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BIOLOGICAL
CATALYST
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Catalysis
Structure
Defence
Regulation
Movement
H2 O2
H2 O +
O2
Enzyme As Catalyst
All enzymes are proteins - with the exception of
some RNAs that catalyze their own splicing all
enzymes are proteins
Catalysis:
- the process of increasing the rate of
chemical reactions
Catalyst:
- the substance that facilitate in catalysis
Enzyme As Catalyst
Enzymes are catalysts:
1. increase the rate of a reaction
2. not consumed by the reaction
3. act repeatedly to increase the rate of reaction
4. enzymes often specific promote only 1
particular reaction, others catalyze a family of
similar reactions
cellulase cellulose as substrate
hexokinase any 6 ring monosaccharide fructose, glucose
Enzyme Catalysis
GENERAL FORMULA
E = enzyme
S = substrate
P = product
Enzyme Catalysis
Active site/catalytic
site - part of enzyme
to which the
substrate binds and
the reaction takes
place
Product
Substrate a
reactant in an
enzyme-catalyzed
reaction
ENZYME-
BIOLOGICAL
CATALYST
(2)
ES
ES*
EP
E + P
ES
ES*
EP
E + P
ES
ES*
EP
E + P
ES
ES*
EP
E + P
E + P
Enzyme Catalysis
Rate of reaction = reaction velocity (V)
- the rate of enzyme reaction is measured by
the rate of the appearance of products or the
rate of disappearance of substrates.
- d[P]/dT or d[S]/dT
mol product/min or mol substrate/min
Enzyme activity
1 unit (U) is the amount of enzyme that catalyses the
reaction of 1 mol of substrate per minute under
specified conditions. Enzyme activity / rate of reaction
enzyme strength
Enzyme Catalysis
The rate of a reaction depends on
its activation energy, DG
an enzyme provides an alternative
pathway with a lower activation energy
ES complex
H2 O2
H2 O +
O2
a) No catalyst,
b) with added Fe3+ salt,
c) with added catalase
Enzyme/substrate
Binding Modelsinteraction
Two models have been developed to describe
formation of the enzyme-substrate complex
1. Lock-and-key model: substrate binds to that
portion of the enzyme with a complementary
shape
Continue
1.
2.
Induced fit model: binding of the substrate induces a change in the conformation
of the enzyme that results in a complementary fit
Enzyme/substrate interaction
1. Lock and key model
- substrate (key) fits into a perfectly shaped space
in the enzyme (lock)
- lots of similarities between the shape of the
enzyme and the shape
of the substrate
- highly stereospecific
- implies a very RIGID
inflexible active site
site is preformed and
RIGID
Enzyme/substrate interaction
2. Induced fit model (hand in glove analogy)
count the flexibility of proteins
substrate fits into a general shape in the enzyme,
causing the enzyme to change shape
(conformation);
close but not perfect fit
of E + S
change in protein
configuration leads to
a near perfect fit of
substrate with enzyme
Active site
Has specificity can discriminate among possible
substrate molecules
- others recognize a functional group (group
specificity)
- only recognize one type of molecule (eg. D vs L
isomer)
(absolute specificity)
Relatively small 3D region within the enzyme
- small cleft or crevice on a large protein
Substrates bind in active site by weak non-covalent
interactions (hydrogen bond, hydrophobic and ionic
interaction)
Active site
The interactions hold the substrate in the proper
orientation for most effective catalysis
The energy derived from these interactions
binding energy
Binding energy is used, in large part to lower the
activation energy and stabilize the transition state
complex (ES*)
Each non-covalent interaction provides energy to
stabilize the transition state
ENZYME-
BIOLOGICAL
CATALYST
(3)
http://www.sumanasinc.com/webcontent/animations/
content/enzymes/enzymes.html
Classification of Enzymes
Have 6 categories
Each enzyme has an official international
name ending with ase and a classification
number
Number consists in 4 digits (referred to a
class and subclass of reaction
Classification of Enzymes
Classification of Enzymes
Example
1
(oxidoreductase)
alcohol
dehydrogenase
2
(transferase)
hexokinase
3
(hydrolase)
chymotrypsin
Reaction
O
CH3CH2OH + NAD+
CH3CH + NADH + H+
Example
4
(lyase)
pyruvate
decarboxylase
Removal of group
- nonhydrolysis
5
(isomerases)
alanine
racemase
6
(ligases)
pyruvate
carboxylase
Forming of
new bond - ATP
Reaction
O
CH3CH + CO2
OO
CH3C C O + H+
D-alanine
L-alanine
OO
CH3C C O + HCO3_
ATP
ADP+Pi
O
OO
O C CH2C C O
Enzyme Inhibitor
http://www.wiley.com/college/pratt/0471393878/stud
ent/animations/enzyme_inhibition/index.html
Enzyme Inhibitors
2 Types of inhibitors:
1. Competitive Inhibitors:
Compete with substrate for active site
Occupy the active site so that substare couldnt bind
there.
Inhibition can be overcome by adding substrate
molecules to the environment.
2. Non Competitive Inhibitors:
Attach to the enzyme in some other place (allosteric site)
than the active site.
Causes the enzymes active site to change its shape (no
longer complementary to substrate).
Enzyme can no longer catalyze the reaction.
Inhibition CANNOT be overcome.
Enzyme Inhibitors
Allosteric Enzymes
Allosteric enzymes
HOMOTROPIC ALLOSTERISM
eg. Tetrameric allosteric enzyme
composed of 4 identical subunits
Each subunit has a catalytic site
where substrate/effector will bound
and transformed to product
Once bound to active site, a
message will be transmitted via
conformational changes to an active
site on another subunit which
makes it easier for a substrate
molecule to bind and react at that
site
This type (substrate and effector)
are the same is called cooperative
or homotropic
HETEROTROPIC ALLOSTERISM
A dimer with nonidentical subunits
Subunit contain the active site
catalytic subunit
Subunit contains the site for
effector binding regulatory
subunit
Binding of a specific effector
molecule to the regulatory site on
the subunit sends a signal via
conformational changes to the
catalytic site on subunit
Substrate and effector different
kinds of molecules - heterotropic
Isoenzymes
Multienzymes
A group of noncovalently
associated enzymes that
catalyze 2 or more sequential
steps in metabolic/biochemical
pathway
eg. Glycolysis involve
multienzyme