule
- The substrate an inhibitor binds to the same that inactivates enzymes
active site but differ in ther overall shape by forming a strong
covalent bond to a part
of the active site
permanently preventing
substrates from occupying it
2. Reversible noncompetitive inhibition
- A noncompetitive enzyme inhibitor is a
molecule that decreases enzyme activity by
binding to a site on an enzyme other than the
active site.
- The presence of the inhibitor causes a
change in the structure of the enzyme
ENZYME REGULATION Feedback Control
- Primarily in Energy Conservation - Feedback control is a process in which
- Enzyme production can be “turned on” and activation or inhibition of the first reaction in a
“turned off” reaction sequence is controlled by a product of
➢ 3 Mechanisms: the reaction sequence.
1. Feedback control associated with
allosteric enzymes
2. Proteolytic enzymes and zymogens
3. Covalent modification
Allosteric Enzymes
➢ Characteristics of all enzymes:
1. All allosteric enzymes have quaternary
structure;
2. All allosteric enzymes have two kinds of
binding sites: those for substrate and
those for regulators.
3. Active and regulatory binding sites are
distinct from each other in both location Proteolytic Enzymes And Zymogens
and shape
4. Binding of a molecule at the regulatory - A zymogen is the inactive precursor of a
site causes changes in the overall proteolytic enzyme.
three-dimensional structure of the - other term: proenzyme
enzyme, including structural changes at - Activation of a zymogen requires an enzyme-
the active site. controlled reaction that removes some part
of the zymogen structure
Covalent Modification
- Covalent modification is a process in which
enzyme activity is altered by covalently
modifying the structure of the enzyme
- Through attachment of a chemical group to or
removal of a chemical group
- The most common type of covalent
modification is phosphorylation
PRESCRIPTION DRUGS THAT INHIBIT ENZYME - Transpeptidase, an enzyme that catalyzes
ACTIVITY the formation of peptide cross links between
polysaccharide strands in bacterial cell walls.
ACE Inhibitors - Transpeptidase, an enzyme that catalyzes
the formation of peptide cross links between
- ACE (Angiotensin-converting enzyme) polysaccharide strands in bacterial cell walls.
- Used to treat highblood pressure by inhibiting - Forms covalent bonds = becomes
ACE. irreversible
- Forms covalent bonds = becomes
irreversible
MEDICAL USES OF ENZYMES
- Enzymes can be used to diagnose certain
diseases
- Some enzymes are not normally found in
the blood but are produced only inside cells of
certain organs and tissues
Sulfa Drugs - Enzymes can also be used in the treatment of
diseases.
- An antibiotic is a substance that kills bacteria - Use of tissue plasminogen activator (TPA),
or inhibits their growth. which activates the enzyme plasminogen.
Antibiotics exert their - Approximately, 700,000 people die each year
action selectively on due to Antimicrobial Resistance (UN,2019)
bacteria.
- Sulfanilamide inhibits
bacterial growth because
it is structurally similar to
PABA (p-aminobenzoic
acid).
Penicillins
- Discovered by Alexander Flemming in 1928
- B-lactam ring structure
- Inhibits the enzyme transpeptidase
