CHAPTER 20

ENZYMES AND VITAMINS

A. Enzymes

Are biological catalysts

Catalyze nearly all of the chemical reactions that
take place in the body
Enzymes increase the rate of a reaction, but are
unchanged themselves at the end of the reaction
An uncatalyzed reaction might eventually take
place, but not at a rate quickly enough to meet
the bodys demands -- this is why we need
enzymes!

How Does An Enzyme Work?

Lowers the activation energy for a reaction.

As a result, less energy is needed to convert
reactants to products. This allows more molecules
to form product.
The enzyme does not affect the equilibrium
position of the reaction.

Enzymes Lower Activation Energy, But Dont

Change Equilibrium Position

Names and Classification of Enzymes

The enzyme name often describes the reaction

taking place, and the enzyme name always ends
with the suffix -ase.

Examples: oxidase catalyzes oxidation

lipid is hydrolyzed by lipase

What type of reaction would you think is catalyzed

by a hydrolase? An isomerase? An
oxidoreductase?
While I dont need you to memorize the classes
and subclasses in table 20.1, I could ask you to
tell me the type of reaction catalyzed by some of
the more obvious classes on the list.

B. Enzyme Action

Each enzyme has a unique three-dimensional

shape that binds and recognizes a group of
reacting molecules called substrates.
The active site of the enzyme is a small pocket
to which the substrate directly binds.
Some enzymes are specific only to one substrate;
others can bind more than one substrate.

Enzyme-Substrate Binding

Models of Enzyme Action

Early theory: lock-and-key model. Active site

(lock) had the same shape as the substrate (key).
Only the right shape key could bind.
Current theory: induced fit model. Active site
closely resembles but does not exactly bind the
substrate.

Allows for more flexibility in type of substrate

Also explains how the reaction itself occurs. As the
substrate flexes to fit the active site, bonds in the
substrate are flexed and stressed -- this causes
changes/conversion to product.

More Detail on Binding

An interactive animation on enzyme specificity
and binding:
http://www.wiley.com/legacy/college/boyer/047000
3790/animations/enzyme_binding/enzyme_binding.sw
f

C. Factors Affecting Enzyme Activity

Enzyme activity is defined as how fast an enzyme

catalyzes its reaction.
Many factors affect enzyme activity:

Temperature: most have an optimum temp around 37oC

pH: most cellular enzymes are optimal around
physiological pH, but enzymes in the stomach have a
lower optimum pH
Concentration of enzyme and substrate: have all of the
enzyme molecules been used up, even though substrate
is still available?

Reaction Rate vs. Enzyme and Substrate

Conc.

D. Enzyme Inhibition

Inhibitors stop the catalytic activity of the

enzyme.
There are different methods of inhibition:

Reversible: the inhibitor can be removed

Competitive inhibitors bind to the active site
Noncompetitive inhibitors bind somewhere other than the
active site and change the conformation of the active site
Irreversible: the inhibitor cannot be removed
Examples: toxins that form a permanent bond to the enzyme,
antibiotics (prevent bacterial cell wall formation)

How a Noncompetitive Inhibitor Works

Thinking about Inhibition

What kind of inhibitor competes with the

substrate for the active site?

In what kind of inhibition does the addition of

more substrate reverse the inhibition?

Competitive

Reversible, competitive

In what kind of inhibition is the structure of the

inhibitor not similar to that of the substrate?

Noncompetitive

E. Control of Enzyme Activity

We dont always need high levels of products of

enzyme-catalyzed reactions around. What kind of
control system is used to regulate amounts of
enzyme and products?
Two main methods: zymogens, and feedback
control.

Zymogens

Many enzymes are active as soon as theyre

made.
However, some are made in an inactive form and
stored. This inactive form is called a zymogen or
proenzyme.
To become active, the body needs only to cleave
off a small peptide fragment.
Many digestive enzymes are produced initially as
zymogens why?

Feedback Control

Some enzymes (allosteric enzymes) bind

molecules called regulators (different from the
substrate) that can affect the enzyme either
positively or negatively

Positive regulator: speeds up the reaction by changing the

shape of the active site -- substrate binds more effectively
Negative regulator: slows down reaction by preventing
proper substrate binding, again, by changing enzyme
shape

Feedback control: the end product acts as a

negative regulator. If there is enough of the end
product, it will slow down the first enzyme in a
pathway. Why does it slow down the first, and not
the third, or fourth?

Feedback Control

F. Enzyme Cofactors and Vitamins

Many enzymes require small molecules or metal

ions called cofactors to catalyze reactions
properly.

Some metal ions (such as Fe2+ and Cu2+) participate in

redox reactions with oxidases
Other metal ions stabilize either the enzyme or substrate
over the course of the reaction

Vitamins: molecules essential for normal health

that must be obtained from the diet (body does
not synthesize)

Classified as either water-soluble (contain polar groups) or

fat-soluble (nonpolar compounds)

Vitamins

Water soluble vitamins: not stored in the body,

excess are eliminated

Many are enzyme cofactors (B vitamins, vitamin C)

Fat soluble vitamins: stored in the body and not

eliminated -- can be toxic if you take too much

Not coenzymes or cofactors but play various important

roles in the body