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Gene Review

TST  -  thiosulfate sulfurtransferase (rhodanese)

Homo sapiens

Synonyms: RDS, Rhodanese, Thiosulfate sulfurtransferase
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Disease relevance of TST


Psychiatry related information on TST

  • The high rhodanese activity in rat nasal epithelium may provide a mechanism for detoxicating inhaled hydrogen cyanide and may also play a role in olfaction by limiting the concentrations of cyanide in the nasal epithelium [3].
  • In contrast to this, rhodanese inactivation by 4, 4'-diisothiocyanatostilbene-2, 2'-disulphonate was found to be biphasic, when log residual enzyme activity was plotted vs reaction time [4].
  • In contrast, alcoholics showed less TST and REM sleep during acute withdrawal than during subacute withdrawal [5].
  • Arousal indices (AI), defined as the number of arousals per hour of sleep, were calculated for total sleep time (AI/TST) and for all the sleep stages [6].
  • A Principal Component Analysis (PCA) was conducted on seven variables from the sample, namely PLM index, patient's age, sleep stage changes per hour, sleep depth index (SWS+PS/TST), diurnal sleep time, number of awakenings exceeding 2 min and presence of a RLS [7].

High impact information on TST

  • The 2.3 A structure of the human Cdc25A catalytic domain reveals a small alpha/beta domain with a fold unlike previously described phosphatase structures but identical to rhodanese, a sulfur-transfer protein [8].
  • In addition to severe deficiency of complex II, manifested by reduction of succinate dehydrogenase and succinate:coenzyme Q oxidoreductase activities to 12 and 22% of normal, respectively, complex III activity was reduced to 37% and rhodanese to 48% of normal [9].
  • Thiosulphate-sulphur transferase (rhodanese) deficiency in Leber's hereditary optic atrophy [10].
  • This unusual post-translational modification is also seen in sulfurtransferases such as rhodanese [11].
  • These results indicate that 3-MST and GAPDH have more suitable potentials as a physiological selenium-delivery protein than rhodanese [12].

Chemical compound and disease context of TST


Biological context of TST

  • Nucleotide sequence revealed an open reading frame coding for a polypeptide of 295 amino acids, which presented a 57% and 58% identity with the bovine and avian rhodanese, respectively [18].
  • The cDNA for the human rhodanese (thiosulfate: cyanide sulfurtransferase, EC, a nuclearly encoded protein of the mitochondrial matrix, was isolated from a human fetal liver cDNA library [18].
  • A comparison with two available amino acid sequences (cow and chicken) showed that sequence similarity is not restricted to the alpha-helices and beta-structures motifs which are remarkably superimposable in the two halves of bovine rhodanese, but extends to adjacent regions [18].
  • In such tissues as the liver or gonads, high GSH levels and high activities of MPST (in the liver) or MPST and rhodanese (in the gonads) seemed to accompany protein biosynthesis during hibernation [19].
  • This is further supported by our findings that mutations within amino acid motifs conserved among these beta cytoplasmic domains, specifically the NXXY, NPXY and TST-like motifs, reduced the ability of these chimeric receptors to regulate beta1 integrin conformation [20].

Anatomical context of TST


Associations of TST with chemical compounds

  • Sulfide (0.1 mM) also increased TST activity, but higher sulfide concentrations (0.3-3 mM) were toxic [1].
  • Using specific antisera to discriminate TST from MST, we found that only TST could detoxify H2S [1].
  • Evidence for the physiological role of a rhodanese-like protein for the biosynthesis of the molybdenum cofactor in humans [2].
  • TMT and RHOD activities were determined using their conventional substrates, 2-mercaptoethanol and sodium thiosulphate, respectively [22].
  • Brain rhodanese and liver beta-mercaptopyruvate sulfurtransferase showed a slight decrease in activity after death [24].

Physical interactions of TST

  • Both procedures used here gave results that were consistent with there being 1 rhodanese binding site/cpn60 tetradecamer [25].
  • The USP8 recognition domain of NRDP1 has a novel protein fold that interacts with a conserved peptide loop of the rhodanese domain [26].

Regulatory relationships of TST

  • Both domains are able to bind to the ATPase domain of HSC70 and inhibit rhodanese aggregation [27].

