Advertisement

Subcellular Compartmentation and Biological Functions of Mercaptopyruvate Sulphurtransferase and Rhodanese

  • Aleksander Koj

Abstract

According to present knowledge transfer of bivalent or sulphane sulphur from thiosulphate, thiocystine, 3-mercaptopyruvate and some other donors is catalyzed by at least three different enzymes: rhodanese /EC 2.8. 1.1/, thiosulphate reductase /no EC number/ and mercapto-pyruvate sulphurtransferase /EC 2.8.1.2/ /for references see Westley, 1973; Koj et al.,1975/. The mechanism of their action is not uniform: rhodanese operates by a double-displacement mechanism /cf. Westley, 1973/ mercaptopyruvate sulphurtransferase by a sequential reaction /Jarabak and Westley,1978/, while the mode of action of thiosulphate reductase is not elucidated.

Keywords

Glutamate Dehydrogenase COOH COOH Selective Permeation Acid Labile Sulphide Intracellular Distribution Pattern 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Auriga,M., and Koj, A., 1975, Protective effect of rhodanese on the respiration of isolated mitochondria intoxicated with cyanide, Bull.Acad.Pol. Sci., Ser.Sci.Biol. 23: 305.Google Scholar
  2. Bonomi, F., Pagani, S., Cerletti, P., Cannella C., 1977, Rhodanes-mediated sulfur transfer to succinate dehydrogenase, Eur,J,Biochem., 72: 17CrossRefGoogle Scholar
  3. Crompton, M., Palmieri, F., Capano, M., and Quaglia- riello, E., 1974, The transport of thiosulphate in rat liver mitochondria, FEBS Lett, 46: 247.PubMedCrossRefGoogle Scholar
  4. DeDuve, C., Pressman, B.C., Gianetto, R., Wattiaux, R., and Appelmans, F., 1955 Tissue fractionation studies. Intracellular distribution patterns of enzymes in rat liver tissues, Biochem.J., 60: 604.Google Scholar
  5. Dudek, M., Frendo, J., and Koj, A,, 1979, Subcellular compartmentation of rhodanese and 3-morcaptopyru- vate sulphurtransferase in the liver of some vertebrate species, Comp.Biochem.Physiol.Google Scholar
  6. Finazzi-Agro, A., Cannella, C., Graziani, M.T., and Cavallini, D., 1971, A possible role for rhodanese: the formation of “labile” sulphur from thiosulphate FEBS Lett., 16: 172.CrossRefGoogle Scholar
  7. Jarabak, R., and J. Vestley, 1978, Steady state kinetics of 3-m©rcaptopyruvate sulphurtransferase from bovine kidney, Arch.Bioch.Bioph., 185: 458.CrossRefGoogle Scholar
  8. Kasperczyk, H., Koj, A., and Z. Wasylewski, 1977, Similarity of some molecular and catalytic parameters of mitochondrial and cytosolic mercapto- pyruvate sulphurtransferase from rat liver, Bull. Acad, Pol.Sci.,Ser.Sci.Biol., 25: 7.Google Scholar
  9. Koj, A., and Ffendo, J., 1967, Oxidation of thiosulphate to sulphate in animal tissues, Folia Biol./Krakow/, 15: 49.Google Scholar
  10. Koj, A., Frendo, J., and Wojtczak, L., 1975, Subcellular distribution and intramitochondrial localization of three sulphurtransferases in rat liver, FEBS Lett., 57: 42.PubMedCrossRefGoogle Scholar
  11. Koj, A., Michalik, M., and Kasperczyk, H., 1977, Mito-chondrial and cytosol activities of three sulphur-transferases in some rat tissues and Morris hepatomas, Bull.Acad.Pol.Sci tSer.Sci.Biol. 25: 1Google Scholar
  12. Marra, E., Boonan, S., Saccone, C., and Quagliariello, E., 1978, Studies on the selective permeation of radioactivelly labelled aspartate aminotransferase isozymes into mitochondria in vitro, Eur.J.Bio chem. 83: 427.Google Scholar
  13. Schatz, G, and Mason, T.L., 1974, The biosynthesis of mitochondrial proteins, Ann.Rev.Biochem.: 51Google Scholar
  14. Schievelbein, H., Baumeister, R., and Vogel, R., 1969, Comparative investigations on the activity of thiosulphate sulphurtransferase, Naturvissenschaf- ten,56:4l6.Google Scholar
  15. Sörbo, B., 1957 Sulphite and complex-bound cyanide as sulphur acceptors for rhodanese, Acta Chem. Scand., 11: 628.CrossRefGoogle Scholar
  16. Szczepkowski, T.W., and Wood, J.L., 1967, The cystathio- naserhodanese system, Biochim. Biophys. Acta, 139: 469.Google Scholar
  17. Taniguchi, T., and Kimura, T., 1974, Role of 3-mercapto- pyruvate sulphurtransferase in the formation of the iron-sulphur chromophore of adrenal ferredoxin, Biochim. Biophys.Acta, 364: 284.Google Scholar
  18. Volini, M, Craven, D., and Ogata, K., 1977 Rhodanese iron protein association in bovine liver extracts, Biochem. Biophys.Res.Comm., 79: 890.CrossRefGoogle Scholar
  19. Westley, J., 1973 Rhodanese, Adv.Enzymol., 39: 327Google Scholar

Copyright information

© Plenum Press, New York 1980

Authors and Affiliations

  • Aleksander Koj
    • 1
  1. 1.Institute of Molecular BiologyJagiellonian University, GrodzkaKrakowPoland

Personalised recommendations