Molecular and Cellular Biochemistry

, Volume 12, Issue 2, pp 89–92 | Cite as

Oxidation of Se-Carboxymethyl-selenocysteine by L-aminoacid oxidase and by D-aspartate oxidase

  • C. de Marco
  • A. Rinaldi
  • M. R. Dessi'
  • S. Dernini
General and Review Articles a. general articles
Received:

Summary

Se-Carboxymethyl-DL-selenocysteine (CMSeC) has been prepared in a pure crystalline form from selenocysteine and monochloroacetic acid. It has been shown that CMSeC is a substrate for the L-aminoacid oxidase from snake venom and for the D-aspartate oxidase from beef kidney. Oxygen consumption and ammonia production indicate that only the L or the D form of CMSeC are acted upon respectively by one or the other of the above enzymes. No noticeable differences were shown in the oxidation rate of CMSeC and S-carboxymethylcysteine, an indication that the substitution of a selenium for a sulfur atom in the molecule does not greatly affect the substrate specificity of the two enzymes. Data have been obtained suggesting that the product of the oxidative deamination of CMSeC is Se-carboxymethyl-selenopyruvic acid.

Keywords

Oxygen Sulfur Ammonia Selenium Oxygen Consumption 
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.
This is a preview of subscription content, log in to check access.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. 1.
    A. Rinaldi, M. B. Fadda, G. Piccaluga, C. De Marco, 1973. Ital. J. Biochem. 22, 46–54.Google Scholar
  2. 2.
    C. De Marco, A. Rinaldi, G. Piccaluga, M. B. Fadda, 1974. Mol. Cell. Biochem. 3, 3–7.Google Scholar
  3. 3.
    A. Fiori, M. Costa, E. Barboni, 1972. Physiol. Chem. Physics, 4, 457–466.Google Scholar
  4. 4.
    L. Michaelis, M. P. Schubert, 1934. J. Biol. Chem., 106, 331–341.Google Scholar
  5. 5.
    A. Rinaldi, 1971. Enzymologia, 40, 314–321.Google Scholar
  6. 6.
    C. De Marco, A. Rinaldi, 1971. FEBS Letters, 15, 27–29.Google Scholar
  7. 7.
    T. E. Friedemann, G. E. Haugen, 1943. J. Biol. Chem. 147, 415–442.Google Scholar
  8. 8.
    D. Cavallini, B. Mondovì, 1957. Clin. Chim. Acta 2, 312–315.Google Scholar
  9. 9.
    K. Shinoara, 1935. J. Biol. Chem. 112, 683–696.Google Scholar
  10. 10.
    C. De Marco, A. Rinaldi, S. Dernini, D. Cavallini, 1975. Gazz. Chim. Ital. 105, 1–3.Google Scholar
  11. 11.
    G. Toennies, J. J. Kolb, 1951. Anal. Chem. 23, 823–825.Google Scholar
  12. 12.
    F. Feigl, 1966. Spot Tests in Organic Analysis, 7th Ed., Elsevier, Amsterdam, p. 88.Google Scholar
  13. 13.
    A. Shrift, 1961. Fed. Proc. 20, 695.Google Scholar
  14. 14.
    C. De Marco, A. Rinaldi, S. Dernini, M. R. Dessì, 1975. Ital. J. Biochem., 24, 207–218.Google Scholar

Copyright information

© Dr. W. Junk b.v. Publishers 1976

Authors and Affiliations

  • C. de Marco
    • 1
    • 2
  • A. Rinaldi
    • 1
    • 2
  • M. R. Dessi'
    • 1
    • 2
  • S. Dernini
    • 1
    • 2
  1. 1.I'Cattedra di Chimica Biologica della Facoltà di Scienze M. F. N. della Università di RomaRomeItaly
  2. 2.Istituto di Chimica Biologica della Università di CagliariCagliariItaly

Personalised recommendations