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SUBSTRATE PRODUCT
(1833) - AnselmePayen
diastase
Louis Pasteur
ferments
Pepsin
Trypsin
Chymotrypsin
x-ray crystallography
Lysozyme
Structural biology
STRUCTURE
MECHANISM
Substrate binding
hydrophilic/hydrophobic characteristics
Enzymes can therefore distinguish between very similar
substrate
molecules
to
be
chemoselective,
regioselective and stereospecific.
Some of these enzymes have "proof-reading"
mechanisms.
Catalysis
Enzymes can accelerate reactions in several ways, all of
which lower the activation energy (G, Gibbs free energy)
1. By stabilizing the transition state:
Creating an environment with a charge distribution
complementary to that of the transition state to
lower its energy.
2. By providing an alternative reaction pathway:
Temporarily reacting with the substrate, forming a
covalent intermediate to provide a lower energy
transition state.
3. By destabilizing the substrate ground state:
Distorting bound substrate(s) into their transition state
form to reduce the energy required to reach the
transition state.
By orienting the substrates into a productive
arrangement to reduce the reaction entropy change.
The contribution of this mechanism to catalysis is
relatively small.
Dynamics
Enzymes are not rigid, static structures; instead they have
complex internal dynamic motions that is, movements of
parts of the enzyme's structure such as individual amino
acid residues, groups of residues forming a protein loop or
unit of secondary structure, or even an entire protein
domain.
Allosteric modulation
Allosteric sites are pockets on the enzyme, distinct from the
active site, that bind to molecules in the cellular
environment.
apoenzymesor apoproteins
Enzymes that require a cofactor but do not have one
bound
Holoenzyme
Coenzymes
INHIBITION
Competitive
Non-competitive
Uncompetitive
Irreversible
Industrial Applications
BIOLOGICAL FUNCTION
ENZYMES
3. Quantity
Enzyme production can be enhanced or diminished by a
cell in response to changes in the cells environment.
This form of gene regulation is called induction.
Note: Starch molecules, for example, are too large to be
absorbed from the intestine, but enzymes hydrolyze the
Regulation
Post-translational Modification
Quantity
Subcellular Distribution
Organ Specialization
1. Regulation
e.g.
phosphorylation,
glycosylation
myristoylationand
5. Organ Specialization
In multicellular eukaryotes, cells in different organs and
tissues have different patterns in gene expression and
therefore have different sets of enzymes available for
metabolic reactions.
INVOLVEMENT IN DISEASE
NAMING CONVENTIONS
EC
1
EC
Oxidoreducta
ses
Transferases
catalyze
oxidation/reduction
reactions
transfer a functional group
Hydrolases
2
EC
3
EC
Lyases
4
EC
Isomerases
5
EC
Ligases
6
Application
Biofuel
Industry
Biological
Detergen
t
Brewing
Industry
Culinary
Uses
Papain
Tenderize meat
cooking.
for
BIOCATALYSIS
Biocatalysts are either proteins (enzymes), or in a few
cases, they may nucleic acids.
Enzymes are necessary in all living systems, to catalyze
all chemical reactions required for their survival and
reproduction rapidly, selectively and efficiently.
Their application covers the production of desired
products for all human material needs, as well as in a
wide
range
of
analytical
purposes,
especially
in
diagnostics.
Properties
for
New
or
Biotechnological Processes:
The Use of Isolated or Intracellular Enzymes as
Biocatalysts
Biotechnological processes use one or more enzymes
with or without cofactors or cosubstrates as biocatalysts. When
more enzymes and cosubstrate regeneration are required,
fermentation processes with living cells are more effective than
processes with isolated enzymes.
A cofactor is a non-protein chemical compound that is
required for the protein's biological activity. These proteins are
commonly enzymes, and cofactors can be considered "helper
molecules" that assist in biochemical transformations.
ADVANTAGES compared with fermentations:
Higher space-time yields can be obtained than with living cells;
smaller reactors can then be used, reducing processing costs.
The risk that a desired product is converted by other enzymes
in the cells can be reduced.
The increased stabilty and reuse of immobilized biocatalysts
allows continuous processing for up to several months.
For such enzyme processes:
1. The required intra- or extracellular enzyme must be
produced in sufficient quantities and purity (free from
other disturbing enzymes and other compounds).
2. Cells without intracellular enzymes that may disturb the
enzyme process must be selected.
3. The enzyme costs must be less than 510 % of the total
product value
Advantage:
Enzymes are proteins that are essential for living
systems and, in the right place, they catalyze all chemical
conversions required for the systems survival and reproduction.
Disadvantage:
However, in the wrong place they can be harmful to an
organism.
Advantage:
Enzymes are normal constituents of food and, as with all
orally ingested proteins, they are hydrolyzed in the stomach and
intestine.
Disadvantage:
However, if enzymes or other proteins are inhaled as
small particles or aerosols in the lungs, they can be transferred
directly into the bloodstream.
An aerosol is
a colloid of
fine solid particles
or liquid droplets, in air or another gas.
(BIO)CHEMISTS
Determine the mechanism and properties of the
catalyzed processes, the kinetics of the enzymecatalyzed process and other relevant properties
(stability, solubility, pH- and temperature dependence of
equilibrium constants, selectivities).