Literature summary for 1.13.11.19 extracted from

Fernandez, R.L.; Elmendorf, L.D.; Smith, R.W.; Bingman, C.A.; Fox, B.G.; Brunold, T.C.
The crystal structure of cysteamine dioxygenase reveals the origin of the large substrate scope of this vital mammalian enzyme (2021), Biochemistry, 60, 3728-3737 .

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Crystallization (Commentary)

Crystallization (Comment)	Organism
structure of cysteamine dioxygenase at 1.9 A resolution, an Fe and three-histidine (3-His) active site is situated at the end of a wide substrate access channel. Whole-protein models of ADO in complex with either cysteamine or an N-terminal-Cys peptide suggest occlusion of access to the active site by peptide substrate binding. A small tunnel that leads from the opposite face of the enzyme into the active site provides a path through which co-substrate O2 can access the Fe center. The entrance to the tunnel is guarded by two Cys residues that may form a disulfide bond to regulate O2 delivery	Mus musculus

Crystallization (Comment)

Organism

structure of cysteamine dioxygenase at 1.9 A resolution, an Fe and three-histidine (3-His) active site is situated at the end of a wide substrate access channel. Whole-protein models of ADO in complex with either cysteamine or an N-terminal-Cys peptide suggest occlusion of access to the active site by peptide substrate binding. A small tunnel that leads from the opposite face of the enzyme into the active site provides a path through which co-substrate O2 can access the Fe center. The entrance to the tunnel is guarded by two Cys residues that may form a disulfide bond to regulate O2 delivery

Mus musculus

Inhibitors

Inhibitors	Comment	Organism	Structure
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	Mus musculus

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Iron	formation of an inner-sphere complex between FeIII-ADO and 2-aminoethanol. Binding occurs via a 3-His triad	Mus musculus

Organism

Organism	UniProt	Comment	Textmining
Mus musculus	Q6PDY2	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
2-aminoethanethiol + O2	-	Mus musculus	hypotaurine	-	?
3-mercaptopropionic acid + O2	-	Mus musculus	3-sulfinopropionic acid	-	?

Synonyms

Synonyms	Comment	Organism
2-aminoethanethiol dioxygenase	-	Mus musculus

General Information

General Information	Comment	Organism
metabolism	substrates 2-aminoethanol and 3-mercaptopropionic acid bind to ADO in the same manner, potentially in a monodentate fashion through the terminal thiolate. The high-spin ferric species exhibit a more axial zero-field splitting relative to that reported for Cys-bound FeIIICDO	Mus musculus