IKA QURROTUL AFIFAH

Metabolism Summary

A long pathway to
convert sugar into
energy

Enzyme as
reaction catalyst
With the exception of a few classes of catalytic RNA molecules all enzymes
are proteins

Taq Polymerase Pepsin Ribozyme

 Protein

ENZYME

Protein
(apoenzyme/apoprotein)

Holoenzyme
Non protein (prosthetic
group)

Cofactor /metal Coenzyme

ion /organic molecule
How enzymes work?
Enzymes Affect Reaction Rates, Not Equilibria
Catalysts enhance reaction rates by lowering activation
energies
What is the source of the energy for the dramatic lowering
of the activation energies for specific reactions?
The first lies in the rearrangement of covalent
bonds during an enzyme-catalyzed reaction.
Chemical reactions of many types take place
between substrates and enzymes’ functional groups
(specific amino acid side chains, metal ions, and
coenzymes). Catalytic functional groups on an
enzyme may form a transient covalent bond with a
substrate and activate it for reaction, or a group
may be transiently transferred from the substrate to
the enzyme. In many cases, these reactions occur
only in the enzyme active site. Covalent interactions
between enzymes and substrates lower the
activation energy (and thereby accelerate the
reaction) by providing an alternative, lower-energy
reaction path. The specific types of rearrangements
that occur are described
The second part of the explanation lies in the
noncovalent interactions between enzyme and
substrate. Noncovalent interactions help stabilize
protein structure and protein protein interactions.
These same interactions are critical to the formation
of complexes between proteins and small molecules,
including enzyme substrates
The energy derived from enzyme-substrate
interaction is called binding energy, ΔGB. Its
significance extends beyond a simple stabilization of
the enzyme substrate interaction. Binding energy is a
major source of free energy used by enzymes to
lower the activation energies of reactions
General Acid-Base Catalysis
Metal Ion Catalysis
• Ionic interactions between an enzyme-bound metal and a substrate
can help orient the substrate for reaction or stabilize charged reaction
transition states
• Metals can also mediate oxidation-reduction reactions by reversible
changes in the metal ion’s oxidation state
Covalent Catalysis
• A transient covalent bond is formed between the enzyme and the
substrate. Consider the hydrolysis of a bond between groups A and B:

• In the presence of a covalent catalyst (an enzyme with a nucleophilic

group X:) the reaction becomes