Literature summary for 1.13.11.20 extracted from

Dominy, J.E.; Hwang, J.; Guo, S.; Hirschberger, L.L.; Zhang, S.; Stipanuk, M.H.
Synthesis of amino acid cofactor in cysteine dioxygenase is regulated by substrate and represents a novel post-translational regulation of activity (2008), J. Biol. Chem., 283, 12188-12201.

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Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli and HepG2/C3A cell	Rattus norvegicus

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining

Organism

Organism	UniProt	Comment	Textmining
Rattus norvegicus	P21816	-	-

Cofactor

Cofactor	Comment	Organism	Structure
additional information	enzyme uses an amino acid cofactor in the active site consisting of two cross-linked residues, cysteine 93 and tyrosine 157. Formation of the Cys-Tyr cofactor requires a transition metal cofactor Fe2+ and O2. Biogenesis of the cofactor is also strictly dependent upon the presence of substrate. In the absence of the Cys-Tyr cofactor, the enzyme possesses appreciable catalytic activity. At physiologically relevant cysteine concentrations, cofactor formation increases catalytic efficiency 10-fold	Rattus norvegicus

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Release 2023.1 (January 2023)