TST (gene): Difference between revisions

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{{Infobox_gene}}
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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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{{GNF_Protein_box
| image = PBB_Protein_TST_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1dp2.
| PDB = {{PDB2|1dp2}}
| Name = Thiosulfate sulfurtransferase (rhodanese)
| HGNCid = 12388
| Symbol = TST
| AltSymbols =; RDS; MGC19578
| OMIM = 180370
| ECnumber = 
| Homologene = 37759
| MGIid = 98852
| GeneAtlas_image1 = PBB_GE_TST_209605_at_tn.png
| Function = {{GNF_GO|id=GO:0004792 |text = thiosulfate sulfurtransferase activity}} {{GNF_GO|id=GO:0016740 |text = transferase activity}}
| Component = {{GNF_GO|id=GO:0005739 |text = mitochondrion}} {{GNF_GO|id=GO:0005743 |text = mitochondrial inner membrane}} {{GNF_GO|id=GO:0005759 |text = mitochondrial matrix}}
  | Process = {{GNF_GO|id=GO:0008272 |text = sulfate transport}} {{GNF_GO|id=GO:0009440 |text = cyanate catabolic process}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 7263
    | Hs_Ensembl = ENSG00000128311
    | Hs_RefseqProtein = NP_003303
    | Hs_RefseqmRNA = NM_003312
    | Hs_GenLoc_db =   
    | Hs_GenLoc_chr = 22
    | Hs_GenLoc_start = 35736853
    | Hs_GenLoc_end = 35745437
    | Hs_Uniprot = Q16762
    | Mm_EntrezGene = 22117
    | Mm_Ensembl = ENSMUSG00000044986
    | Mm_RefseqmRNA = NM_009437
    | Mm_RefseqProtein = NP_033463
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 15
    | Mm_GenLoc_start = 78226520
    | Mm_GenLoc_end = 78233120
    | Mm_Uniprot = Q545S0
  }}
}}
'''Thiosulfate sulfurtransferase (rhodanese)''', also known as '''TST''', is a human [[gene]].<ref name="entrez">{{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 = }}</ref>


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{{PBB_Summary
{{PBB_Summary
| 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">{{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 = }}</ref>
| 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|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| 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   |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 | 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   |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  | 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   |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 | 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  | 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  | 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  | 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  | 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   |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 | 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  | 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  | 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  | 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  | 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  | 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  | 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  | 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  | 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   |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 | 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   |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 | 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   |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 | 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  | 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  | 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   |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 | 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   |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 | 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   |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 | 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  | 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  | 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   |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 | 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 }}
}}
}}
{{refend}}
{{refend}}
{{PDB Gallery|geneid=7263}}
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Latest revision as of 12:23, 15 September 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

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. ↑ 2.0 2.1 "Entrez Gene: TST thiosulfate sulfurtransferase (rhodanese)".

Further reading



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