BIOCATALYSIS

Chapter 4

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Outline
4.1 General characteristcs of enzymes
4.2 Characteristics of enzymes
4.3 Enzymes speed up chemical reactions
4.4 Enzymes required in minute quantities
4.5 Enzymes are highly specific
4.6 Temperature affect enzymes activity
4.7 pH affect enzymes activity
4.8 Other factors affect enzymes activity
4.9 Enzymes catalyse reversible reaction
4.10 Enzymes and cofactors
4.11 Enzymes and inhibition
 4.1 Enzymes
An enzyme is a protein molecule that is a biological
catalyst that carry out most catalysis in living
organisms. Enzyme has several charateristics.
1. Speed up chemical reaction - Lowers activation
energy necessary for new bonds to form or to break
existing bond
2. Required in minute quantities
3. Most enzymes act specifically with only one
reactant (called a substrate) to produce products.
4. Unique three-dimensional shape of an enzyme
enables it to stabilize a temporary association
between substrates.
5. The enzymes itself is not changed or
consumed in the reaction, can be used over
and over.
Eg. Carbonic anhydrase (enzyme in RBC)
6. Sensitive to pH and temperature
7. Some can catalyse reversible reaction.
8. Some requires cofactor
9. Can be inhibit by inhibitors
Activation energy
Every chemical reaction usually has an energy barrier
which prevents them from occuring spontaneously
The energy barrier is called the (Activation Energy,
E A)
Activation energy- minimum energy needed to break
the bonds in molecule and start a reaction so that an
effective reaction occur.
Enzymes speed up reaction by lowering energy barrier
(activation energy) so TRANSITION STATE can be
reached earlier
Transition state – unstable condition of reactant
molecules that have absorbed enough free energy to
react

 Activation Energy and Catalysis
Free energy (G)

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Endergonic Reaction – Not occurs spontaneously and
requires
energy input. (∆G positive)
Exergonic Reaction - Occurs spontaneously and releases
excess
free energy. (∆G negative)
Free energy (G)

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How Enzymes Work
Most enzymes are globular proteins with one or
more pockets or clefts, called active sites for
substrates to bind.
Substrate molecules must fit precisely into an
active site.
Amino acids side group of enzyme end up very
close to certain bonds of the substrate.
These groups interact chemically with the
substrate, usually stressing or distorting a
particular bond and consequently lowering the
activation energy needed to break the bond.
After the bonds of the substrates are broken, new
bonds are formed, the substrates have been
converted to products.
Products dissociate from the enzyme.
The enzyme ready to binds its next substrate and
begin the cycle again!..
Enzyme Catalytic Cycle

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COFACTORS
Enzyme Cofactors - Enzyme function assisted by
additional chemical components.
Metal ions – non organic. Eg. Metallic ion zinc,
molybdenum, manganase.
Coenzyme – cofactor is a nonprotein organic
molecules non covalently bound to enzyme
(loosely bound).Eg. Vitamin B6 and B12.
Prosthetic groups - a nonprotein organic melecules
covalently bound to enzymes (tightly bound). Eg.
Heme
Biochemical Pathways
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