Literature summary for 1.13.11.19 extracted from

Fernandez, R.L.; Juntunen, N.D.; Fox, B.G.; Brunold, T.C.
Spectroscopic investigation of iron(III) cysteamine dioxygenase in the presence of substrate (analogs) implications for the nature of substrate-bound reaction intermediates (2021), J. Biol. Inorg. Chem., 26, 947-955 .

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Inhibitors

Inhibitors	Comment	Organism	Structure
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	Mus musculus
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	Mus musculus

Organism

Organism	UniProt	Comment	Textmining
Mus musculus	Q6PDY2	-	-

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Release 2023.1 (January 2023)