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Gene Review

TST  -  thiosulfate sulfurtransferase (rhodanese)

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Disease relevance of TST

  • When the E. coli recombinant protein was analyzed on a nondenaturing gel, only one species was observed that co-electrophoresed with the more electropositive variant seen in purified bovine liver rhodanese [1].
  • Similar rates of increase in TST across the finishing phase corresponded with similar rates of live and carcass weight gain among treatments [2].
  • The amino acid sequence of the protein has similarity to bovine liver rhodanese, an enzyme that transfers the thiol group of thiosulfate to a thiophilic acceptor molecule, and a rhodaneselike protein of Saccharopolyspora erythraea [3].
  • The rhdA gene identified in Azotobacter vinelandii codes for a protein, RhdA, which displays rhodanese (thiosulfate-cyanide sulfurtransferase) activity [4].

Psychiatry related information on TST


High impact information on TST

  • Bovine liver rhodanese is a single polypeptide of 293 amino acids in which the halves of the molecule assume analogous tertiary structures in the absence of substantial sequence homology [6].
  • Rhodanese (EC ) normally occurs as a persulfide of a critical cysteine residue and is believed to function as a sulfur-delivery protein [7].
  • E-Se rhodanese was stable in the presence of excess GSH at neutral pH at 37 degrees C. E-Se rhodanese could effectively replace the high concentrations of selenide normally used in the selenophosphate synthetase in vitro assay in which the selenium-dependent hydrolysis of ATP is measured [7].
  • Formation of a selenium-substituted rhodanese by reaction with selenite and glutathione: possible role of a protein perselenide in a selenium delivery system [7].
  • These results show that a selenium-bound rhodanese could be used as the selenium donor in the in vitro selenophosphate synthetase assay [7].

Chemical compound and disease context of TST


Biological context of TST


Anatomical context of TST


Associations of TST with chemical compounds

  • Mutation of all nonessential cysteine residues in rhodanese turns the enzyme into a form (C3S) that is fully active but less stable than wild type (WT) [19].
  • Chemical modification studies of bovine liver rhodanese have underscored important distinctions between free rhodanese and the catalytic intermediate in which the sulfane atom of the sulfur donor is bound covalently to the enzyme (sulfur-rhodanese) [20].
  • Analysis of rate data for the iodoacetate reaction showed that the apparent pK of this group is 7.8 in free rhodanese and 6.7 to 7.0 in complexes of the enzyme with analogs of sulfur donor substrates, in agreement with the previous inference from steady state kinetic observations [20].
  • Inactivation of free rhodanese by phenylglyoxal in the presence of cyanide was shown to be caused by a novel reaction in which disulfide bonds are formed between Cys-247 and either Cys-254 or Cys-263 [20].
  • Fluorograms of denaturing polyacrylamide gels detected a large increase in a polypeptide that co-migrated with the native protein and reacted with anti-rhodanese antibodies [1].

Other interactions of TST

  • Cyanogen bromide fragments from reduced and carboxymethylated rhodanese have been isolated by gel filtration and ion exchange chromatography on columns of Sephadex G-50 and sulfoethyl-Sephadex C-25, respectively [13].
  • Intermediate cpn60 species, possibly heptamers, are detected at intermediate urea concentrations after addition of unfolded rhodanese [21].
  • The present work demonstrates that the rhodanese-cpn60 complex can be dissociated by urea to allow folding to proceed, thus removing the obligatory requirement for cpn10 and ATP [21].
  • The requirement of both catalase and superoxide dismutase to prevent rhodanese inactivation indicates that hydroxyl radical could be the most efficient inactivating agent [22].
  • Reduced thioredoxin as a sulfur-acceptor substrate for rhodanese [23].

Analytical, diagnostic and therapeutic context of TST

  • Sequence analysis indentified a GroEL-bound fragment of approximately 11,000 M(r) and a well defined fragment of approximately 7,000 M(r) from the two homologous domains of rhodanese [24].
  • Analysis of the peptides by circular dichroism showed that anionic liposomes can induce alpha-helical structure only in rho(1-23) and denatured rhodanese [17].
  • Titration of a sample of sulfur-substituted rhodanese (ES) with either cyanide or sulfite gave a stoichiometry that is consistent with one persulfide/molecule of rhodanese (Mr = 33,000) [25].
  • The two-domain structure of rhodanese was not significantly altered by drastically different crystallization conditions or crystal packing suggesting rigidity of the native rhodanese domains and the stabilization of the interdomain interactions by the crystal environment [26].
  • These results indicate significant stabilization of rhodanese after immobilization, and instabilities caused by adventitious solution components are not the sole reasons for irreversibility of thermal denaturation seen with the soluble enzyme [27].


