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'''Thiosulfate sulfurtransferase''' is an [[enzyme]] that in humans is encoded by the ''TST'' [[gene]].<ref name="pmid1953758">{{cite journal | vauthors = 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 |date=Dec 1991 | pmid = 1953758 | pmc = | doi =10.1016/S0006-291X(05)81148-9 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: TST thiosulfate sulfurtransferase (rhodanese)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7263| accessdate = }}</ref> | |||
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| section_title = | | section_title = | ||
| 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.<ref name="entrez" | | 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.<ref name="entrez" /> | ||
}} | }} | ||
==References== | ==References== | ||
{{reflist | {{reflist}} | ||
==Further reading== | ==Further reading== | ||
{{refbegin | 2}} | {{refbegin | 2}} | ||
{{PBB_Further_reading | {{PBB_Further_reading | ||
| citations = | | citations = | ||
*{{cite journal | *{{cite journal |vauthors=Pecci L, Pensa B, Costa M, etal |title=Reaction of rhodanese with dithiothreitol |journal=Biochim. Biophys. Acta |volume=445 |issue= 1 |pages= 104–11 |year= 1976 |pmid= 986188 |doi= 10.1016/0005-2744(76)90163-7}} | ||
*{{cite journal | *{{cite journal |vauthors=Polo CF, Vazquez ES, Caballero F, etal |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=10.1016/0305-0491(92)90440-3 }} | ||
*{{cite journal |vauthors=Lewis JL, Rhoades CE, Gervasi PG, etal |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=10.1016/0041-008X(91)90274-I }} | |||
*{{cite journal | *{{cite journal | vauthors=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 | | *{{cite journal | vauthors=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=10.1016/0020-711X(87)90337-5 }} | ||
*{{cite journal | | *{{cite journal |vauthors=Pallini R, Martelli P, Bardelli AM, etal |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= 10.1212/wnl.37.12.1878}} | ||
*{{cite journal | *{{cite journal | vauthors=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= 10.1016/0167-4838(83)90312-6}} | ||
*{{cite journal | | *{{cite journal | vauthors=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=10.1111/j.1471-4159.1984.tb00932.x }} | ||
*{{cite journal | | *{{cite journal | vauthors=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=10.1016/0378-1119(94)90802-8 }} | ||
*{{cite journal | | *{{cite journal | vauthors=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 | | *{{cite journal |vauthors=Aita N, Ishii K, Akamatsu Y, etal |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 | *{{cite journal |vauthors=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, etal |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=10.1016/S0378-1119(97)00411-3 }} | ||
*{{cite journal | *{{cite journal |vauthors=Dunham I, Shimizu N, Roe BA, etal |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 | *{{cite journal | vauthors=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=10.1021/bi001774v }} | ||
*{{cite journal | | *{{cite journal |vauthors=Picton R, Eggo MC, Merrill GA, etal |title=Mucosal protection against sulphide: importance of the enzyme rhodanese |journal=Gut |volume=50 |issue= 2 |pages= 201–5 |year= 2002 |pmid= 11788560 |doi=10.1136/gut.50.2.201 | pmc=1773108 }} | ||
*{{cite journal | *{{cite journal |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |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 | pmc=139241 }} | ||
*{{cite journal | *{{cite journal |vauthors=Gevaert K, Goethals M, Martens L, etal |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 | *{{cite journal | vauthors=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=10.1016/S1357-2725(03)00005-0 }} | ||
*{{cite journal | | *{{cite journal |vauthors=Ota T, Suzuki Y, Nishikawa T, etal |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 }} | ||
*{{cite journal | |||
}} | }} | ||
{{refend}} | {{refend}} | ||
{{PDB Gallery|geneid=7263}} | |||
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Latest revision as of 12:23, 15 September 2017
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Species | Human | Mouse | |||||
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RefSeq (mRNA) |
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Location (UCSC) | n/a | n/a | |||||
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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
- ↑ 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.
- ↑ 2.0 2.1 "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.
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