Literature summary 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.
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
1.13.11.20 |
expression in Escherichia coli and HepG2/C3A cell |
Rattus norvegicus |
Localization
EC Number |
Localization |
Comment |
Organism |
GeneOntology No. |
Textmining |
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Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
1.13.11.20 |
Rattus norvegicus |
P21816 |
- |
- |
Cofactor
EC Number |
Cofactor |
Comment |
Organism |
Structure |
---|
1.13.11.20 |
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 |
|