Cysteamine dioxygenase

Part of the Springer Handbook of Enzymes book series (HDBKENZYMES, volume 25)

Nomenclature

EC number

1.13.11.19

Systematic name

cysteamine:oxygen oxidoreductase

Recommended name

cysteamine dioxygenase

Synonyms

cysteamine oxygenase

oxygenase, cysteamine

oxygenase, cysteamine di-

persulfurase

CAS registry number

9033-41-4

Keywords

Electron Paramagnetic Resonance Methylene Blue Ammonium Chloride Ammonium Sulfate Enzymatic Oxidation 
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]
    Nozaki, M.: Nonheme iron dioxygenase. Mol. Mech. Oxygen Activ. (Hayaishi, O., ed.) Academic Press, New York, 135–165 (1974)Google Scholar
  2. [2]
    Richerson, R.B.; Ziegler, D.M.: Cysteamine dioxygenase. Methods Enzymol., 143, 410-415 (1987)Google Scholar
  3. [3]
    Duffel, M.W.; Logan, D.J.; Ziegler, D.M.: Selenocysteine. Methods Enzymol., 143, 148–155 (1987)CrossRefGoogle Scholar
  4. [4]
    Cavallini, D.; Scandurra, R.; Dupre, S.: Cysteamine oxygenase (horse kidney). Methods Enzymol., 17B, 479–483 (1971)Google Scholar
  5. [5]
    Cavallini, D.; Federici, G.; Ricci, G.; Dupre, S.; Antonucci, A.; De Marco, C.: The specificity of cysteamine oxygenase. FEBS Lett., 56, 348–351 (1975)PubMedCrossRefGoogle Scholar
  6. [6]
    Rotilio, G.; Federici, G.; Calabrese, L.; Costa, M.; Cavallini, D.: An electron paramagnetic resonance study of the nonheme iron of cysteamine oxygenase. J. Biol. Chem., 245, 6235–6239 (1970)PubMedGoogle Scholar
  7. [7]
    Cavallini, D.; Canella, C.; Federici, G.; Dupre, S.; Fiori, A.; Del Grosso, E.: Molecular weight of native and dissociated cysteamine oxygenase. Eur. J. Biochem., 16, 537–540 (1970)PubMedCrossRefGoogle Scholar
  8. [8]
    Cavallini, D.; Canella, C.; Barboni, E.; Fiori, A.; Marcucci, M.: Interaction of cysteamine oxygenase with o-phenanthroline. Eur. J. Biochem., 11, 360–363 (1969)PubMedCrossRefGoogle Scholar
  9. [9]
    Cavallini, D.; Dupre, S.; Scandurra, R.; Graziani, M. T.; Cotta-Ramusino, F.: Metal content of cysteamine oxygenase. Eur. J. Biochem., 4, 209–212 (1968)PubMedCrossRefGoogle Scholar
  10. [10]
    Wood, J.L.; Cavallini, D.: Enzymic oxidation of cysteamine to hypotaurine in the absence of a cofactor. Arch. Biochem. Biophys., 119, 368–372 (1967)PubMedCrossRefGoogle Scholar
  11. [11]
    Cavallini, D.; De Marco, C.; Scandurra, R.; Dupre, S.; Graziani, M.T.: The enzymatic oxidation of cysteamine to hypotaurine. Purification and properties of the enzyme. J. Biol. Chem., 241, 3189–3196 (1966)PubMedGoogle Scholar
  12. [12]
    Kataoka, H.; Ohishi, K.; Imai, J.; Mukai, M.: Distribution of cysteamine oxygenase in animal tissues. Agric. Biol. Chem., 52, 1611–1613 (1988)Google Scholar

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