Mechanism

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General Mechanism

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Mechanism
1. Covalent Catalysis
2. Acid-Base Catalysis
3. Metal Ion Catalysis

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Covalent Catalysis
• In covalent catalysis, a transient covalent bond is formed between the
enzyme and the substrate.
• This alters the pathway of the reaction, and it results in catalysis only
when the new pathway has a lower activation energy than the
uncatalyzed pathway.

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Acid-Base Catalysis
• Many biochemical reactions involve the formation of
unstable charged intermediates that tend to break down
rapidly to their constituent reactants species, thus impeding
the reaction.
• In the active site of an enzyme, a number of amino acid side
chains can similarly act as proton donors and acceptor to
stabilized the charge.

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Metal Ion Catalysis
• Metals, whether tightly bound to the enzyme or taken up
from solution along with the substrate, can participate in
catalysis in several ways.

• Ionic interactions between an enzyme-bound metal and a

substrate can help orient the substrate for reaction or
stabilize charged reaction transition states.

• Metal ions may also be agents of oxidation and reduction.

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Example of Enzymatic Reaction

Chymotrypsin - a digestive
enzyme belonging to a super
family of enzymes called
serine proteases.

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Chymotrypsin (free enzyme)

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Catalytic Triad - a set of three coordinated amino acids that can be
found in the active site of enzymes.

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Regulation

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Regulatory Enzymes - exhibit increased or decreased catalytic
activity in response to certain signals.

The activities of regulatory enzymes are modulated in a variety

of ways:

▪ Allosteric enzymes function through reversible, noncovalent

binding of regulatory compounds called allosteric
modulators or allosteric effectors, which are generally
small metabolites or cofactors.

▪ Other enzymes are regulated by reversible covalent

modification.

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Allosteric Regulation
• Allosteric regulation,
broadly speaking, is just
any form of regulation
where the regulatory
molecule (an activator or
inhibitor) binds to an
enzyme someplace other
than the active site. The
place where the regulator
binds is called
the allosteric site.

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Feedback inhibition of metabolic pathways

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Example: Conversion of L-
Threonine to L-Isoleucine

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Reversible Covalent
Modification
- In another important
class of regulatory
enzymes, activity is
modulated by
covalent modification
of one or more of the
amino acid residues in
the enzyme molecule.

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