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
-
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
- 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
Advanced search results
Posttranslational Modification
Posttranslational Modification on EC 1.13.11.20 - cysteine dioxygenase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
no modification
additional information
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
additional information
-
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
additional information
the residues Tyr-157 and Cys-93 appear to be covalently linked between Tyr-157 CE and Cys-93 SG, because these two atoms lie within 2.2 A
additional information
-
the residues Tyr-157 and Cys-93 appear to be covalently linked between Tyr-157 CE and Cys-93 SG, because these two atoms lie within 2.2 A
additional information
Cys93-Sgamma is covalently bound to Tyr157-Cepsilon2 forming a cysteinyl-tyronsine linkage.
additional information
-
two posttranslational modifications adjacent to the catalytic iron center: a thioether cross-link between Cys93 and Tyr157 and extra electron density at Cys164 which is variously explained as cystine or cysteine sulfinic acid
additional information
residues C93-Y157 crosslink as a result of a posttranslational modification
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