Tymoczko Berg Stryer

Biochemistry: A Short Course

Second Edition
CHAPTER 6

Basic Concepts of Enzyme Action

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2013 W. H. Freeman and Company

CHAPTER 6

Basic Concepts of Enzyme Action

Outline
6.1 Enzymes Are Powerful and Highly Specic Catalysts
6.2 Many Enzymes Require Cofactors for AcDvity
6.3 Free Energy Is a Useful Thermodynamic FuncDon for
Understanding Enzymes
6.4 Enzymes Facilitate the FormaDon of the TransiDon
State
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Enzymes

have

specific

substrates:

trypsin

K or R^

thrombin

LVPR^GS

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1.

Oxidoreductase catalyze oxida4on-reduc4on reac4ons.

2.

Transferases move func4onal groups between molecules.

3.

Hydrolyases cleave bonds with the addi4on of water.

4.

Lyases remove atoms to form double bonds or add atoms to double bonds.

5.

Isomerases move func4onal groups within a molecule.

6.

Ligases join two molecules at the expense of ATP.

For the reac4on:

The free energy change is given by:

Where Go is the standard free energy, R is the gas

constant, T is 298 kelvins, and the brackets denote
concentra4on in moles.
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Enzymes accelerate the reaction rate, but will not alter

the reaction equilibrium

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ac4va4on energy

Enzymes cannot
alter this Grxn
Can enzymes make
a non-spontaneous rxn
occur?
Enzymes accelerate reactions by decreasing

G, the free energy of activation.

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Enzymes bring
substrates together to
form an enzyme-
substrate complex on a
par4cular region of the
enzyme called the
ac4ve site.
The interac4on of the
enzyme and substrates
at the ac4ve site
promotes the forma4on
of the transi4on state.

Active sites may include distant residues

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1. The ac4ve site is a three-dimensional cleV or crevice created by amino

acids from dierent parts of the primary structure.
2. The ac4ve site cons4tutes a small por4on of the enzyme volume.
3. Ac4ve sites create unique microenvironments.
4. The interac4on of the enzyme and substrate at the ac4ve site involves
mul4ple weak interac4ons.
5. Enzyme specicity depends on the molecular architecture at the ac4ve
site.

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Two models of enzymesubstrate binding:

Lock-and-key model

Induced-fit model

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proline racemase

inhibitor

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