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
Reaction
Reaction 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.
L-cysteine + O2 = 3-sulfinoalanine
Upon binding substrate, the structure of the iron site is pertubed but is still consistent with six O/N donor, indicating that cysteine may bind to the iron center, but is not bound via the sulfur atom.
-
L-cysteine + O2 = 3-sulfinoalanine
reaction mechanism with internal electron transfer involving the ferric/ferrous enzyme forms, formation of a transient substrate-bound FeIII-superoxo species, overview
-
L-cysteine + O2 = 3-sulfinoalanine
catalytic mechanism of cysteine dioxygenase compared to the mechanism of sulfoxide synthase EgtB, EC 1.14.99.50, and its function of the active-site Tyr377 residue. In the sulfoxide syntase reaction, the conserved tyrosine residue reacts via proton-coupled electron transfer with the iron(III)-superoxo species and creates an iron(III)-hydroperoxo intermediate, thereby preventing the possible thiolate dioxygenation side reaction, detailed overview
L-cysteine + O2 = 3-sulfinoalanine
proposed catalytic cycle of CDO enzymes: the pentacoordinated resting state structure can convert to a hexacoordinated structure by binding of water. Upon binding of molecular oxygen the water molecule is displaced and an iron(III)-superoxo structure is formed. The terminal oxygen atom of the iron(III)-superoxo group attacks the sulfur of the cysteinate group to form a ring-structure, which can homogeneously split into a sulfoxide and iron(IV)-oxo species. The sulfoxide-bound complex rotates from sulfur-bound to oxygen-bound to the iron center. The latter transfers the oxygen atom from the iron(IV)-oxo group to substrate in a final step to form cysteine sulfinic acid product complex
L-cysteine + O2 = 3-sulfinoalanine
reaction mechanism and structure-function analysis
L-cysteine + O2 = 3-sulfinoalanine
reaction mechanism of cysteine oxygenation by CDO enzymes and reactivity of [TpMe,PhFe(CysOEt)] towards O2, detailed quantum mechanics/molecular mechanics calculations, overview
L-cysteine + O2 = 3-sulfinoalanine
reaction mechanism and structure-function analysis
-
-