Date published: 2025-12-24

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CYP2D22 Inhibitors

Chemical inhibitors of CYP2D22 include a range of compounds that interact with the enzyme to reduce its metabolic activity. Quinidine, a known CYP2D22 inhibitor, binds competitively at the active site of the enzyme, which hampers the metabolic function that CYP2D22 typically carries out. Similarly, ajmalicine engages with CYP2D22 in a competitive manner, blocking access for substrates to the active site, thereby diminishing the enzyme's activity. Fluoxetine, another chemical in this list, directly inhibits CYP2D22 by occupying the active site, which impairs the catalytic efficiency of the enzyme. Paroxetine inhibits CYP2D22 by a similar mechanism, binding to the active site and consequently obstructing the enzyme's function in metabolizing substrates. Methadone also contributes to the inhibition of CYP2D22, with its binding to the active site leading to a reduction in the enzyme's ability to process substrates.

Furthermore, ritonavir binds to CYP2D22 and is known to interfere with the substrate metabolism that is characteristic of the enzyme. Haloperidol's interaction with CYP2D22 results in a decrease in the enzyme's capacity to metabolize its substrates by direct inhibition. Diphenhydramine and chlorpheniramine each competitively inhibit CYP2D22 by occupying the active site, which lowers the enzymatic activity and prevents the metabolism of the enzyme's natural substrates. Codeine, acting as a competitive inhibitor, contests with endogenous substrates for the active site on CYP2D22, which results in a decrease in enzyme activity. Dextromethorphan binds to the enzyme's active site, inhibiting the normal metabolic processing of substrates by CYP2D22. Lastly, bufuralol inhibits CYP2D22 by binding to the active site, which in turn diminishes the metabolic capacity of CYP2D22 to process its substrates, effectively reducing the overall activity of the enzyme. Each of these chemicals directly influences CYP2D22's ability to function by engaging with the enzyme in a manner that leads to the inhibition of its metabolic processes.

Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

Quinidine

56-54-2sc-212614
10 g
$102.00
3
(1)

Quinidine is known to inhibit CYP2D22 by competing with the enzyme's natural substrates for binding at the active site, thus impeding its metabolic function.

Fluoxetine

54910-89-3sc-279166
500 mg
$312.00
9
(1)

Fluoxetine directly inhibits CYP2D22 by binding to the enzyme's active site, which leads to a decrease in its catalytic efficiency.

Paroxetine

61869-08-7sc-507527
1 g
$180.00
(0)

Paroxetine inhibits CYP2D22 by directly interacting with the enzyme's active site, thereby hindering its normal function in metabolizing substrates.

Ritonavir

155213-67-5sc-208310
10 mg
$122.00
7
(1)

Ritonavir is a known inhibitor of CYP2D22, as it can bind to the active site of the enzyme and interfere with substrate metabolism.

Haloperidol

52-86-8sc-507512
5 g
$190.00
(0)

Haloperidol inhibits CYP2D22 by directly interacting with the enzyme, leading to a reduction in its ability to metabolize various substrates.

Diphenhydramine hydrochloride

147-24-0sc-204729
sc-204729A
sc-204729B
10 g
25 g
100 g
$51.00
$82.00
$122.00
4
(1)

Diphenhydramine competitively inhibits CYP2D22 by occupying the active site, which results in decreased enzymatic activity.

Dextromethorphan

125-71-3sc-278927
sc-278927A
sc-278927B
10 g
100 g
500 g
$174.00
$1133.00
$5106.00
3
(1)

Dextromethorphan can inhibit CYP2D22 by binding to the enzyme's active site, hindering the normal metabolic processing of substrates.