Other interactions of TST


Analytical, diagnostic and therapeutic context of TST

  • Cloning and sequence analysis of the human liver rhodanese: comparison with the bovine and chicken enzymes [18].
  • Rhodanese-mediated sulfide transfer was directly demonstrated when the reactivation of NADH dehydrogenase was performed in the presence of radioactive thiosulfate (labeled in the outer sulfur) and the 35S-loaded flavoprotein was re-isolated by gel filtration chromatography [30].
  • In order to better determine what these factors and mechanism of action are, and to determine if the TST marker protein is in fact the critical toxin, a reliable animal model is badly needed [31].
  • Two enzyme immunoassays, the Vitek Immuno-Diagnostic Assay System (VIDAS; Vitek Systems, Hazelwood, Mo.) and the Toxostat Test Kit (TST; Whittaker Bioproducts, Walkersville, Md.), were compared for their ability to detect T. gondii immunoglobulin G antibodies in fresh human sera [32].
  • Health care workers with infectious TB patient contact should be instructed in the epidemiology of M. tuberculosis transmission, the role of respirators in protecting the health care worker from airborne inoculation, and the importance of periodic health care worker TST [33].


  1. Sulfide-detoxifying enzymes in the human colon are decreased in cancer and upregulated in differentiation. Ramasamy, S., Singh, S., Taniere, P., Langman, M.J., Eggo, M.C. Am. J. Physiol. Gastrointest. Liver Physiol. (2006) [Pubmed]
  2. Evidence for the physiological role of a rhodanese-like protein for the biosynthesis of the molybdenum cofactor in humans. Matthies, A., Rajagopalan, K.V., Mendel, R.R., Leimkühler, S. Proc. Natl. Acad. Sci. U.S.A. (2004) [Pubmed]
  3. The cyanide-metabolizing enzyme rhodanese in human nasal respiratory mucosa. Lewis, J.L., Rhoades, C.E., Gervasi, P.G., Griffith, W.C., Dahl, A.R. Toxicol. Appl. Pharmacol. (1991) [Pubmed]
  4. Inactivation of rhodanese from human gastric mucosa and stomach adenocarcinoma by 2,4, 6-trinitrobenzenesulphonate and by 4,4'-diisothiocyanatostilbene-2,2'-disulphonate. Malliopoulou, V.A., Rakitzis, E.T., Malliopoulou, T.B. Anticancer Res. (1989) [Pubmed]
  5. Polygraphic sleep measures differentiate alcoholics and stimulant abusers during short-term abstinence. Thompson, P.M., Gillin, J.C., Golshan, S., Irwin, M. Biol. Psychiatry (1995) [Pubmed]
  6. Effect of age on EEG arousals in normal sleep. Boselli, M., Parrino, L., Smerieri, A., Terzano, M.G. Sleep. (1998) [Pubmed]
  7. Sleep/wake abnormalities in patients with periodic leg movements during sleep: factor analysis on data from 24-h ambulatory polygraphy. Bastuji, H., García-Larrea, L. Journal of sleep research. (1999) [Pubmed]
  8. Crystal structure of the catalytic domain of the human cell cycle control phosphatase, Cdc25A. Fauman, E.B., Cogswell, J.P., Lovejoy, B., Rocque, W.J., Holmes, W., Montana, V.G., Piwnica-Worms, H., Rink, M.J., Saper, M.A. Cell (1998) [Pubmed]
  9. Mitochondrial myopathy with succinate dehydrogenase and aconitase deficiency. Abnormalities of several iron-sulfur proteins. Hall, R.E., Henriksson, K.G., Lewis, S.F., Haller, R.G., Kennaway, N.G. J. Clin. Invest. (1993) [Pubmed]
  10. Thiosulphate-sulphur transferase (rhodanese) deficiency in Leber's hereditary optic atrophy. Cagianut, B., Rhyner, K., Furrier, W., Schnebli, H.P. Lancet (1981) [Pubmed]
  11. Structural basis for the oxidation of thiosulfate by a sulfur cycle enzyme. Bamford, V.A., Bruno, S., Rasmussen, T., Appia-Ayme, C., Cheesman, M.R., Berks, B.C., Hemmings, A.M. EMBO J. (2002) [Pubmed]
  12. Characterization of potential selenium-binding proteins in the selenophosphate synthetase system. Ogasawara, Y., Lacourciere, G.M., Ishii, K., Stadtman, T.C. Proc. Natl. Acad. Sci. U.S.A. (2005) [Pubmed]
  13. The growth of two murine hemangioendotheliomas intracranially, subcutaneously, and in culture, and their comparison with human cerebellar hemangioblastomas: morphological and immunohistochemical studies. Vinores, S.A., Herman, M.M., Perentes, E., Nakagawa, Y., Thomas, C.B., Innes, D.J., Rubinstein, L.J. Acta Neuropathol. (1992) [Pubmed]
