1.13.11.19: cysteamine dioxygenase
This is an abbreviated version!
For detailed information about cysteamine dioxygenase, go to the full flat file.
Word Map on EC 1.13.11.19
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1.13.11.19
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hypotaurine
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sulfinic
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3-mercaptopropionate
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dioxygenation
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nonheme
- 1.13.11.19
- hypotaurine
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sulfinic
- 3-mercaptopropionate
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dioxygenation
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nonheme
Reaction
Synonyms
2-aminoethanethiol dioxygenase, ADO, CDO, cysteamine oxygenase, Gm237, oxygenase, cysteamine, oxygenase, cysteamine di-, persulfurase
ECTree
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Inhibitors
Inhibitors on EC 1.13.11.19 - cysteamine dioxygenase
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2-mercaptoethanol
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inhibition at high concentration, activation at low concentration
azide
Fe(III)ADO incubated with azide displays a rhombic, high-spin (S = 5/2) EPR signal that closely resembles that of purified ADO. Azide may bind to the Fe(III)ADO active site by replacing a ligand with comparable donor strength, likely a solvent-derived hydroxide. Azide is unable to coordinate to cysteamine-bound Fe(III)ADO
cyanide
cyanide binds to either cysteamine- or Cys-bound Fe(III)ADO, binding causes the appearance of a dominant low-spin (S = 1/2) EPR signal and a small but noticeable change to the electronic absorption spectrum
S
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sulfide, elemental sulfur, elemental selenium or hydroxylamine required in catalytic amount, inhibition when added over a critical concentration (with the exception of hydroxylamine)
Se
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sulfide, elemental sulfur, elemental selenium or hydroxylamine required in catalytic amount, inhibition when added over a critical concentration (with the exception of hydroxylamine)
Sulfide
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sulfide, elemental sulfur, elemental selenium or hydroxylamine required in catalytic amount, inhibition when added over a critical concentration (with the exception of hydroxylamine)
cysteine
weak competitive inhibitor, Cys can bind directly to the ADO iron center with formation of a low-spin (S=1/2) FeIII complex. The ratio of low-spin to high-spin ferric species can be modulated by the addition of glycerol, with the high-spin Cys-FeIII-ADO complex being the predominant form in the absence of a glassing agent
substrate cysteamine is capable of reducing the catalytically inactive ferric center to the enzymatically active ferrous state. Presence of cysteamine alters the binding behavior of nitric oxide to the nonheme iron center of ADO
Iron
substrate cysteamine is capable of reducing the catalytically inactive ferric center to the enzymatically active ferrous state. Presence of cysteamine alters the binding behavior of nitric oxide to the nonheme iron center of ADO