TST (gene)

Thiosulfate sulfurtransferase (rhodanese)
PDB rendering based on 1dp2.
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 1dp2​
Identifiers
Symbols	TST ; RDS
External IDs	OMIM: 180370 MGI: 98852 HomoloGene: 37759 GeneCards: TST Gene
EC number	2.8.1.1
Gene ontology Molecular function • thiosulfate sulfurtransferase activity • 5S rRNA binding Cellular component • extracellular space • mitochondrion • mitochondrial inner membrane • mitochondrial matrix • extracellular exosome Biological process • sulfur amino acid metabolic process • sulfur amino acid catabolic process • cyanate catabolic process • epithelial cell differentiation • cellular nitrogen compound metabolic process • rRNA import into mitochondrion • small molecule metabolic process • rRNA transport • sulfide oxidation, using sulfide:quinone oxidoreductase Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	7263	22117
Ensembl	ENSG00000128311	ENSMUSG00000044986
UniProt	Q16762	P52196
RefSeq (mRNA)	NM_001270483	NM_009437
RefSeq (protein)	NP_001257412	NP_033463
Location (UCSC)	Chr 22: 37.01 – 37.02 Mb	Chr 15: 78.4 – 78.41 Mb
PubMed search

Thiosulfate sulfurtransferase is an enzyme that in humans is encoded by the TST gene.^[1][2]

The product of this gene is a mitochondrial matrix enzyme that is encoded by the nucleus. It may play roles in cyanide detoxification, the formation of iron-sulfur proteins, and the modification of sulfur-containing enzymes. The gene product contains two highly conservative domains (rhodanese homology domains), suggesting these domains have a common evolutionary origin.^[2]

References

1. Pallini R, Guazzi GC, Cannella C, Cacace MG (Dec 1991). "Cloning and sequence analysis of the human liver rhodanese: comparison with the bovine and chicken enzymes". Biochem Biophys Res Commun 180 (2): 887–93. doi:10.1016/S0006-291X(05)81148-9. PMID 1953758.
2. "Entrez Gene: TST thiosulfate sulfurtransferase (rhodanese)".

Further reading

• Pecci L, Pensa B, Costa M, et al. (1976). "Reaction of rhodanese with dithiothreitol". Biochim. Biophys. Acta 445 (1): 104–11. doi:10.1016/0005-2744(76)90163-7. PMID 986188.
• Polo CF, Vazquez ES, Caballero F, et al. (1993). "Heme biosynthesis pathway regulation in a model of hepatocarcinogenesis pre-initiation". Comp. Biochem. Physiol., B 103 (1): 251–6. doi:10.1016/0305-0491(92)90440-3. PMID 1451437.
• Lewis JL, Rhoades CE, Gervasi PG, et al. (1991). "The cyanide-metabolizing enzyme rhodanese in human nasal respiratory mucosa". Toxicol. Appl. Pharmacol. 108 (1): 114–20. doi:10.1016/0041-008X(91)90274-I. PMID 2006499.
• Malliopoulou VA, Rakitzis ET, Malliopoulou TB (1989). "Inactivation of rhodanese from human gastric mucosa and stomach adenocarcinoma by 2,4, 6-trinitrobenzenesulphonate and by 4,4'-diisothiocyanatostilbene-2,2'-disulphonate". Anticancer Res. 9 (4): 1133–6. PMID 2817794.
• Vazquez E, Buzaleh AM, Wider E, Batlle AM (1987). "Red blood cell rhodanese: its possible role in modulating delta-aminolaevulinate synthetase activity in mammals". Int. J. Biochem. 19 (2): 217–9. doi:10.1016/0020-711X(87)90337-5. PMID 3471602.
• Pallini R, Martelli P, Bardelli AM, et al. (1987). "Normal rhodanese activity in leukocytes from Leber patients: enzyme characterization and activity levels". Neurology 37 (12): 1878–80. doi:10.1212/wnl.37.12.1878. PMID 3479705.
• Pagani S, Galante YM (1983). "Interaction of rhodanese with mitochondrial NADH dehydrogenase". Biochim. Biophys. Acta 742 (2): 278–84. doi:10.1016/0167-4838(83)90312-6. PMID 6402020.
• Mimori Y, Nakamura S, Kameyama M (1984). "Regional and subcellular distribution of cyanide metabolizing enzymes in the central nervous system". J. Neurochem. 43 (2): 540–5. doi:10.1111/j.1471-4159.1984.tb00932.x. PMID 6588145.
• Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
• Merrill GA, Butler M, Horowitz PM (1993). "Limited tryptic digestion near the amino terminus of bovine liver rhodanese produces active electrophoretic variants with altered refolding". J. Biol. Chem. 268 (21): 15611–20. PMID 8340386.
• Aita N, Ishii K, Akamatsu Y, et al. (1997). "Cloning and expression of human liver rhodanese cDNA". Biochem. Biophys. Res. Commun. 231 (1): 56–60. doi:10.1006/bbrc.1996.6046. PMID 9070219.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
• Dunham I, Shimizu N, Roe BA, et al. (1999). "The DNA sequence of human chromosome 22". Nature 402 (6761): 489–95. doi:10.1038/990031. PMID 10591208.
• Wieprecht T, Apostolov O, Beyermann M, Seelig J (2001). "Interaction of a mitochondrial presequence with lipid membranes: role of helix formation for membrane binding and perturbation". Biochemistry 39 (50): 15297–305. doi:10.1021/bi001774v. PMID 11112515.
• Picton R, Eggo MC, Merrill GA, et al. (2002). "Mucosal protection against sulphide: importance of the enzyme rhodanese". Gut 50 (2): 201–5. doi:10.1136/gut.50.2.201. PMC 1773108. PMID 11788560.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Gevaert K, Goethals M, Martens L, et al. (2004). "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides". Nat. Biotechnol. 21 (5): 566–9. doi:10.1038/nbt810. PMID 12665801.
• Kwiecień I, Sokołowska M, Luchter-Wasylewska E, Włodek L (2004). "Inhibition of the catalytic activity of rhodanese by S-nitrosylation using nitric oxide donors". Int. J. Biochem. Cell Biol. 35 (12): 1645–57. doi:10.1016/S1357-2725(03)00005-0. PMID 12962704.
• Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.