- Reactions in the biologic systems are

- There is always a backward and forward always coupled

reaction.

- Same as action potential (threshold

must be reached)
- The forward reaction occurs more
- If activation is low, it is easy to reach,
rapidly than the backward reaction
thus reaction could occur rapidly (faster
- There is still backward reaction (but in
reactions have lower activation
small instances)
energies)

- Spontaneous (can occur without the aid

of energy)
 - Collision theory (increased no. of
collision, more products – by increasing
temp to increase kinetic energy)
2. Reactant concentration
- Increased concentration, increased rate
or probability of the products to collide
with one another.
3. Presence of Catalyst (e.g., enzymes)
- Aids reactions, or promote reactions.

- There is energy release

- [exergonic] The initial energy of the
reactants is higher than the energy of
the products.
- Activation energy is still needed

- A number that tells us which is the

favored reaction.
- Tells us which is faster

- [Endergonic] Initial energy of the

reactants is lower than the products.
Energy stored in products is higher.
- Endergonic requires higher activation
energy to proceed.

FACTORS AFFECTING REACTION RATES - Ratio of the product over the reactants

1. Temperature
- Higher kinetic energy
- Increased reaction rate
- Molecules tend to move faster
- Product is favored (Keq > 1 – numerator
is greater than the denominator)
- With increased concentration of the
product, more product is produced.
(Creation of product is faster – forward
- Enzymes lower the threshold
reaction)
- They work by forming complexes with
the substrate resulting in a lower
activation energy

- Backward reaction is favored (Keq < 1)

- Enzymes are proteins that promote

biological reactions however they are
not used up (they are present during
and after the reaction)

- Cancelled out
 - Enzymes lower activation energy hence
- Substrate (or reactant) binding speeding up the chemical reaction
- Enzyme binds to the substrate (enzyme-
substrate complex)
- Catalytic step (bond breaking)
 - Apoenzymes

- Active site of the enzyme

- Prosthetic groups can either be

cofactors or coenzymes (very difficult to
separate because they are covalently
bonded)
 SUBSTRATE CONCENTRATION

- Enzymes are already saturated, no

- Iron can be a prosthetic group. more active sites for binding
- Iron can be present in other heme-
containing enzymes

- Highest at optimum temperature.

- If it exceeds the optimum temperature,
it declines (denatured)

- For every enzyme there is optimum pH

- Pepsin optimum at low pH (stomach);
Trypsin optimum at pH 7-8 (small
intestine – by the pancreas)
- Combination of zero and the first order
- hyperbolic curve
- as the reactant concentration increases,
the rate increases
- as the concentration rises, velocity
becomes constant

- enzyme a has higher activity

- relationship between affinity and Km is
inverse
 - Reversible if substrate concentration is
increased

- Vmax value decreases

- Km and affinity are constant

- michaelis contant increases

- Km increased, Vmax unaffected
- Km increased  affinity decreased

- Inhibitor binds to the other site (instead

of the active site) – ALLOSTERIC SITE
- It inactivates the enzyme
- Lowers the overall reaction rate
- Reversible
- Vmax change as a consequence of Km
reduction
- Affinity is increased

- Only competitive inhibition is

reversible, the others are irreversible
- LYASES – enzymes that break bonds
- HYDROLYASES break bonds by adding
water

- Pepsin  initially secreted as

pepsinogen (inactive)
- If exposed to HCl  activates pepsin
READING
ASSIGNMENT:
Different
Mechanism of
Enzyme Catalysis
- Electron
transport