TST (gene)

Thiosulfate sulfurtransferase (rhodanese), also known as TST, is a human gene.cite web | title = Entrez Gene: TST thiosulfate sulfurtransferase (rhodanese)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7263| accessdate = ]

PBB_Summary
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summary_text = 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.cite web | title = Entrez Gene: TST thiosulfate sulfurtransferase (rhodanese)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7263| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Pecci L, Pensa B, Costa M, "et al." |title=Reaction of rhodanese with dithiothreitol. |journal=Biochim. Biophys. Acta |volume=445 |issue= 1 |pages= 104–11 |year= 1976 |pmid= 986188 |doi=
*cite journal | author=Polo CF, Vazquez ES, Caballero F, "et al." |title=Heme biosynthesis pathway regulation in a model of hepatocarcinogenesis pre-initiation. |journal=Comp. Biochem. Physiol., B |volume=103 |issue= 1 |pages= 251–6 |year= 1993 |pmid= 1451437 |doi=
*cite journal | author=Pallini R, Guazzi GC, Cannella C, Cacace MG |title=Cloning and sequence analysis of the human liver rhodanese: comparison with the bovine and chicken enzymes. |journal=Biochem. Biophys. Res. Commun. |volume=180 |issue= 2 |pages= 887–93 |year= 1991 |pmid= 1953758 |doi=
*cite journal | author=Lewis JL, Rhoades CE, Gervasi PG, "et al." |title=The cyanide-metabolizing enzyme rhodanese in human nasal respiratory mucosa. |journal=Toxicol. Appl. Pharmacol. |volume=108 |issue= 1 |pages= 114–20 |year= 1991 |pmid= 2006499 |doi=
*cite journal | author=Malliopoulou VA, Rakitzis ET, Malliopoulou TB |title=Inactivation of rhodanese from human gastric mucosa and stomach adenocarcinoma by 2,4, 6-trinitrobenzenesulphonate and by 4,4'-diisothiocyanatostilbene-2,2'-disulphonate. |journal=Anticancer Res. |volume=9 |issue= 4 |pages= 1133–6 |year= 1989 |pmid= 2817794 |doi=
*cite journal | author=Vazquez E, Buzaleh AM, Wider E, Batlle AM |title=Red blood cell rhodanese: its possible role in modulating delta-aminolaevulinate synthetase activity in mammals. |journal=Int. J. Biochem. |volume=19 |issue= 2 |pages= 217–9 |year= 1987 |pmid= 3471602 |doi=
*cite journal | author=Pallini R, Martelli P, Bardelli AM, "et al." |title=Normal rhodanese activity in leukocytes from Leber patients: enzyme characterization and activity levels. |journal=Neurology |volume=37 |issue= 12 |pages= 1878–80 |year= 1987 |pmid= 3479705 |doi=
*cite journal | author=Pagani S, Galante YM |title=Interaction of rhodanese with mitochondrial NADH dehydrogenase. |journal=Biochim. Biophys. Acta |volume=742 |issue= 2 |pages= 278–84 |year= 1983 |pmid= 6402020 |doi=
*cite journal | author=Mimori Y, Nakamura S, Kameyama M |title=Regional and subcellular distribution of cyanide metabolizing enzymes in the central nervous system. |journal=J. Neurochem. |volume=43 |issue= 2 |pages= 540–5 |year= 1984 |pmid= 6588145 |doi=
*cite journal | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171–4 |year= 1994 |pmid= 8125298 |doi=
*cite journal | author=Merrill GA, Butler M, Horowitz PM |title=Limited tryptic digestion near the amino terminus of bovine liver rhodanese produces active electrophoretic variants with altered refolding. |journal=J. Biol. Chem. |volume=268 |issue= 21 |pages= 15611–20 |year= 1993 |pmid= 8340386 |doi=
*cite journal | author=Aita N, Ishii K, Akamatsu Y, "et al." |title=Cloning and expression of human liver rhodanese cDNA. |journal=Biochem. Biophys. Res. Commun. |volume=231 |issue= 1 |pages= 56–60 |year= 1997 |pmid= 9070219 |doi= 10.1006/bbrc.1996.6046
*cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, "et al." |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149–56 |year= 1997 |pmid= 9373149 |doi=
*cite journal | author=Dunham I, Shimizu N, Roe BA, "et al." |title=The DNA sequence of human chromosome 22. |journal=Nature |volume=402 |issue= 6761 |pages= 489–95 |year= 1999 |pmid= 10591208 |doi= 10.1038/990031
*cite journal | author=Wieprecht T, Apostolov O, Beyermann M, Seelig J |title=Interaction of a mitochondrial presequence with lipid membranes: role of helix formation for membrane binding and perturbation. |journal=Biochemistry |volume=39 |issue= 50 |pages= 15297–305 |year= 2001 |pmid= 11112515 |doi=
*cite journal | author=Picton R, Eggo MC, Merrill GA, "et al." |title=Mucosal protection against sulphide: importance of the enzyme rhodanese. |journal=Gut |volume=50 |issue= 2 |pages= 201–5 |year= 2002 |pmid= 11788560 |doi=
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899
*cite journal | author=Gevaert K, Goethals M, Martens L, "et al." |title=Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. |journal=Nat. Biotechnol. |volume=21 |issue= 5 |pages= 566–9 |year= 2004 |pmid= 12665801 |doi= 10.1038/nbt810
*cite journal | author=Kwiecień I, Sokołowska M, Luchter-Wasylewska E, Włodek L |title=Inhibition of the catalytic activity of rhodanese by S-nitrosylation using nitric oxide donors. |journal=Int. J. Biochem. Cell Biol. |volume=35 |issue= 12 |pages= 1645–57 |year= 2004 |pmid= 12962704 |doi=
*cite journal | author=Ota T, Suzuki Y, Nishikawa T, "et al." |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285

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