Enzymes

11/5/07
Cell Biology 1 Metabolism

Preamble
First Law of Thermodynamics
- energy can neither be created or destroyed, but it
may be transmuted

Second Law of Thermodynamics
- entropy rules (chaos is the natural disorder of the
universe)

A. Cellular Metabolism
- refers to all of the enzyme-mediated (chemical)
reactions within a cell

Anabolic metabolism to build
Catabolic metabolism to break down


B. Activation Energy
- the speed of a reaction depends on the amount of
activation energy required to break existing bonds





In either kind of reaction, additional energy must be
supplied to start the reaction. This energy is the activation
energy.

Notes











Catabolic Reactions Associated with
Digestion (for Cell Respiration)

source: Madder, 9e




















Endergonic - Refers to a chemical
reaction that consumes energy.

Exergonic - Describes a chemical
reaction that releases energy in the form
of heat, light, etc.

Enzymes

Cell Processes and Applications 2 Metabolism


Source:
http://faculty.clintoncc.suny.edu/faculty/Michael.Gregory/files/Bio%20100/Bio%20100
%20Lectures/Enzymes/energy.htm


C. Catalyst
- a catalyst lowers the activation energy needed (by
stressing chemical bonds)

- a substance that speeds up a chemical reaction,
- but is itself not a part of the final product
- and would not cause a reaction that would not
normally occur given sufficient energy

- enzymes are the cells catalysts


Source:
http://faculty.clintoncc.suny.edu/faculty/Michael.Gregory/files/Bio%20100/Bio%20100
%20Lectures/Enzymes/energy.htm

D. Enzyme
- cells contain many different enzymes
- each of which catalyses a different reaction
- enzymes cannot speed up reactions that
would not occur on their own

- a given enzyme interacts with only one set of
reactants (customarily called substrates), or
occasionally with a few closely related ones












































Exothermic vs Exergonic
Endothermic vs Endogonic

Neither exergonic and exothermic are
synonymous nor endergonic and
endothermic, however, if you find it easier
to think of them as synonymous, then go
for it.

The -thermic terms tend to be limited to
describing heat energy (!H) while the -
gonic terms are broader, referring to free
energy (!G). That is, two possible things
can drive a reaction spontaneously
forward: A release of energy as reactants
go to products or an increase in entropy as
reactants go to products.

!G takes into account not only changes in
internal energy but also changes in entropy
(!S) that may accompany a reaction. For
most ordinary simple chemical reactions,
the entropy factor is not great, so chemists
usually talk about !H. For many biological
reactions,the entropy factor is significant,
so biochemists usually talk about !G. !G
= !H - (T x !S ). Despite the signs, which
have to do with the way these terms are
defined, !G is the sum of the 2 effects.

The -thermic terms more or less only deal
with the release of energy while the -gonic
terms refers to both the release of energy
and an increase in entropy.
Enzymes

Cell Processes and Applications 3 Metabolism
- enzymes are mostly globular proteins
- with one or more invaginations on their surface,
called the active site
- where catalysis occurs
Source: http://en.wikipedia.org/wiki/Enzyme

- in order for catalysis to occur the substrate must fit
perfectly into this depression (Lock & Key theory
diagram)



- proteins are not rigid, so the enzyme may give a
little allowing an induced fit (diagram)


source: http://www.accessexcellence.org/AB/GG/

E. Factors Affecting Enzyme Activity

1. Temperature
- human enzymes work best between 35 and 40C











































An allosteric enzyme has an active site
where substrate molecules bind and
another site that binds with intermediate or
end-product molecules.
Enzymes

Cell Processes and Applications 4 Metabolism
- rate of chemical reaction is reduced by half for
every 10C drop
- below this temp. protein is not flexible to allow
induced fit
- and becomes deactivated (! denatured,
because deactivation, unlike denaturation is
reversible if the enzyme is warmed)

- above this temp. the H-bonds are too weak
- upper limit of enzyme activity before being
denatured is 40C
- damaged caused by mild heating may in
some cases be reversible, but
- continued warming would continue to
denature more and more of the enzyme until
no active enzyme remains, e.g., amylase
would be completely denatured at 80C

- Denaturing results in the
! loss of the active site

2. pH
- optimum pH between 6 to 8 (exceptions, e.g., pepsin
pH2)
- denatures protein by disrupting bond charges
- disrupts H-bonds between R groups
! loss of the active site

3. Inhibitors
- Competitive Inhibitors blocks active site












































Enzymes

Cell Processes and Applications 5 Metabolism
- A competitive inhibitor binds reversibly to the
enzyme, preventing the binding of substrate. On the
other hand, binding of substrate prevents binding of
the inhibitor, thus substrate and inhibitor compete
for the enzyme.
Source: http://en.wikipedia.org/wiki/Enzyme

- Non-competitive Inhibitor
- e.g., heavy metal poisoning, e.g, Lead or
Mercury
Source: http://en.wikipedia.org/wiki/Enzyme

- Binds to the enzyme and alters the shape of the active
site, so the substrate no longer fits

4. Cofactors
- often enzymes use additional chemical components
to aid catalysis
- called cofactors,
e.g.,
- some enzymes have metal ions locked into their
active sites
- ions that draw electrons from substrate molecules
- e.g., carboxypeptidase has a zinc ion that draws
electrons from the bonds joining a.a.

- why the need for trace elements for good health,

- nonprotein organic molecules used as cofactors are
called coenzymes
- vitamins are coenzymes



























Enzymes

Cell Processes and Applications 6 Metabolism
- an inactive enzyme (protein) is an apoenzyme
- apoenzyme + coenzyme = holoenzyme (a fully
functional enzyme)

- in many enzyme-catalyzed oxidation-reduction
reactions, energy bearing electrons are harvested
- the electrons pass from active site to coenzyme
(electron acceptor)
- which carries them to another enzyme
catalysing another reaction, and then returns
for another load

- coenzymes shuttle energy in the form of an atom
from one place in the cell to another (diagram)

- NB coenzymes do not provide E, they provide
the atom, which in turn supplies the E to the
enzyme mediated reaction

e.g., in Cell Respiration

- NAD (nicotinamide adenine dinucleotide)
- aka Niacin
- a coenzyme that functions as an electron acceptor in
many oxidation reactions of the cell

- NADH
2
(NADre) is the reduced form, or energy
rich form
- a coenzyme that functions as an electron
donor, involved in reduction reactions







Enzymes

Cell Processes and Applications 7 Metabolism
Vocab Extras (Endocrine System):

Thyroxine [Thyroxin] (T4)
- Hormone secreted by the thyroid gland (neck)
- Stimulates the body's oxidative metabolism;
regulates growth and development

Thyroid Stimulating Hormone (TSH)
- Secreted by the anterior pituitary
- Stimulates the thyroid glandand therefore
thyroxine

- e.g., thyroxine action increases metabolic heat
reducing cold stress



Source: http://www.biol.sc.edu/courses/bio102/f97-41.html

TSHRH = "Thyroid Stimulating Hormone Releasing Hormone"
TSH = "Thyroid Stimulating Hormone"
TH = "Thyroxine"