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Literature summary extracted from

  • Cavallini, D.; Dupre, S.; Scandurra, R.; Graziani, M.T.; Cotta-Ramusino, F.
    Metal content of cysteamine oxygenase (1968), Eur. J. Biochem., 4, 209-212.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.13.11.19 8-hydroxyquinoline complete inhibition at 7.5 mM Equus caballus
1.13.11.19 alpha,alpha'-dipyridyl slight inhibition Equus caballus
1.13.11.19 diethyldithiocarbamate 70% inhibition at 10 mM Equus caballus
1.13.11.19 KCN 60-70% inhibition at 10 mM Equus caballus
1.13.11.19 Neocuproine 45-55% inhibition at 10 mM Equus caballus
1.13.11.19 o-phenanthroline 45-55% inhibition at 10 mM Equus caballus
1.13.11.19 Salicylaldoxime slight inhibition Equus caballus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.13.11.19 Cu 1 atom of Cu per molecule of enzyme Equus caballus
1.13.11.19 Fe 1 atom of iron per molecule of enzyme Equus caballus
1.13.11.19 Zn 1 atom of zinc per molecule of enzyme Equus caballus

Organism

EC Number Organism UniProt Comment Textmining
1.13.11.19 Equus caballus
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.13.11.19 cysteamine + O2
-
 Equus caballus hypotaurine
-
 ?