Properties of Enzymes

Table 3 Effects of reversible inhibitors on kinetic constants

Type of inhibitor Effect

Competitive (I binds to E only) Raises Km

Vmax remains unchanged
Uncompetitive (I binds to ES only) Lowers Vmax and Km
Ratio of Vmax/Km remains unchanged
Noncompetitive (I binds to E or ES) Lowers Vmax
Km remains unchanged

A. Competitive Inhibition
Competitive inhibitors are the most commonly encountered inhibitors in biochem-
istry. In competitive inhibition, the inhibitor can bind only to free enzyme molecules
that have not bound any substrate. Competitive inhibition is illustrated in Figure 8 and
by the kinetic scheme in Figure 9a. In this scheme only ES can lead to the formation
of product. The formation of an EI complex removes enzyme from the normal path-
way.
Once a competitive inhibitor is bound to an enzyme molecule, a substrate mole-

AP Photo/Paul Sakuma
cule cannot bind to that enzyme molecule. Conversely, the binding of substrate to an
enzyme molecule prevents the binding of an inhibitor. In other words, S and I compete
for binding to the enzyme molecule. Most commonly, S and I bind at the same site on
the enzyme, the active site. This type of inhibition is termed classical competitive inhi-
bition (Figure 8). This is not the only kind of competitive inhibition (see Figure 8). In
some cases, such as allosteric enzymes (Section 10), the inhibitor binds at a different
site and this alters the substrate binding site preventing substrate binding. This type Competitive inhibition. The active
of inhibition is called nonclassical competitive inhibition. When both I and S are ingredient in the weed killer Roundup © is
glyphosate, a competitive inhibitor of the
plant enzyme 5-enolpyruvylshikimate-3-
phosphate synthase.

(a) Classical competitive inhibition (b) Nonclassical competitive inhibition

S S

I I

The substrate (S) and the inhibitor The binding of substrate (S) at the active
(I) compete for the same site on site prevents the binding of inhibitor (I)
the enzyme. at a separate site and vice versa.

(c) Uncompetitive inhibition (d) Noncompetitive inhibition

S
S

S
S I I
I

The inhibitor (I) binds only to the
enzyme substrate (ES) complex
preventing the conversion of
substrate (S) to product.
The inhibitor (I) can bind to either E or
ES. The enzyme becomes inactive when
I binds. Substrate (S) can still bind to
the EI complex but conversion to
product is inhibited.
Figure 8
Diagrams of reversible enzyme inhibition. In
this scheme, catalytically competent enzymes
are green and inactive enzymes are red.

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