1.13.11.20: cysteine dioxygenase
This is an abbreviated version!
For detailed information about cysteine dioxygenase, go to the full flat file.
Word Map on EC 1.13.11.20
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1.13.11.20
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taurine
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sulfinic
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non-heme
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hypotaurine
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cysteinesulfinate
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cysteamine
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cystathionine
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3-mercaptopropionate
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cys-tyr
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taut
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adenosyltransferase
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desulfhydration
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2-his-1-carboxylate
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gamma-lyase
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cupins
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2-aminoethanethiol
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medicine
- 1.13.11.20
- taurine
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sulfinic
-
non-heme
- hypotaurine
-
cysteinesulfinate
- cysteamine
- cystathionine
- 3-mercaptopropionate
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cys-tyr
-
taut
-
adenosyltransferase
-
desulfhydration
-
2-his-1-carboxylate
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gamma-lyase
-
cupins
- 2-aminoethanethiol
- medicine
Reaction
Synonyms
3-mercaptopropionate dioxygenase, 3MDO, ADO, Arg-type CDO, BsCDO, CDO, CDO1, CDO2, CdoA, CdoB, cysteine dioxygenase, cysteine dioxygenase type 1, cysteine oxidase, Fe(II) cysteine dioxygenase, H16_A1614, H16_B1863, NP_251292, oxygenase, cysteine di-, PA2602, PCO1, PCO4
ECTree
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Cofactor
Cofactor on EC 1.13.11.20 - cysteine dioxygenase
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NADH
enzyme uses NAD+/NADH as pharmacological chaperone. Presence of 0.1 mM NADH increase activity 1.3fold
Cys-Tyr cofactor
a unique post-translational modification of human CDO consisting of a cross-link between cysteine 93 and tyrosine 157 (Cys-Tyr), which increases catalytic efficiency in a substrate-dependent manner. Production of a Cys-Tyr cofactor-saturated enzyme and analysis of the Cys-Tyr cofactor on kinetic properties, overview. The Cys-Tyr cofactor strongly contributes to efficient iron coordination in the active center of CDO
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additional information
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NAD+ does not appear to be a cofactor, the role of NAD+ in the stimulation of the enzyme is unclear
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additional information
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no requirement of NAD, NADP, NADH or NADPH for the enzymic activity of protein-B. The enzymic activity of protein-B alone is extremely low, protein-A alone does not exhibit catalytic activity, however a significant activity is observed in the presence of both fractions, requirement of protein-A for the catalytic activity of protein-B
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additional information
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NADPH or NADH do not act as cosubstrates, most of added NADPH disappears from the incubation mixture during the first 10 min, while cysteinesulfinic acid remains linear for up to 30 min, the role of NADHP or NADH may be one of stabilization, as allosteric activators or other type of activating agents
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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
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