Date published: 2026-4-24

1-800-457-3801

SCBT Portrait Logo
Seach Input

Rhodanese Inhibitors

Rhodanese inhibitors belong to a class of chemical compounds that interact with and modulate the activity of the enzyme rhodanese. Rhodanese is a sulfurtransferase enzyme found in various organisms, including bacteria, plants, and animals. Its primary function is to catalyze the transfer of a sulfur atom from thiosulfate to cyanide, resulting in the formation of thiocyanate, a less toxic compound. This detoxification process is crucial for organisms exposed to cyanide-containing compounds. Rhodanese inhibitors, as the name suggests, are molecules that inhibit the normal functioning of rhodanese.

They typically exert their effects by binding to the active site of the enzyme, disrupting its catalytic activity. These inhibitors can have diverse chemical structures and mechanisms of action, but their common feature is their ability to interfere with the sulfur transfer reaction carried out by rhodanese. Studying rhodanese inhibitors and their interactions with the enzyme provides valuable insights into the enzyme's mechanism, as well as applications in various fields where modulation of sulfur metabolism is relevant.

SEE ALSO...

Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

Dimethyl Sulfoxide (DMSO)

67-68-5sc-202581
sc-202581A
sc-202581B
100 ml
500 ml
4 L
$31.00
$117.00
$918.00
136
(6)

Alters the conformation of rhodanese through binding to the protein, leading to changes in its active site and inhibiting its catalytic activity.

Mercaptosuccinic acid

70-49-5sc-250305
sc-250305A
100 g
500 g
$50.00
$188.00
2
(0)

Forms a reversible complex with rhodanese, blocking the active site and preventing the enzyme from transferring sulfur ions, thus inhibiting its detoxification role.

Allyl isothiocyanate

57-06-7sc-252361
sc-252361A
sc-252361B
5 g
100 g
500 g
$44.00
$67.00
$119.00
3
(1)

Reacts with the active site cysteine residues of rhodanese, forming covalent bonds and irreversibly inhibiting its catalytic activity in sulfur transfer reactions.