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Thiosulfate sulfurtransferase

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Springer Handbook of Enzymes

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References

  1. Scott, E.M.; Wright, R.C.: Identity of β-mercaptopyruvate sulfurtransferase and rhodanese in human erythrocytes. Biochem. Biophys. Res. Commun., 97, 1334–1338 (1980)

    Article  PubMed  CAS  Google Scholar 

  2. Pagani, S.; Sessa, G.; Sessa, F.; Colnaghi, R.: Properties of Azotobacter vinelandii rhodanese. Biochem. Mol. Biol. Int., 29, 595–604 (1993)

    PubMed  CAS  Google Scholar 

  3. Vazquez, E.S.; Buzaleh, A.M.; Wider, E.A.; Battle, A.M.Del C.: Porphyrin biosynthesis in Rp. palustris. X. Purification and some properties of rhodanese. Int. J. Biochem., 19, 1193–1197 (1987)

    Article  CAS  Google Scholar 

  4. Wrobel, M.; Frendo, J.: Comparison of some molecular and catalytic properties of mitochondrial and cytosolic rhodanese and mercaptopyruvate sulphurtransferase from frog (Rana temporaria) liver. Bull. Pol. Acad. Sci. Biol. Sci., 32, 303–313 (1984)

    CAS  Google Scholar 

  5. Van Rensburg, L.J.; Schabort, J.C.: Rhodanese from Cercopithecus aethiops (vervet monkey) liver. I. Purification and some physical characteristics. Int. J. Biochem., 16, 539–546 (1984)

    Article  Google Scholar 

  6. Anosike, E.O.; Jack, A.S.: A comparison of some biochemical properties of liver thiosulphate sulphurtransferase from guinea pig (Lepus caniculus) & albino rat. Indian J. Biochem. Biophys., 19, 13–16 (1982)

    PubMed  CAS  Google Scholar 

  7. Cannella, C.; Pecci, L.; Federici, G.: Crystalline rhodanese from beef kidney. Ital. J. Biochem., 21, 1–7 (1972)

    PubMed  CAS  Google Scholar 

  8. Westley, J.: Rhodanese. Adv. Enzymol. Relat. Areas Mol. Biol., 39, 327–368 (1973)

    Article  CAS  Google Scholar 

  9. Westley, J.: Thiosulfate: cyanide sulfurtransferase (rhodanese). Methods Enzymol., 77, 285–291 (1981)

    PubMed  CAS  Google Scholar 

  10. Drenth, J.; Smit, J.D.G.: Crystallographic data for rhodanese from bovine liver. Biochem. Biophys. Res. Commun., 45, 1320–1322 (1971)

    Article  PubMed  CAS  Google Scholar 

  11. Burrous, M.R.; Lane, J.; Westley, A.; Westley, J.: Chromogenic and fluorigenic substrates for sulfurtransferases. Methods Enzymol., 143, 235–239 (1987)

    Article  PubMed  CAS  Google Scholar 

  12. Oi, S.: Inhibition of bovine liver rhodanese by α-ketoglutarate. J. Biochem., 76, 455–458 (1974)

    PubMed  CAS  Google Scholar 

  13. Pagani, S.; Bonomi, F.; Cerletti, P.: The inhibition of rhodanese by lipoate and iron-sulfur proteins. Biochim. Biophys. Acta, 742, 116–121 (1983)

    PubMed  CAS  Google Scholar 

  14. Miller, D.M.; Kurzban, G.P.; Mendoza, J.A.; Chirgwin, J.M.; Hardies, S.C.; Horowitz, P.M.: Recombinant bovine rhodanese: purification and comparison with bovine liver rhodanese. Biochim. Biophys. Acta, 1121, 286–292 (1992)

    PubMed  CAS  Google Scholar 

  15. Miller, D.M.; Delgado, R.; Chirgwin, J.M.: Expression of cloned bovine adrenal rhodanese. J. Biol. Chem., 266, 4686–4691 (1991)

    PubMed  CAS  Google Scholar 

  16. Horowitz, P.M.; Patel, K.: Some comparisons between solution and crystal properties of thiosulfate sulfurtransferase. Biochem. Biophys. Res. Commun., 94, 419–423 (1980)

    Article  PubMed  CAS  Google Scholar 

  17. Oi, S.: Inhibition of rat liver rhodanese by di-, tricarboxylic, and α-keto acids. J. Biochem., 78, 825–834 (1975)

    PubMed  CAS  Google Scholar 

  18. Boey, C.G.; Yeoh, H.H.; Chew, M.Y.: Purification of tapioca leaf rhodanese. Phytochemistry, 15, 1343–1344 (1976)

    Article  CAS  Google Scholar 

  19. Oi, S.: Purification and some properties of Trametes sanguinea rhodanese. Agric. Biol. Chem., 37, 629–635 (1973)

    CAS  Google Scholar 

  20. Pallini, R.; Guazzi, G.C.; Cannella, C.; Cacace, M.G.: Cloning and sequence analysis of the human liver rhodanese: comparison with the bovine and chicken enzymes. Biochem. Biophys. Res. Commun., 180, 887–893 (1991)

