The Stabilizing Protein, Protein-A, of Cysteine Dioxygenase

  • Kenji Yamaguchi
  • Yu Hosokawa
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 217)

Abstract

Cysteine dioxygenase [EC.1.13.11.20] catalyzes the oxygenation of cysteine to cysteine sulfinic acid, a key intermediate of cysteine metabolism to hypotaurine, taurine, isethionic acid and sulfate in mammalian tissues (1,3,8,10,11,18,19,22). The rat liver cysteine dioxygenase is obtained as an inactive form, which is activated by preincubation with L-cysteine under anaerobic condition, but the activated enzyme is rapidly and irreversibly inactivated during aerobic assay conditions. This inactivation during assay is prevented by a distinct cytoplasmic protein, called protein-A (13,14,18).

Keywords

High Protein Diet Standard Assay Condition Sulfur Amino Acid Hepatic Enzyme Activity Cysteine Sulfinic Acid 
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.

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References

  1. 1.
    Chapeville, F., and Fromageot, P., 1955, La formation de l’acide cysteinesulfinique a partir la cysteine chez le rat, Biochim. Biophys. Acta, 17:275.PubMedCrossRefGoogle Scholar
  2. 2.
    Daniels, K.H., and Stipanuk, M.H., 1982, The effect of dietary cysteine level on cysteine metabolism in rats, J. Nutr., 112:2130–2141.PubMedGoogle Scholar
  3. 3.
    De Marco, C, Mosti, R., and Cavallini, D., 1966, Sulla ossidazion della cisteina e della cisteamina a dirivati solfinice, catalizata dal fegato di ratto, Boll. Soc. Ital. Biol. Sper., 42:94–96.PubMedGoogle Scholar
  4. 4.
    Di Giorgio, R.M., Tucci G., and Macaione, S., 1975, Cysteine oxidase activity in rat retina during development, Life Sci., 16:429–436.PubMedCrossRefGoogle Scholar
  5. 5.
    Hosokawa, Y., Yamaguchi, K., Kohashi, N., Kori, Y., Fujii, O., and Ueda, I., 1980, Immaturity of the enzyme activity and response to inducers of rat liver cysteine dioxygenase during development, J. Biochem., 88:389–394.PubMedGoogle Scholar
  6. 6.
    Hosokawa, Y., Kohashi, N., and Yamaguchi, K., 1980, Study of cysteine dioxygenase, Sulfur-containing Amino Acids, 1:251–263.Google Scholar
  7. 7.
    Hosokawa, Y., Fujii, O., Nasu, S., and Yamaguchi, K., 1980, Study of the stabilizing protein of cysteine dioxygenase, Sulfur-containing Amino Acids, 3:237–243.Google Scholar
  8. 8.
    Jacobsen, J.G., and Smith Jr., L.H., 1968, Biochemistry and physiology of taurine and taurine derivatives, Physiol. Rev., 48:424–511.PubMedGoogle Scholar
  9. 9.
    Kohashi, N., Yamaguchi, K., Hosokawa, Y., Kori, Y., Fujii, O., and Ueda, I., 1978, Dietary control of cysteine dioxygenase in rat liver, J. Biochem., 84:159–168.PubMedGoogle Scholar
  10. 10.
    Lombardini, J.B., Turini, P., Biggs, D.R., and Singer, T.P., 1969, Cysteine oxygenase: 1. General properties, Physiol. Chem. & Physics, 1:1–23.Google Scholar
  11. 11.
    Lombardini, J.B., Singer, T.P., and Boyer, P.D., 1969, Cysteine oxygenase: 2. Study on the metabolism of the reaction with 18oxygen, J. Biol. Chem., 244:1172–1175.PubMedGoogle Scholar
  12. 12.
    Loriette, C., and Chatagner, F., 1978, Cysteine oxidase and cysteine sulfinic acid decarboxylase in developing rat liver, Experientia, 34:981–982.PubMedCrossRefGoogle Scholar
  13. 13.
    Sakakibara, S., Yamaguchi, K., Ueda, I., and Sakamoto, Y., 1973, Two components of cysteine oxldase In rat liver, Biochim. Biophys. Res. Commun., 52:1093–1099.CrossRefGoogle Scholar
  14. 14.
    Sakaibara, S., Yamaguchi, K., Hosokawa, Y., Kohashl, N., Ueda, I., and Sakamoto, Y., 1976, Purification and some proerties of rat liver cysteine oxidase(cysteine dioxygenase), Biochim. Biophys. Acta, 422:273–279.CrossRefGoogle Scholar
  15. 15.
    Sorbo, B., and Ewetz, L., 1965, Enzymatic oxidation of cysteine to cysteine-sulfinate in rat liver, Biochem. Biophys. Res. Commun., 19:359–363.CrossRefGoogle Scholar
  16. 16.
    Stipauk, M.H., 1979, Effect of excess dietary methionione on the catabolism of cysteine in rats, J. Nutr., 109:2126–2139.Google Scholar
  17. 17.
    Tabachnik, M., and Turver, H., 1955, The conversion of methionine-35S to cystathionine-35s and taurine-35S in the rat, Arch. Biochem. Biophys., 56:115–121.CrossRefGoogle Scholar
  18. 18.
    Yamaguchi, K., Hosokawa, Y., Kohashi, N., Kori, Y., Sakakbara S., and Ueda, I., 1978, Rat liver cysteine dioxygenase, J. Biochem., 83:479–491.PubMedGoogle Scholar
  19. 19.
    Yamaguchi, Y., Sakakibara, S., Koga K., and Ueda, I., 1971, Induction and activation of cysteine oxidase of rat liver, Biochim. biophys. Acta, 273: 502–512.CrossRefGoogle Scholar
  20. 20.
    Yamaguchi, K., Sakakibara, S., Asamizu, J., and Ueda, I., 1973, Induction and activation of in vivoactivity of cysteine oxidase of rat liver: II. The measurement of cysteine metabolism in vivo and the activaton of in vivo activity of cysteine oxidase, Biochim. Biophys. Acta, 297:48–59.PubMedCrossRefGoogle Scholar
  21. 21.
    Yamaguchi, K., Hosokawa, Y, Niizeki, S., Tojo J., and Sato, I., 1985, Nutritional significance of cysteine dioxygenase on the biological evaluation of dietary protein in growing rats in: “Taurine: Biological Actions and Clinical Perspectives”, S.S. Oja, L. Ahtee, P. Kontro and M.K. Passonen eds., Alan R. Liss, Inc., New York, pp. 23–32.Google Scholar
  22. 22.
    Yamaguchi, K., 1981, Cysteine dioxygenase and its possible role on taurine formation in rats, in: “The Effects of Taurine on Excitable Tissues”, S.W. Schaffer, S.L. Baskin, and J.J. Kocsis Eds., Spectrum Pub. Inc., New York, pp. 5–20.CrossRefGoogle Scholar
  23. 23.
    Yamaguchi, K., 1980, Cysteine dioxygenase of rat liver: some properties and its significance on cysteine metabolism of rat in: “Natural Sulfur Compounds”, D. Cavallini, G.E. Gaull and V. Zappia eds., Plenum Publ. Co., New York, pp. 175–186.CrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media New York 1987

Authors and Affiliations

  • Kenji Yamaguchi
    • 1
  • Yu Hosokawa
    • 1
  1. 1.Division of Maternal and Child NutritionNational Institute of Nutrition1-23-1, Toyama, Shinjuku-ku, TokyoJapan

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