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