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Summary: Important Statements About Enzymes

● Most are proteins


● Primary purpose is to increase the rate of a chemical reaction
● Most reactions occur a million times faster (or more) with an enzyme
● Many can be isolated from cells and studied in a test tube
● They are highly specific for certain substrates (reactants)
Summary: Important Statements About Enzymes, cont’d
● Most are named by adding the suffix “ase” to the root name of the substrate
molecule it is acting upon (Hence: lipase, peptidase, sucrase)
● They occur in small amounts in the cell
● They are not consumed or degraded in a chemical reaction
● They often function within metabolic pathways and are regulated to meet the
needs of the cell
● Even if one enzyme is non-functional, the results can be disastrous to the cell and
the organism
Summary: Important Statements About Enzymes, cont’d
● Most are named by adding the suffix “ase” to the root name of the substrate
molecule it is acting upon (Hence: lipase, peptidase, sucrase)
● They occur in small amounts in the cell
● They are not consumed or degraded in a chemical reaction
● They often function within metabolic pathways and are regulated to meet the
needs of the cell
● Even if one enzyme is non-functional, the results can be disastrous to the cell and
the organism
● They don’t affect the thermodynamics of a reaction, they only affect the rate of
the reaction.
First Law of Thermodynamics

Figure 3-8 Essential Cell Biology (© Garland Science 2010)


Second Law of
Thermodynamics
Second Law of
Thermodynamics
Spontaneous reaction

Requires energy input – not spontaneous


Figure 3-5 Essential Cell Biology (© Garland Science 2010)
Anabolic reactions are those
that synthesize compounds.
Energy is required for these
reactions.
Reactions that break down
molecules are called catabolic
reactions. Energy is released
when molecules are broken
down.
ATP produced by catabolic reactions provides the energy for anabolic reactions.
Anabolic and catabolic reactions are therefore coupled (they require each other)
through the use of ATP.
A sugar molecule has
higher free energy
(and more order) than
CO2 and H2O
● The energy in one
glucose molecule is
used to produce 36
ATP.

● ATP has approximately


the right amount of
energy for most
cellular reactions.

● ATP is produced and


used continuously.

● The entire amount of


ATP in an organism is
recycled once per
minute.

● Most cells maintain


only a few seconds
supply of ATP.
Reactions with enzymes are up to 10 billion times faster than those without
enzymes.

Enzymes typically react with between 1 and 10,000 molecules per second.

Fast enzymes catalyze up to 500,000 molecules per second.

Substrate concentration, enzyme concentration, Temperature, and pH


affect the rate of enzyme reactions.
● At lower concentrations, the active sites on most of the enzyme molecules
are not filled because there is not much substrate.
● Higher concentrations cause more collisions between the molecules. With
more molecules and collisions, enzymes are more likely to encounter
molecules of reactant.
● The maximum velocity of a reaction is reached when the active sites are
almost continuously filled. Increased substrate concentration after this point
will not increase the rate. Reaction rate therefore increases as substrate
concentration is increased but it levels off.
● Higher temperature generally causes more collisions among the
molecules and therefore increases the rate of a reaction. More collisions
increase the likelihood that substrate will collide with the active site of the
enzyme, thus increasing the rate of an enzyme-catalyzed reaction.
● Above a certain temperature, activity begins to decline because the
enzyme begins to denature.
● The rate of chemical reactions therefore increases with temperature but
then decreases.
● Each enzyme has an optimal pH.
● A change in pH can alter the ionization of the R groups of the amino acids.
When the charges on the amino acids change, hydrogen bonding within the
protein molecule change and the molecule changes shape. The new shape
may not be effective.
● The diagram below shows that pepsin functions best in an acid
environment. This makes sense because pepsin is an enzyme that is
normally found in the stomach where the pH is low due to the presence of
hydrochloric acid. Trypsin is found in the duodenum, and therefore, its
optimum pH is in the neutral range to match the pH of the duodenum.
Competitive Inhibition Noncompetitive Inhibition
In competitive inhibition, a similar- ● Another form of inhibition involves
shaped molecule competes with an inhibitor that binds to an
the substrate for active sites. allosteric site of an enzyme. An
allosteric site is a different
location than the active site.
● The binding of an inhibitor to the
allosteric site alters the shape of
the enzyme, resulting in a
distorted active site that does not
function properly.
● The binding of an inhibitor to an
allosteric site is usually
temporary.
Many enzymatic pathways are
regulated by feedback inhibition.
As an enzyme's product
accumulates, it turns off the
enzyme just as heat causes a
thermostat to turn off the
production of heat.

The end product of the pathway


binds to an allosteric site on the
first enzyme in the pathway and
shuts down the entire sequence.

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