    Article  PubMed  CAS  Google Scholar 

  21. Vandenbergh, P.A.; Berk, R.S.: Purification and characterization of rhodanese from Acinetobacter calcoaceticus. Can. J. Microbiol., 26, 281–286 (1980)

    Article  PubMed  CAS  Google Scholar 

  22. Fukumori, Y.; Hoshiko, K.; Yamanaka, T.: Purification and some properties of thiosulphate-cleaving enzyme from Thiobacillus novellus. FEMS Microbiol. Lett., 65, 159–164 (1989)

    Article  CAS  Google Scholar 

  23. Turkowsky, A.; Blotevogel, K.-H.; Fischer, U.: Properties of a soluble thiosulfate sulfur transferase (rhodanese) of the marine methanogen Methanosarcina frisia. FEMS Microbiol. Lett., 81, 251–256 (1991)

    Article  CAS  Google Scholar 

  24. Alexander, K.; Volini, M.: Properties of an Escherichia coli rhodanese. J. Biol. Chem., 262, 6595–6604 (1987)

    PubMed  CAS  Google Scholar 

  25. Aird, B.A.; Heinrikson, R.L.; Westley, J.: Isolation and characterization of a prokaryotic sulfurtransferase. J. Biol. Chem., 262, 17327–17335 (1987)

    PubMed  CAS  Google Scholar 

  26. Bauer, M.; Papenbrock, J.: Identification and characterization of single-domain thiosulfate sulfurtransferases from Arabidopsis thaliana. FEBS Lett., 532, 427–431 (2002)

    Article  PubMed  CAS  Google Scholar 

  27. Spallarossa, A.; Forlani, F.; Pagani, S.; Salvati, L.; Visca, P.; Ascenzi, P.; Bolognesi, M.; Bordo, D.: Inhibition of Azotobacter vinelandii rhodanese by NO-donors. Biochem. Biophys. Res. Commun., 306, 1002–1007 (2003)

    Article  PubMed  CAS  Google Scholar 

  28. Pagani, S.; Forlani, F.; Carpen, A.; Bordo, D.; Colnaghi, R.: Mutagenic analysis of Thr-232 in rhodanese from Azotobacter vinelandii highlighted the differences of this prokaryotic enzyme from the known sulfurtransferases. FEBS Lett., 472, 307–311 (2000)

    Article  PubMed  CAS  Google Scholar 

  29. Melino, S.; Cicero, D.O.; Orsale, M.; Forlani, F.; Pagani, S.; Paci, M.: Azotobacter vinelandii rhodanese: Selenium loading and ion interaction studies. Eur. J. Biochem., 270, 4208–4215 (2003)

    Article  PubMed  CAS  Google Scholar 

  30. Nandi, D.L.; Horowitz, P.M.; Westley, J.: Rhodanese as a thioredoxin oxidase. Int. J. Biochem. Cell Biol., 32, 465–473 (2000)

    Article  PubMed  CAS  Google Scholar 

  31. Ybarra, J.; Bhattacharyya, A.M.; Panda, M.; Horowitz, P.M.: Active rhodanese lacking nonessential sulfhydryl groups contains an unstable C-term-inal domain and can be bound, inactivated, and reactivated by GroEL*. J. Biol. Chem., 278, 1693–1699 (2003)

    Article  PubMed  CAS  Google Scholar 

  32. Trevino, R.J.; Gliubich, F.; Berni, R.; Cianci, M.; Chirgwin, J.M.; Zanotti, G.; Horowitz, P.M.: NH −2 terminal sequence truncation decreases the stability of bovine rhodanese, minimally perturbs its crystal structure, and enhances interaction with GroEL under native conditions. J. Biol. Chem., 274, 13938–13947 (1999)

    Article  PubMed  CAS  Google Scholar 

  33. Luo, G.-X.; Horowitz, P.M.: The sulfurtransferase activity and structure of rhodanese are affected by site-directed replacement of Arg-186 or Lys-249. J. Biol. Chem., 269, 8220–8225 (1994)

    PubMed  CAS  Google Scholar 

  34. Miller-Martin, D.M.; Chirgwin, J.M.; Horowitz, P.M.: Mutations of noncatalytic sulfhydryl groups influence the stability, folding, and oxidative susceptibility of rhodanese. J. Biol. Chem., 269, 3423–3428 (1994)

    CAS  Google Scholar 

  35. Kramer, G.; Ramachandiran, V.; Horowitz, P.; Hardesty, B.: An additional serine residue at the C terminus of rhodanese destabilizes the enzyme. Arch. Biochem. Biophys., 385, 332–337 (2001)

    Article  PubMed  CAS  Google Scholar 

  36. Nazifi, S.; Aminlari, M.; Alaibakhsh, M.A.: Distribution of rhodanese in tissues of goat (Capra hircus). Comp. Biochem. Physiol. B, 134B, 515–518 (2003)

    Article  CAS  Google Scholar 

  37. Trevino, R.J.; Hunt, J.; Horowitz, P.M.; Chirgwin, J.M.: Chinese hamster rhodanese cDNA: activity of the expressed protein is not blocked by a C-terminal extension. Protein Expr. Purif., 6, 693–699 (1995)

