PBIO-534 CELL & MOLECULAR PHYSIOLOGY

Enzyme Kinetics 1 – Properties of Enzymes

This material is most likely review, but it is important to understand the nomeclature. We will be
using the nomenclature to describe how enzymes work as well as the strategies for regulating enzymes.
This lecture focused on enzyme kinetics and thermodynamics in general while the next lecture focuses
on the enzyme kinetics as it relates to biochemistry.
NOMENCLATURE
Reactions can be defined by:
a) the number of substrates – monomolecular, bimolecular, termolecular
b) their kinetics – zero order, first order, second order

Zero Order Reactions:

The reaction velocity is dependent only on the concentration of the catalyst/enzyme. It does not
change with various concentrations of the substrate. So if you want to make the reaction faster, you just
need to add more enzyme. These reactions are incredibly common in biochemistry (ex: metabolism).

First Order Reactions:

The rate of reaction is proportional to the substrate concentration – as substrate concentration
increases, so does the velocity. These reactions are also very common in biochemistry.
PBIO-534 Enzyme Kinetics I: Properties of Enzymes CELL & MOLECULAR PHYSIOLOGY

Second Order Reactions:

This is usually referring to bimolecular reactions (ex: S + A → P) and depends on lots of other factors
besides substrate concentrations.

THERMODYNAMICS
Basically, we want to use thermodynamics to predict whether a reaction is favorable and
spontaneous. After all, if we want to regulate a process, we must understand what makes it favorable.
The first two laws of thermodynamics on their own are not really sufficient to make such a prediction,
so Gibbs combined the two laws to achieve this goal.

First Law of Thermodynamics – Conservation of Energy

The complicating factor here is that we must take both the system and surroundings into account.
• system = reaction that we are studying (ex: A+B → P)
• surroundings = the rest of the universe
We use this law to define two types of reactions
Exothermic vs Endothermic
-systems that give off heat/energy -systems that require heat/energy
-enthalpy change is negative -enthalpy change is positive
PBIO-534 Enzyme Kinetics I: Properties of Enzymes CELL & MOLECULAR PHYSIOLOGY
-products are at a lower energy state -products are at a higher energy state
than the reactants (products are more than the reactants (reactants are
stable) more stable)

So this law can tell us whether a reaction is exothermic or endothermic – does it form products
that are more stable than the reactants – BUT that does not necessarily correspond to whether a reaction
is spontaneous or not. Usually, exothermic reactions are spontaneous but not always.

Second Law of Thermodynamics – The Increasingly Disordered Universe

Entropy is a measure of disorder and randomness and occurs spontaneously in the universe.
PBIO-534 Enzyme Kinetics I: Properties of Enzymes CELL & MOLECULAR PHYSIOLOGY
There is no such thing as negative entropy, but there can be a negative change in entropy. When
taking the surroundings into account, there is still an overall increase in disorder. Protein folding
is an example of this. A protein becomes more ordered (a decrease in entropy) when it folds, so
one would think that this process is not thermodynamically favorable. However, the protein is
the system and the aqueous environment is the surroundings. So by taking in account the fact
that the water molecules around the protein become much more disordered, there is a net
increase in entropy in the universe.

Gibbs Free Energy – Combining the two laws

By combining the first and second laws of thermodynamics, we can now predict whether
reactions are favorable and spontaneous.

• If G is negative → the reaction is spontaneous and thermodynamically favorable

• If G is positive → no reaction unless more energy is added
• If G = 0 → equilibrium (This equilibrium means that the transition between products and
reactants are occurring at the same rate. This is not a steady state equilibrium. Appreciate
the power of equilibrium, as it can be used to drive reactions.)
Here is an example of an exothermic reaction:

ENZYMES
Why do we care about enzymes? All this talk about Gibbs is great because we can now
determine whether reactions are spontaneous and thermodynamically favorable; however, Gibbs does
NOT address the issue of how fast these reactions can occur. Remember, spontaneous does not mean
PBIO-534 Enzyme Kinetics I: Properties of Enzymes CELL & MOLECULAR PHYSIOLOGY
fast. But enzymes are catalysts and can, therefore, be used to speed up the rate of reaction. In effect,
enzymes make reactions more practical in terms of biology.
Enzymes are important because they can lower activation energy (Ea). Ea is like a down payment
of energy needed to make the reaction occur. Thus enzymes make the reaction cheaper – you need to put
less energy in to drive the same reaction.

Enzymes do NOT change the reaction equilibrium or change underlying thermodynamics. But they DO
change rate at which equilibrium is reached – they help a reaction that would occur normally to occur
faster.

Enzymes lower the activation energy of reactions by creating an environment that encourages the
transition of reactants to products. For example, they can bind to the substrate in order to stabilize the
transition state.
PBIO-534 Enzyme Kinetics I: Properties of Enzymes CELL & MOLECULAR PHYSIOLOGY

In addition, remember that reactions follow kinetic molecular theory. So molecules are moving at
random and can collide. However, not every collision results in a reaction – there must be sufficient

energy and the molecules must collide in the correct orientation. Enzymes can help orient the molecules
in order to make more productive collisions.