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Biochemistry Reviewer
Biochemistry Reviewer
Biochemistry Reviewer
ELASTIN
ENZYMES
Terms:
1. Holoenzyme – active enzyme with its nonprotein component
2. Apoenzyme – enzyme without its nonprotein component; inactive
3. Cofactor – if the nonprotein moiety is a metal
4. Coenzyme – if the nonprotein moiety is a small organic molecule; commonly derived from
vitamins
a. Co-substrate – Only transiently associate with the enzyme; dissociate from the enzyme in an
altered state (i.e. NAD+ - contains niacin)
b. Prosthetic group – if permanently associated with the enzyme (i.e. FAD – contains
riboflavin)
Isozyme – tissue-specific forms of an enzyme; catalyze the same reaction but differ in their amino acid
composition (primary structure)
The lower the free energy of activation, the faster the
reaction rate. Enzymes lower the free energy of activation
by (1) providing an alternate, energetically favorable
reaction pathway and (2) stabilizing the transition state of
this pathway.
MICHAELIS-MENTEN KINETICS
- Describes how reaction velocity varies with
substrate concentration
E + S <-> ES <-> E + P
Assumptions:
1. [S] >>>> [E]
2. Steady state assumption: concentration of [ES] does not change with time (rate of formation
is equal to the rate of breakdown)
3. At the start of the reaction, the concentration of product is very small and thus the rate of
the back reaction is negligible.
Conclusions:
1. Michaelis constant (Km) – reflects the affinity of an enzyme for its substrate; numerically equal
to the substrate concentration at which the reaction velocity is equal to ½ Vmax; not affected by
enzyme concentration
o Low Km: high affinity
o High KM: low affinity
2. Rate of reaction is directly proportional to enzyme concentration.
3. First order reaction: [S] <<< Km; rxn velocity is thus directly proportional to substrate
concentration
Zero order reaction: [S] >>> Km: rnx velocity is constant and independent of substrate
concentration
INHIBITION OF ENZYME ACTIVITY
1. Competitive inhibition: apparent Km increases
2. Noncompetitive inhibition: decrease in apparent Vmax; Km is not affected
BIOENERGETICS
Enthalpy: measure of the change in heat content of the reactants and products
Entropy: measure of the change in randomness or disorder of the reactants and products
Free energy (G): predicts the direction in which a reaction will proceed; measure of the capacity of a
system to do work as it proceed to equilibrium
∆G: represents the change in free energy at any specified concentration of reactants and products
If negative: reaction is exergonic; reaction will proceed forward
If positive: reaction is endergonic;
0
∆G (standard free energy change): energy change when the reactants and products are at concentration
of 1 mol/L; constant
PRIMARY CoQ DEFICIENCY: will decrease ATP production due to impedance of e- transfer from
complexes I and II; manifests as muscle weakness and exercise intolerance
CYANIDE POISONING: binds and inactivates Complex IV
Site-specific inhibitors: all e- carriers before the block are reduced while those after are oxidized
Reperfusion injury: incomplete reduction of O2 to water (caused by the rapid return of O2) produces
ROS which damage DNA and proteins and cause lipid peroxidation
‘antioxidant’ enzymes: superoxide dismutase, catalase, glutathione peroxidase