  14. Partitioning of rhodanese onto GroEL. Chaperonin binds a reversibly oxidized form derived from the native protein. Smith, K.E., Voziyan, P.A., Fisher, M.T. J. Biol. Chem. (1998) [Pubmed]
  15. Surface changes and role of buried water molecules during the sulfane sulfur transfer in rhodanese from Azotobacter vinelandii: a fluorescence quenching and nuclear magnetic relaxation dispersion spectroscopic study. Fasano, M., Orsale, M., Melino, S., Nicolai, E., Forlani, F., Rosato, N., Cicero, D., Pagani, S., Paci, M. Biochemistry (2003) [Pubmed]
  16. A persulfurated cysteine promotes active site reactivity in Azotobacter vinelandii Rhodanese. Bordo, D., Forlani, F., Spallarossa, A., Colnaghi, R., Carpen, A., Bolognesi, M., Pagani, S. Biol. Chem. (2001) [Pubmed]
  17. Production of rhodanese by bacteria present in bio-oxidation plants used to recover gold from arsenopyrite concentrates. Gardner, M.N., Rawlings, D.E. J. Appl. Microbiol. (2000) [Pubmed]
  18. Cloning and sequence analysis of the human liver rhodanese: comparison with the bovine and chicken enzymes. Pallini, R., Guazzi, G.C., Cannella, C., Cacace, M.G. Biochem. Biophys. Res. Commun. (1991) [Pubmed]
  19. Sulfurtransferases and the content of cysteine, glutathione and sulfane sulfur in tissues of the frog Rana temporaria. Wróbel, M., Sura, P., Srebro, Z. Comp. Biochem. Physiol. B, Biochem. Mol. Biol. (2000) [Pubmed]
  20. Amino acid motifs required for isolated beta cytoplasmic domains to regulate 'in trans' beta1 integrin conformation and function in cell attachment. Mastrangelo, A.M., Homan, S.M., Humphries, M.J., LaFlamme, S.E. J. Cell. Sci. (1999) [Pubmed]
  21. Mercaptopyruvate sulfurtransferase as a defense against cyanide toxication: molecular properties and mode of detoxification. Nagahara, N., Ito, T., Minami, M. Histol. Histopathol. (1999) [Pubmed]
  22. Mucosal protection against sulphide: importance of the enzyme rhodanese. Picton, R., Eggo, M.C., Merrill, G.A., Langman, M.J., Singh, S. Gut (2002) [Pubmed]
  23. Normal rhodanese activity in leukocytes from Leber patients: enzyme characterization and activity levels. Pallini, R., Martelli, P., Bardelli, A.M., Guazzi, G.C., Federico, A. Neurology (1987) [Pubmed]
  24. Regional and subcellular distribution of cyanide metabolizing enzymes in the central nervous system. Mimori, Y., Nakamura, S., Kameyama, M. J. Neurochem. (1984) [Pubmed]
  25. Intermediates in the chaperonin-assisted refolding of rhodanese are trapped at low temperature and show a small stoichiometry. Mendoza, J.A., Lorimer, G.H., Horowitz, P.M. J. Biol. Chem. (1991) [Pubmed]
  26. Amino-terminal Dimerization, NRDP1-Rhodanese Interaction, and Inhibited Catalytic Domain Conformation of the Ubiquitin-specific Protease 8 (USP8). Avvakumov, G.V., Walker, J.R., Xue, S., Finerty, P.J., Mackenzie, F., Newman, E.M., Dhe-Paganon, S. J. Biol. Chem. (2006) [Pubmed]
  27. Domain structure of the HSC70 cochaperone, HIP. Velten, M., Gomez-Vrielynck, N., Chaffotte, A., Ladjimi, M.M. J. Biol. Chem. (2002) [Pubmed]
  28. Predictors of objective level of daytime sleepiness in patients with sleep-related breathing disorders. Roehrs, T., Zorick, F., Wittig, R., Conway, W., Roth, T. Chest (1989) [Pubmed]
  29. Ethanol inhibits in-vitro metabolism of nifedipine, triazolam and testosterone in human liver microsomes. Patki, K.C., Greenblatt, D.J., von Moltke, L.L. J. Pharm. Pharmacol. (2004) [Pubmed]
  30. Interaction of rhodanese with mitochondrial NADH dehydrogenase. Pagani, S., Galante, Y.M. Biochim. Biophys. Acta (1983) [Pubmed]
  31. The disease spectrum, epidemiology, and etiology of toxic-shock syndrome. Chesney, P.J., Bergdoll, M.S., Davis, J.P., Vergeront, J.M. Annu. Rev. Microbiol. (1984) [Pubmed]
  32. Comparison of the Vitek Immunodiagnostic Assay System with an indirect immunoassay (Toxostat Test Kit) for detection of immunoglobulin G antibodies to Toxoplasma gondii in clinical specimens. Sandin, R.L., Knapp, C.C., Hall, G.S., Washington, J.A., Rutherford, I. J. Clin. Microbiol. (1991) [Pubmed]
  33. Prevention of nosocomial transmission of Mycobacterium tuberculosis. Cookson, S.T., Jarvis, W.R. Infect. Dis. Clin. North Am. (1997) [Pubmed]
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