1380960835.1698lecture 4 & 5. Enzymes
1380960835.1698lecture 4 & 5. Enzymes
1380960835.1698lecture 4 & 5. Enzymes
Why are we
devoting two whole
lecture topic to a
enzyme?
From the Virtual Cell Biology Classroom on ScienceProfOnline.com Image: Jumping rope, Meagan E. Klein
Outline
• Composition, structure and properties
of enzyme
• How Enzymes work
• Enzyme activity
• Factors affecting enzyme activity
• Regulation of enzyme activities
• Enzymes in clinical diagnosis
1. Definition of enzyme
•Enzymes are biological catalysts.
•A Catalyst is defined as "a substance
that increases the rate of a chemical
reaction without being itself changed in
the process.”
Enzymes as Biological Catalysts
• Enzymes are
proteins that increase
the rate of reaction
by lowering the
energy of activation
• They catalyze nearly
all the chemical
reactions taking place
in the cells of the
body
• Enzymes have
unique three-
dimensional shapes
that fit the shapes of
reactants
(substrates)
2. Properties of enzymes (important!)
Activation
Energy
What is the difference between an enzyme
and a protein?
Binding site
Active site
Catalytic site
Enzymatic reaction steps
• Concentration of substrate
• Concentration of enzyme
• Temperature
• pH
• Activators
• Inhibitors
Enzyme velocity
• Enzyme activity is commonly expressed by the
intial rate (V0) of the reaction being catalyzed.
(why?)
[S]>>[E] V∝[E]
• The initial rate of an
enzyme-catalyzed
reaction is always
proportionate to the
concentration of enzyme.
• This property of enzyme
is made use in determining
the serum enzyme for the
diagnosis of diseases.
(3) Effect of temperature on velocity
Bell-shaped curve
(4) Effect of pH value on velocity
Bell-shaped curve
• Each enzyme has
an optimal pH or pH
range (where the
enzyme has maximal
activity).
• Requirements for
the catalytic groups
in the active site in
appropriate
ionization state is a
•The pH optimum varies for common reason for
different enzymes. this phenomenon.
•Most enzyme: neutral pH (6-
8).
(5) Effect of activator on velocity
•Enzyme activators are molecules that bind to
enzymes and increase their activity.
(ii). Organic
• Reducing agents, such as Cys 、 GSH
(iii). Proteins
(6) Inhibition of enzyme activities
(very important!)
• Inhibitor: any molecule which acts
directly on an enzyme to lower its
catalytic rate is called an inhibitor.
(not denaturation)
• Some enzyme inhibitors are normal
body metabolites.
• Other may be foreign
substances,such as drugs or toxins.
8. REGULATION OF ENZYME ACTIVITY
1. Allosteric binding sites: Allosteric enzymes
are regulated by molecules called effectors
(modifiers) that binds nonconvalently at a site
other than the active site.
2. By Covalent Modification: Many enzymes
are regulated by covalent modification, most
frequently by the addition or removal of
‘phosphate’ group to serine, threonine or
tyrosine residue of the enzyme by kinases.
(enzyme)
3. Induction and repression of enzyme
sysnthesis: Cells can also regulate the
amount of enzymes present by altering the rate
of enzyme synthesis.
REGULATION CONT….
• 4. Zymogen Cleavage: Some enzyme are
synthesized as inactive precursor, called
zymogens, that are activated by proteolysis
(e.g., digestive enzyme, pepsinogen is inactive
and cleaved to pepsin which is active
chymotrypsin)
• 5.Location within the cell: Many enzymes are
localized in specific organelles within the cell.
This, compartmentation helps in the regulation of
the metabolic pathway.
9. Enzymes in clinical diagnosis
• An enzyme test is a blood test or urine test
that measures levels of certain enzymes to
assess how well the body’s systems are
functioning and whether there has been any
tissue damage. (why?)
• Common enzymes used for clinical diagnosis
include:
– alanine aminotransferase(ALT,also called
glutamate pyruvate transaminase,GPT)
– alkaline phosphatase
– amylase
– aspartate aminotransferase
– creatine kinase
– lactate dehydrogenase