Enzymes = Biological catalysts
Large proteins Permit reactions
to go at
body conditions
Process millions
of molecules
every second
Model of
trios-p-isomerase
Very specific
react with only
1 or a few types
of molecules
(substrates).
Effect of enzymes on Eact
For a reaction to go it
must get over the
activation energy hurdle.
Energy
Enzyme catalyzed
reaction
This reduces the
activation energy.
It makes it faster.
reactants
H
Enzymes change
how a reaction
will proceed.
Eact
products
Enzyme nomenclature
Name is based
on:
what with or
-ase
how
ending
it reacts
Examples
To react with lactose.
lactase
To remove carboxyl from pyruvate.
pyruvate decarboxylase
Classification of enzymes
Based on type of
reaction
catalyze a redox reaction
Oxireductase
transfer a group
Transferasecatalyze hydrolysis rxns
Hydrolase Make or break double bonds
Lyase
Isomerasesjoin two molecules
Ligase
rearrange atoms
The Active Site
Enzymes are typically HUGE proteins, yet only a
small part are actually involved in reaction.
The active site has two basic components.
Catalytic site
Binding
Site
Where reaction
occurs
holds
substrate
in
place
Substrate
Enzyme
Enzyme-substrate complex
Step 1: (All of these steps are in equilibrium)
Enzyme and substrate combine to form complex
E
+
S
ES
Enzyme
Substrate
Complex
ES
Enzyme-product complex
Step 2:
An enzyme-product complex is formed.
ES
ES
EP
transition
state
EP
Product
The enzyme and product separate
EP
E + PThe product
is made
EP
Enzyme is
ready
for
another
substrate.
Lock and Key Theory
Enzyme is lock and Substrate is
key.
Substrate
structure
must fit into
enzymes
structure.
Induced Fit Theory
Active site may not fit substrate.
Site must change in
order to form the
complex.
Effect of Temp on Enzymatic
Rxns Optimum Temp
Reaction
Rate
usually
37ooC.
Temperature
Exceeding
normal pH
and
temperature
ranges
always
reduces
enzyme
reaction
rates.
Effect of pH on Enzymatic Rxns
Reaction
Rate
Most enzymes
work best near
pH 7.4
though not
all.
pH
Examples of optimum pH
Enzyme Location Substrate
Pepsin
Stomach Peptide Bonds
Urease
Urea
Liver
Small Intestine
Sucrase
Sucrose
Pancreatic
Amylase Pancrease Amylose
Small
Peptide Bonds
Trypsin
Intestine
Arginase Liver
Arginine
pH
2
5
6.2
7
8
9.7
Rate of reaction
(velocity)
Effect of substrate
concentration
For non-enzyme catalyzed reactions
Rate
Rateincreases
increasesifif
concentration
concentrationof
of
the
thesubstrate
substrateincreases
increases
Substrate concentration
Effect of substrate concentration
For Enzyme catalyzed reactions
Rate of reaction
(velocity)
Rates increase but only to a certain point
Saturation point
Vmax w/ more enzyme
Vmax w/ some enzyme
At
At V
Vmax
max
the
the enzyme
enzyme is
is working
working as
as fast
fast as
as itit
can.
can.
Rate
Rateis
islimited
limitedby
by
the
theconcentration
concentrationof
ofboth
both
the
thesubstrate
substrateand
andenzyme.
enzyme.
Substrate concentration
Factors Affecting Enzyme
Activity
Rates increases when amount
Enzyme Activity
of Enzyme increases
Enzyme Concentration
COMPETITIVE INHIBITOR
ENZYME INHIBITION
Enzyme
mistakes
inhibitor for
substrate
Effect reversed by increasing substrate
concentration.
Resembles
substrate:
Competes with
substrate for
the active site.
Competitive Inhibitors
O
Sulfa Drugs
OH
Folic Acid : obtained
H N
p-aminobenzoic acid
from the diet or
H
from microorganisms in the intestinal tract.
