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Chemical Biology (Biomolecules)
ENZYMES
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Enzymes
Proteins that act as
catalysts
for biochemical
reactions
Enzymes
Undergo all the reactions of
proteins
including
denaturation
They are a "true
catalyst
" - they remain
unchanged
after the reaction
General classes of enzymes
Simple
enzyme (
protein
only)
Conjugated
enzyme (nonprotein part +
protein
part)
Apoenzyme
Protein part of a
conjugated
enzyme
Cofactor
Nonprotein
part of a
conjugated
enzyme
Holoenzyme
Biochemically
active
conjugated
enzyme
Types of cofactors
Small
organic
molecules (co-enzymes or co-substrates)
Inorganic
molecules (non-metallic ion cofactor Cl-)
Derived from dietary
vitamins
Derived from dietary
minerals
Substrate
Reactant in an enzyme-catalyzed reaction, the
substance
upon which the enzyme "acts" and is
converted
to products
Nomenclature of enzymes
Unsystematic/Nonsystematic name (suffix
-ase
identifies it as an enzyme, exceptions have suffix
-in
)
Systematic name (e.g. ATP: creatine phosphotransferase (EC
2.7.3.2
))
Six major classes of enzymes
Oxidoreductases
Transferases
Hydrolases
Lyases
Isomerases
Ligases
Oxidoreductases
Catalyze oxidation-reduction reactions
Oxidation occurs when hydrogen atoms
decrease
and
oxygen
atoms increase, reduction is the opposite
Transferases
Catalyze the
transfer
of a
functional
group from one molecule to another
Hydrolases
Catalyze
hydrolysis
reactions, splitting or
separation
Lyases
Catalyze the addition or
removal
of groups to/from substrates without
hydrolysis
Isomerases
Catalyze the
interconversion
of isomers, the
rearrangement
of atoms within a molecule
Ligases
Catalyze the joining or formation of new
bonds
, not
separation
Models of enzyme action
Active site
- where
substrate
binds
Enzyme-substrate complex
-
intermediate
reaction species formed when substrate binds to active site
Enzyme remains unchanged after catalysis, can
catalyze
again
Enzymes as
catalysts
Can
speed
up reactions greatly
Are not
permanently
altered or
consumed
by the reaction
Most are
proteins
, some are
RNA
Have
complex
, specific structures unlike metal
catalysts
Work under mild conditions of
temperature
and
pressure
Fermentation
in
yeast
First use of
enzymes
as a
reference
Enzymes are the first recognition that components are
separable
from
living
cells
Most
catalysts
enzymes are
protein
, though some are made of RNA
Active site
Each enzyme has an active site where
catalysis
takes place
Catalysis
The increase in rate of a chemical reaction due to an added substance known as a
catalyst
Enzyme catalysts
Have
complex
, specific structures
The catalysis may be associated with
conformational
changes
Work under
mild
conditions (T and P)
Act only on a specific
substance
(substrate)
Some will act on the
L-enantiomer
, but not the
D
Some are more "
Promiscuous
" than others
Knowing "
WHEN
" and "
WHY
" enzymes work is as important as "HOW"
Classes of Enzymes
Oxidoreductases
Transferases
Hydrolases
Lyases
Ligases
Isomerases
Reaction velocity
How fast the reaction is catalyzed by the enzyme, expressed as
micromol
of product formed per
minute
Factors that affect reaction velocity
Temperature
pH
Substrate
concentration
Enzyme
concentration
Presence of
inhibitors
Presence of
cofactors
As temperature increases
The reaction rate
increases
At the optimum temperature
The
reaction rate
is
fastest
If temperature increases further
The reaction rate
decreases
due to enzyme
denaturation
Optimum temperature for human enzymes
37
C (body temperature)
Increased temperature (high fever)
Leads to
decreased
enzyme activity
If enzymes are
denatured
Some biochemical reactions will
shut down
Optimal pH for most enzymes
7.0
-
7.5
Pepsin
Optimum pH =
2.0
Trypsin
Optimum pH =
8.0
As pH increases for Trypsin
The reaction rate
increases
If pH continues to increase for enzymes
The reaction rate
decreases
due to
denaturation
Increasing substrate concentration
Increases
enzyme
activity (with
constant
enzyme concentration)
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