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2.1.2.1 Reversible inhibition modeling

The model used to face the presence of an inhibitor is again
represented by the Michaelis–Menten equation (Eq. 15.4):
(15.9)v=vmaxappsKmapp+s.
In this case, the maximum reaction velocity (vmaxapp) and the
Michaelis–Menten constant (Kmapp) depend also on the
concentration of the inhibitor (i) and the dissociation constants of the
reactions in which the inhibitor is involved (Ki). The most common
types of inhibition action are [8]:
•
Competitive: The inhibitor adsorbs at the substrate binding site.
In this case, two types of complexes are formed: enzyme–
inhibitor (EI) and enzyme–substrate (ES); complex EI has no
enzyme activity.
•
Uncompetitive: The inhibitor binds only to the ES complex; it
does not interfere with the binding of substrate to the active site
but prevents the dissociation of the ES complex: it results in the
dependence of the inhibition on only the inhibitor concentration
and its Ki value.
•
Noncompetitive: The enzyme–inhibitor–substrate (EIS)
complex is unable to dissociate to give a product of reaction. In
this case, inhibitor binds to E or to the ES complex. The binding
of the inhibitor to the enzyme reduces its activity but does not
affect the binding of substrate. As a result, the extent of the
inhibition depends on only the concentration of the inhibitor (i).
•
Mixed: This action is generated by the combination of different
types of inhibition.
Table 15.3 summarizes the cases described above and correlates, for
each case, the respective expression of vmaxapp and Kmapp.
Table  15.3. Typology of inhibition attack and related expression of the Michaelis–Menten constants.
 Model
Type Equations Dissociat Constant expressions
ion
constant
sa

Competitiv E+S↔ESE+I↔EIES→k2E+P KsKi vmaxapp=vmax=k2e0Kmapp=

e Ks(1+iKi)

Uncompetit E+S↔ESES+I↔EISES→k2E+P KsKi vmaxapp=k2e0/

ive (1+iKi)Kmapp=Ks/(1+iKi)

Noncompet E+S↔ESEI+S↔EISE+I↔EIES+I↔EI KsKsKiKi vmaxapp=k2e0/

itive SES→k2E+P (1+iKi)Kmapp=Ks
a
Remember that for the noncompetitive type, the inhibitor and the substrate do not influence each
other as to affinity for the complex with the enzyme. For this reason the dissociation constants are
just Ks and Ki.

Usually, to recognize the presence of an inhibitor, a comparison of the

Lineweaver–Burk plots with and without the inhibitor species is done
(Figs. 15.8 and 15.9).

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 Figure  15.8. Qualitative overview by means of Lineweaver–Burk plot of

different cases of inhibition [9]. (A) Competitive inhibitor, (B) noncompetitive

inhibitor, (C) uncompetitive inhibitor, (D) mixed inhibitor.

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