  1. Expression of cloned bovine adrenal rhodanese. Miller, D.M., Delgado, R., Chirgwin, J.M., Hardies, S.C., Horowitz, P.M. J. Biol. Chem. (1991) [Pubmed]
  2. Effect of live weight gain of steers during winter grazing: II. Visceral organ mass, cellularity, and oxygen consumption. Hersom, M.J., Krehbiel, C.R., Horn, G.W. J. Anim. Sci. (2004) [Pubmed]
  3. Isolation and characterization of a sulfur-regulated gene encoding a periplasmically localized protein with sequence similarity to rhodanese. Laudenbach, D.E., Ehrhardt, D., Green, L., Grossman, A. J. Bacteriol. (1991) [Pubmed]
  4. Crystallization and preliminary crystallographic investigations of rhodanese from Azotobacter vinelandii. Bordo, D., Colnaghi, R., Deriu, D., Carpen, A., Storici, P., Pagani, S., Bolognesi, M. Acta Crystallogr. D Biol. Crystallogr. (1999) [Pubmed]
  5. Modification and inactivation of rhodanese by 2,4,6-trinitrobenzenesulphonic acid. Malliopoulou, T.B., Rakitzis, E.T. J. Enzym. Inhib. (1988) [Pubmed]
  6. The covalent and tertiary structure of bovine liver rhodanese. Ploegman, J.H., Drent, G., Kalk, K.H., Hol, W.G., Heinrikson, R.L., Keim, P., Weng, L., Russell, J. Nature (1978) [Pubmed]
  7. Formation of a selenium-substituted rhodanese by reaction with selenite and glutathione: possible role of a protein perselenide in a selenium delivery system. Ogasawara, Y., Lacourciere, G., Stadtman, T.C. Proc. Natl. Acad. Sci. U.S.A. (2001) [Pubmed]
  8. Different conformations of nascent peptides on ribosomes. Tsalkova, T., Odom, O.W., Kramer, G., Hardesty, B. J. Mol. Biol. (1998) [Pubmed]
  9. Enzyme-mediated sulfide production for the reconstitution of [2Fe-2S] clusters into apo-biotin synthase of Escherichia coli. Sulfide transfer from cysteine to biotin. Bui, B.T., Escalettes, F., Chottard, G., Florentin, D., Marquet, A. Eur. J. Biochem. (2000) [Pubmed]
  10. Enhancement of serine-sensitivity by a gene encoding rhodanese-like protein in Escherichia coli. Hama, H., Kayahara, T., Ogawa, W., Tsuda, M., Tsuchiya, T. J. Biochem. (1994) [Pubmed]
  11. Escherichia coli GlpE is a prototype sulfurtransferase for the single-domain rhodanese homology superfamily. Spallarossa, A., Donahue, J.L., Larson, T.J., Bolognesi, M., Bordo, D. Structure (Camb.) (2001) [Pubmed]
  12. Active site structural features for chemically modified forms of rhodanese. Gliubich, F., Gazerro, M., Zanotti, G., Delbono, S., Bombieri, G., Berni, R. J. Biol. Chem. (1996) [Pubmed]
  13. The covalent structure of bovine liver rhodanese. Isolation and partial structural analysis of cyanogen bromide fragements and the complete sequence of the enzyme. Russell, J., Weng, L., Keim, P.S., Heinrikson, R.L. J. Biol. Chem. (1978) [Pubmed]
  14. Bovine mitochondrial rhodanese is a phosphoprotein. Ogata, K., Dai, X., Volini, M. J. Biol. Chem. (1989) [Pubmed]
  15. Micelle-assisted protein folding. Denatured rhodanese binding to cardiolipin-containing lauryl maltoside micelles results in slower refolding kinetics but greater enzyme reactivation. Zardeneta, G., Horowitz, P.M. J. Biol. Chem. (1992) [Pubmed]
  16. Activation and release of enzymatically inactive, full-length rhodanese that is bound to ribosomes as peptidyl-tRNA. Kudlicki, W., Odom, O.W., Kramer, G., Hardesty, B. J. Biol. Chem. (1994) [Pubmed]
  17. Analysis of the perturbation of phospholipid model membranes by rhodanese and its presequence. Zardeneta, G., Horowitz, P.M. J. Biol. Chem. (1992) [Pubmed]
  18. Mitochondrial rhodanese: membrane-bound and complexed activity. Ogata, K., Volini, M. J. Biol. Chem. (1990) [Pubmed]
  19. Active rhodanese lacking nonessential sulfhydryl groups contains an unstable C-terminal domain and can be bound, inactivated, and reactivated by GroEL. Ybarra, J., Bhattacharyya, A.M., Panda, M., Horowitz, P.M. J. Biol. Chem. (2003) [Pubmed]
  20. Active site cysteinyl and arginyl residues of rhodanese. A novel formation of disulfide bonds in the active site promoted by phenylglyoxal. Weng, L., Heinrikson, R.L., Westley, J. J. Biol. Chem. (1978) [Pubmed]
  21. Alteration of the quaternary structure of cpn60 modulates chaperonin-assisted folding. Implications for the mechanism of chaperonin action. Mendoza, J.A., Demeler, B., Horowitz, P.M. J. Biol. Chem. (1994) [Pubmed]
  22. Interaction of rhodanese with intermediates of oxygen reduction. Cannella, C., Berni, R. FEBS Lett. (1983) [Pubmed]
  23. Reduced thioredoxin as a sulfur-acceptor substrate for rhodanese. Nandi, D.L., Westley, J. Int. J. Biochem. Cell Biol. (1998) [Pubmed]
  24. Binding of defined regions of a polypeptide to GroEL and its implications for chaperonin-mediated protein folding. Hlodan, R., Tempst, P., Hartl, F.U. Nat. Struct. Biol. (1995) [Pubmed]
  25. Spectral differences between rhodanese catalytic intermediates unrelated to enzyme conformation. Chow, S.F., Horowitz, P.M. J. Biol. Chem. (1985) [Pubmed]
  26. NH2-terminal sequence truncation decreases the stability of bovine rhodanese, minimally perturbs its crystal structure, and enhances interaction with GroEL under native conditions. Trevino, R.J., Gliubich, F., Berni, R., Cianci, M., Chirgwin, J.M., Zanotti, G., Horowitz, P.M. J. Biol. Chem. (1999) [Pubmed]
  27. Reversible thermal denaturation of immobilized rhodanese. Horowitz, P., Bowman, S. J. Biol. Chem. (1987) [Pubmed]
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