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
-
sulfinic
-
non-heme
- hypotaurine
-
cysteinesulfinate
- cysteamine
- cystathionine
- 3-mercaptopropionate
-
cys-tyr
-
taut
-
adenosyltransferase
-
desulfhydration
-
2-his-1-carboxylate
-
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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Activating Compound
Activating Compound on EC 1.13.11.20 - cysteine dioxygenase
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cysteine
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protein expression of recombinant wild-type enzyme in HepG2/C3A cells increases by 160% when extracellular cysteine levels are increased from 0 to 1 mM cysteine
ethylxanthate
0.002 mM, 110% of initial activity, 0.004 mM, 89% of initial activity
cysteamine
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at a reaction time of 45 min, CDO activity increases almost 20times in the presence of 5.8 mM cysteamine
L-cysteine
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activates the purified enzyme under anaerobic conditions
L-cysteine
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acts as an initial signal for regulation of the enzyme, upregulates enzyme activity
NADH
enzyme uses NAD+/NADH as pharmacological chaperone. Presence of 0.1 mM NADH increase activity 1.3fold
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cysteine mediates the up-regulation of enzyme in cultured hepatocytes
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additional information
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with pure cysteine dioxygenase no effect of addition of NAD+ to the cysteine diosygenase is found.
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additional information
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effect of dietary protein or cystine on CDO expression and enzyme activity in rat liver and adipose tissue
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additional information
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covalent post-translational modification between the residues C93 and Y157, in close proximity to the active site, enhances the enzyme's activity. The presence of ferrous iron and oxygen is a prerequisite for C93-Y157 crosslink formation. Both the enzymatic rate of cysteine oxidation and the amount of cross-linking between C93 and Y157 increased significantly upon exposure of CDO to air/oxygen and substrate cysteine in the presence of iron in a hitherto unreported two-phase process. The non-crosslinked form has negligible enzymatic activity
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additional information
the enzyme activity is in part modulated by the formation of a Cys93-Tyr157 crosslink that increases its catalytic efficiency over 10fold, mechanism, overview. The crosslink enhances activity by positioning the Tyr157 hydroxyl to enable proper Cys binding, proper oxygen binding, and optimal chemistry
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