InterPro domain: IPR045078

This entry represents a group of sulfurtransferases, including thiosulfate sulfurtransferases and 3-mercaptopyruvate sulfurtransferases.

Thiosulfate sulfurtransferase (also known as rhodanese, 2.8.1.1 ) is an enzyme which catalyses the transfer of the sulphane atom of thiosulphate to cyanide, to form sulphite and thiocyanate. In vertebrates, rhodanese is a mitochondrial enzyme that is involved in forming iron-sulphur complexes and cyanide detoxification. A cysteine residue takes part in the catalytic mechanism [ 1 , 2 ]. Some bacterial proteins may also express sulfotransferase activity. These include, SseA from Mycobacterium leprae and Escherichia coli, Azotobacter vinelandii rhdA, Saccharopolyspora erythraea cysA [ 3 ] and Synechococcus sp. (strain PCC 7942) rhdA [ 4 ].

3-Mercaptopyruvate sulfurtransferase (MPST, 2.8.1.2 catalyses the desulfuration of 3-mercaptopyruvate to generate an enzyme-bound hydropersulfide [ 5 ].

1. Thiosulfate: cyanide sulfurtransferase (rhodanese). Meth. Enzymol. 77, 285-91
2. Molecular cloning, sequencing and characterization of cDNA to rat liver rhodanese, a thiosulphate sulphurtransferase. Biochem. J. 275 ( Pt 1), 227-31
3. Disruption of a rhodaneselike gene results in cysteine auxotrophy in Saccharopolyspora erythraea. J. Bacteriol. 172, 350-60
4. Isolation and characterization of a sulfur-regulated gene encoding a periplasmically localized protein with sequence similarity to rhodanese. J. Bacteriol. 173, 2751-60
5. 3-Mercaptopyruvate sulfurtransferase: an enzyme at the crossroads of sulfane sulfur trafficking. Biol Chem 402, 223-237