    Article  PubMed  CAS  Google Scholar 

  38. Ray, W.K.; Zeng, G.; Potters, M.B.; Mansuri, A.M.; Larson, T.J.: Characterization of a 12-kilodalton rhodanese encoded by glpE of Escherichia coli and its interaction with thioredoxin. J. Bacteriol., 182, 2277–2284 (2000)

    Article  PubMed  CAS  Google Scholar 

  39. Adams, H.; Teertstra, W.; Koster, M.; Tommassen, J.: PspE (phage-shock protein E) of Escherichia coli is a rhodanese. FEBS Lett., 518, 173–176 (2002)

    Article  PubMed  CAS  Google Scholar 

  40. Wrobel, M.; Wlodek, L.: Effects of thiazolidine-4(R)-carboxylates and other low-molecular-weight sulfur compounds on the activity of mercaptopyruvate sulfurtransferase, rhodanese, and cystathionase in Ehrlich ascites tumor cell and tumor-bearing mouse liver. Amino Acids, 12, 309–314 (1997)

    Article  CAS  Google Scholar 

  41. Picton, R.; Eggo, M.C.; Merrill, G.A.; Langman, M.J.S.; Singh, S.: Mucosal protection against sulphide: Importance of the enzyme rhodanese. Gut, 50, 201–205 (2002)

    Article  PubMed  CAS  Google Scholar 

  42. Lee, C.Y.; Hwang, J.H.; Lee, Y.S.; Cho, K.S.: Purification and characterization of mouse liver rhodanese. J. Biochem. Mol. Biol., 28, 170–176 (1995)

    CAS  Google Scholar 

  43. Wrobel, M.; Papla, B.: Rhodanese activity and total sulfur content in frog and mouse liver. Folia Histochem. Cytobiol., 38, 11–17 (2000)

    PubMed  CAS  Google Scholar 

  44. Vazquez, E.; Polo, C.; Stedile, G.; Schebor, C.; Karahanian, E.; Batlle, A.: Isolation and partial purification of mitochondrial and cytosolic rhodanese from liver of normal and p-dimethylaminoazobenzene treated mice. Int. J. Biochem. Cell Biol., 27, 523–529 (1995)

    Article  PubMed  CAS  Google Scholar 

  45. Vazquez, E.; Gazzaniga, S.; Polo, C.; Batlle, A.: Mitochondrial and cytosolic rhodanese from liver of DAB-treated mice. III. Inhibition kinetic studies. Cancer Biochem. Biophys., 15, 285–293 (1997)

    PubMed  CAS  Google Scholar 

  46. Ihm, J.-S.; Kim, Y.-H.: Thiosulfate sulfurtransferase and UDP-glucuronosyl-transferase activities in cholestatic rat liver induced by common bile duct ligation. Exp. Mol. Med., 29, 197–201 (1997)

    CAS  Google Scholar 

  47. Ezzi, M.I.; Pascual, J.A.; Gould, B.J.; Lynch, J.M.: Characterization of the rhodanese enzyme in Trichoderma spp. Enzyme Microb. Technol., 32, 629–634 (2003)

    CAS  Google Scholar 

  48. Aminlari, M.; Vaseghi, T.; Ali Kargar, M.: The cyanide-metabolizing enzyme rhodanese in different parts of the respiratory systems of sheep and dog. Toxicol. Appl. Pharmacol., 124, 67–71 (1994)

    Article  PubMed  CAS  Google Scholar 

  49. Kudlicki, W.; Coffman, A.; Kramer, G.; Hardesty, B.: Renaturation of rhodanese by translational elongation factor (EF) Tu. Protein refolding by EF-Tu flexing. J. Biol. Chem., 272, 32206–32210 (1997)

    Article  PubMed  CAS  Google Scholar 

  50. Bordo, D.; Deriu, D.; Colnaghi, R.; Carpen, A.; Pagani, S.; Bolognesi, M.: The crystal structure of a sulfurtransferase from Azotobacter vinelandii highlights the evolutionary relationship between the rhodanese and phosphatase enzyme families. J. Mol. Biol., 298, 691–704 (2000)

    Article  PubMed  CAS  Google Scholar 

  51. Gliubich, F.; Berni, R.; Colapietro, M.; Barba, L.; Zanotti, G.: Structure of sulfur-substituted rhodanese at 1.36 A resolution. Acta Crystallogr. Sect. D, 54 (Pt 4), 481–486 (1998)

    Article  CAS  Google Scholar 

  52. Al-Qarawi, A.A.; Mousa, H.M.; Ali, B.H.: Tissue and intracellular distribution of rhodanese and mercaptopyruvate sulfurtransferase in ruminants and birds. Vet. Res., 32, 63–70 (2001)

    Article  PubMed  CAS  Google Scholar 

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(2008). Thiosulfate sulfurtransferase. In: Schomburg, D., Schomburg, I., Chang, A. (eds) Springer Handbook of Enzymes. Springer Handbook of Enzymes, vol 39. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-540-71524-5_31

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