Enzyme Catalysis
Enzyme Catalysis
Enzyme Catalysis
Catalysis
CHM-203
What are enzymes?
Enzyme nomenclature
What are we
Mechanism of enzyme catalysis
going to
cover? Factors affecting enzyme activity
Enzyme control
Enzymes
Prosthetic
Metal Ions Coenzymes Groups
Metal Ions
Activity
For every reaction to occur, the
Mechanism activation energy barrier ought to
be crossed.
Substrate
Temperature pH
concentration
Presence of
inhibitors
Temperature
Non-
Competitive Irreversible
competitive
Competitive
Inhibition
+ This occurs when the inhibitor
mimics the substrate molecule
and binds to the active site of
the enzyme in a reversible
manner.
+ This reduces enzyme activity
because many of the active sites
of the enzyme molecules are
blocked by bound inhibitor
molecules and thus cannot bind
substrate molecules at the
active site
Non-competitive
inhibition
+ A noncompetitive inhibitor, on
the other hand, binds to the
enzyme surface at a location
other than the active site.
+ It does not block substrate
binding directly but inhibits
enzyme activity indirectly by
causing a change in protein
conformation that can either
inhibit substrate binding to the
active site or greatly reduce the
catalytic activity at the active
site.
Irreversible
Inhibition
+ An irreversible inhibitor
binds to the enzyme
covalently, causing
permanent loss of
catalytic activity.
+ Some irreversible
inhibitors of enzymes
can be used as
therapeutic agents
Enzyme Control
Feedback inhibition
Allosteric regulation
+ Proteolytic cleavage is an
example of irreversible covalent
modification.
+ This is usually seen in digestive
tract enzymes.
+ They are usually released as
inactive precursors called
zymogens since in their active
state, they are harmful where
they are released
+ When they have to be activated,
certain polypeptide chains are
cleaved to activate the enzyme.