Literature summary for 1.13.11.19 extracted from

Wang, Y.; Davis, I.; Chan, Y.; Naik, S.G.; Griffith, W.P.; Liu, A.
Characterization of the nonheme iron center of cysteamine dioxygenase and its interaction with substrates (2020), J. Biol. Chem., 295, 11789-11802 .

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Inhibitors

Inhibitors	Comment	Organism	Structure
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	Homo sapiens
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	Mus musculus

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	Q96SZ5	-	-
Mus musculus	Q6PDY2	-	-

General Information

General Information	Comment	Organism
metabolism	in the presence of nitric oxide as a spin probe and oxygen surrogate, both cysteamine and the peptide substrate regulator of G protein signaling 5 coordinate the iron center with their free thiols in a monodentate binding mode. A substrate-bound B-type dinitrosyl iron center complex is observed, as well as a substrate-mediated reduction of the iron center from ferric to the ferrous oxidation state with possible disulfide formation of the substrates	Mus musculus
metabolism	in the presence of nitric oxide as a spin probe and oxygen surrogate, both cysteamine and the peptide substrate regulator of G protein signaling 5 coordinate the iron center with their free thiols in a monodentate binding mode. A substrate-bound B-type dinitrosyl iron center complex is observed, as well as a substrate-mediated reduction of the iron center from ferric to the ferrous oxidation state with possible disulfide formation of the substrates	Homo sapiens

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Release 2023.1 (January 2023)