Microorganisms make folic acid from PABA.
H2N
N
N
N
N
OH
O
NH
C NH CH C OH
CH2
CH2
C OH
O
Sulfa Drugs
Competitive Inhibitors
Illnesses caused by invading microorganisms like
bacterium can be combated using a competitive inhibitor
called an antimetabolite.
Folic Acid is a coenzyme in many biosynthetic processes
like synthesis of amino acids and nucleotides.
In 1930 it was discovered that sulfanilamide, along with
sulfapyridine and sulfathiazole, could kill many types of harmful
bacteria and help cure several diseases.
The bacteria are tricked into using the sulfa drugs instead of
PABA.
They make a molecule that also has a folic acid type of structure
but is not exactly the same.
When they try to use this fake folic acid as a coenzyme, not only
doesnt it work, it is now a competitive inhibitor.
Many of the bacterias amino acids and nucleotides cannot be
made, and the bacteria die.
Sulfa Drugs
Competitive Inhibitors
ENZYME INHIBITION
NONCOMPETITIVE INHIBITOR
Changes
Enzyme shape
so substrate
cant react
Binds
somewhere
other than the
active site.
Effect cant be reversed by increasing substrate
concentration.
Cofactors
Cofactor = Non protein Group
needed to activate apoenzyme
Co2+
Co
Apoenzyme
protein portion
Inactive
ES
2+
Co2+
Coenzymes
= organic molecule that temporarily binds
to apoenzyme in order for it to work.
apoenzyme
coenzyme
often
Vitamins
holoenzyme
Vitamin Coenzymes
Vitamin
Thiamine (B1)
Coenzyme Made
Thiamine
Pyrophosphate
Riboflavin (B2) FAD, FMN
folic acid
biotin
tetrahydrofolic acid
biocytin
Function
Decarboxlation
Electron Transfer
amino acid metabolism
CO2 fixation
Pantothenic Acid
Coenzyme A
acyl group carrier
Ascorbic Acid (C)
Vitamin C
Collagen synthesis
Healing
Learning Check/Seatwork
Match the type of reaction with an enzyme.
1) aminase 2) dehydrogenase
3) isomerase 4) synthetase
A. Converts a cis-fatty acid to a trans-fatty acid.
B. Removes 2 H atoms to form a double bond.
C. Combines two molecules to make a new
compound.
D. Adds NH3.
Learning Check/Seatwork
5. The active site is
(1) the enzyme
(2) a section of the enzyme
(3) the substrate
6. In the induced fit model, the shape of
the enzyme when substrate binds
(1) stays the same
(2) adapts to the shape of the
substrate
Learning Check/Seatwork
Sucrase has an optimum temperature of 37C
and an optimum pH of 6.2. Determine the
effect of the following on its rate of reaction.
1) no change
2) increase
3) decrease
7. Increasing the concentration of sucrose
8. Increasing the concentration of sucrase
9. Changing the pH to 4
10. Running the reaction at 70C
Solution
Match the type of reaction with an enzyme.
1) aminase 2) dehydrogenase
3) isomerase 4) synthetase
1.
2.
3.
4.
D. Adds NH3.
B. Removes 2 H atoms to form a double bond.
A. Converts a cis-fatty acid to a trans-fatty acid.
C. Combines two molecules to make a new
compound.
Solution
5. The active site is
(2) a section of the enzyme
6. In the induced fit model, the
shape of the enzyme when
substrate binds
(2) adapts to the shape of the
substrate
Solution
Sucrase has an optimum temperature of 37C
and an optimum pH of 6.2. Determine the
effect of the following on its rate of reaction
1) no change
2) increase
3) decrease
7. 1 Increasing the concentration of sucrose
8. 2 Increasing the concentration of sucrase
9. 3 Changing the pH to 4
10. 3 Running the reaction at 70C
