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Gene Review

Tst  -  thiosulfate sulfurtransferase

Rattus norvegicus

Synonyms: Rhodanese, Thiosulfate sulfurtransferase
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Psychiatry related information on Tst

  • The difference in the levels of rhodanese activity in the two types of rodents is discussed in relation to their dietary habits [1].

High impact information on Tst

  • In this study, the N-terminal 23 residues of the matrix enzyme rhodanese could import several passenger proteins but were unable to import the mature form of mitochondrial aldehyde dehydrogenase (mALDH) [2].
  • Further, rhodanese cross-reacts with anti-MST antibody [3].
  • An active site cysteine residue (Cys246; site of formation of persulfide in catalysis) and an arginine residue (Arg185; substrate binding site) in rhodanese were also conserved in MST [3].
  • The thermodynamic parameters of binding of the peptide RHD and of four of its double D-isomers were determined for 30 nm (SUVs) and 100 nm (LUVs) unilamellar vesicles composed of phosphatidylcholine/phosphatidylglycerol (3:1) using circular dichroism spectroscopy, fluorescence spectroscopy, and isothermal titration calorimetry [4].
  • Computer-generated structural modelling of rat rhodanese indicated that few amino acid substitutions were present within close proximity to the active site or within the hinge region (connecting loop) between the A and B domains [5].

Biological context of Tst


Anatomical context of Tst


Associations of Tst with chemical compounds


Other interactions of Tst


Analytical, diagnostic and therapeutic context of Tst

  • Molecular cloning, sequencing and characterization of cDNA to rat liver rhodanese, a thiosulphate sulphurtransferase [5].
  • Circular dichroism data indicated that a peptide corresponding to the region of fusion between rhodanese and mALDH had less structure than corresponding peptides from imported fusion proteins, suggesting that mALDH may alter the helix in the rhodanese signal sequence, thus preventing import [2].
  • Rhodanese which detoxifes cyanide is also found to be inhibited in rats fed low protein diet while the inhibition was only marginal in the high protein fed groups [17].


  1. Kidney rhodanese from the guinea pig (Lepus caniculus) and albino rat (Mus musculus). Anosike, E.O., Jack, A.S. Enzyme (1982) [Pubmed]
  2. Influence of the mature portion of a precursor protein on the mitochondrial signal sequence. Waltner, M., Hammen, P.K., Weiner, H. J. Biol. Chem. (1996) [Pubmed]
  3. Cytosolic mercaptopyruvate sulfurtransferase is evolutionarily related to mitochondrial rhodanese. Striking similarity in active site amino acid sequence and the increase in the mercaptopyruvate sulfurtransferase activity of rhodanese by site-directed mutagenesis. Nagahara, N., Okazaki, T., Nishino, T. J. Biol. Chem. (1995) [Pubmed]
  4. Interaction of a mitochondrial presequence with lipid membranes: role of helix formation for membrane binding and perturbation. Wieprecht, T., Apostolov, O., Beyermann, M., Seelig, J. Biochemistry (2000) [Pubmed]
  5. Molecular cloning, sequencing and characterization of cDNA to rat liver rhodanese, a thiosulphate sulphurtransferase. Weiland, K.L., Dooley, T.P. Biochem. J. (1991) [Pubmed]
  6. Influence of cassava diets on placental thiocyanate transfer, tissue rhodanese activity and performance of rats during gestation. Tewe, O.O., Maner, J.H., Gomez, G. J. Sci. Food Agric. (1977) [Pubmed]
  7. Toxicogenomics of resveratrol in rat liver. Hebbar, V., Shen, G., Hu, R., Kim, B.R., Chen, C., Korytko, P.J., Crowell, J.A., Levine, B.S., Kong, A.N. Life Sci. (2005) [Pubmed]
  8. Immobilized rhodanese: some aspects of anion inhibition kinetics and modulation by cations. Nok, A.J., Nasir, S.M., Sa Adatu, Y. J. Biochem. Toxicol. (1993) [Pubmed]
  9. Inhibition of rat liver rhodanese by di-, tricarboxylic, and alpha-keto acids. Oi, S. J. Biochem. (1975) [Pubmed]
  10. Metabolism of organonitriles to cyanide by rat nasal tissue enzymes. Dahl, A.R., Waruszewski, B.A. Xenobiotica (1989) [Pubmed]
  11. Variations in rhodanese activity in rat submandibular gland with time of day. Abiko, Y., Tanaka, M., Muro, H. Nichidai Koko Kagaku (1984) [Pubmed]
  12. L-cysteine metabolism in guinea pig and rat tissues. Wróbel, M., Ubuka, T., Yao, W.B., Abe, T. Comp. Biochem. Physiol. B, Biochem. Mol. Biol. (1997) [Pubmed]
  13. Bioactivation of cyanide to cyanate in sulfur amino acid deficiency: relevance to neurological disease in humans subsisting on cassava. Tor-Agbidye, J., Palmer, V.S., Lasarev, M.R., Craig, A.M., Blythe, L.L., Sabri, M.I., Spencer, P.S. Toxicol. Sci. (1999) [Pubmed]
  14. Effects of oxygen on the antagonism of cyanide intoxication: cytochrome oxidase, in vitro. Isom, G.E., Way, J.L. Toxicol. Appl. Pharmacol. (1984) [Pubmed]
  15. The case against laetrile: the fraudulent cancer remedy. Greenberg, D.M. Cancer (1980) [Pubmed]
  16. The cyanide-metabolizing enzyme rhodanese in rat nasal respiratory and olfactory mucosa. Dahl, A.R. Toxicol. Lett. (1989) [Pubmed]
  17. Effect of protein supplemented cassava diet in rats. Sreeja, V.G., Leelamma, S. Indian J. Biochem. Biophys. (1996) [Pubmed]
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