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
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non-heme
- hypotaurine
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cysteinesulfinate
- cysteamine
- cystathionine
- 3-mercaptopropionate
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cys-tyr
-
taut
-
adenosyltransferase
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desulfhydration
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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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Substrates Products
Substrates Products on EC 1.13.11.20 - cysteine dioxygenase
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REACTION DIAGRAM
beta-mercaptoethanol + O2
2-hydroxyethanesulfinate
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slight activity
-
?
H2N-CGGAIISDFI-COOH + O2
H2N-(sulfino-Cys)-GGAIISDFI-COOH + H2N-(sulfono-Cys)-GGAIISDFI-COOH
synthetic 10-mer peptide corresponding to the methionine excised N termini of the ERF-VIIs RAP2.2, RAP2.12 and HRE2
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-
?
N-terminal Cys of RGS4 + O2
N-terminal Cys-sulfinic acid of RGS4
i.e. regulator of G-protein signalling
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-
?
N-terminal Cys of RGS5 + O2
N-terminal Cys-sulfinic acid of RGS5
i.e. regulator of G-protein signalling
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-
?
3-sulfinopropanoate + H+
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reaction of EC 1.13.11.91
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-
?
3-mercaptopropanoate + O2
3-sulfinopropanoate + H+
reaction of EC 1.13.11.91
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-
?
3-mercaptopropanoate + O2
3-sulfinopropanoate + H+
reaction of EC 1.13.11.91
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-
?
3-mercaptopropanoate + O2
3-sulfinopropanoate + H+
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
reaction of EC 1.13.11.91
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-
?
3-mercaptopropanoate + O2
3-sulfinopropanoate + H+
reaction of EC 1.13.11.91
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-
?
3-mercaptopropanoate + O2
3-sulfinopropanoate + H+
-
reaction of EC 1.13.11.91
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-
?
3-mercaptopropanoate + O2
3-sulfinopropanoate + H+
reaction of EC 1.13.11.91
-
-
?
3-sulfinopropionate
3fold higher activity compared to L-cysteine. 3-Mercaptopropionate does not occur naturally in cells of strain H16
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-
?
3-mercaptopropionate + O2
3-sulfinopropionate
3fold higher activity compared to L-cysteine. 3-Mercaptopropionate does not occur naturally in cells of strain H16
-
-
?
3-mercaptopropionate + O2
3-sulfinopropionate
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
3fold higher activity compared to L-cysteine. 3-Mercaptopropionate does not occur naturally in cells of strain H16
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-
?
L-cysteine + O2
3-sulfino-L-alanine
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highly specific for L-cysteine
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?
L-cysteine + O2
3-sulfino-L-alanine
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probable role in the mycelial to yeast phase transition
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?
L-cysteine + O2
3-sulfino-L-alanine
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key enzyme in sulfate production, involved in the production of sulfate for the maintenance of a metabolic barrier against the entry of airborne xenobiotics and protein synthesis
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-
?
L-cysteine + O2
3-sulfino-L-alanine
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-
-
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?
L-cysteine + O2
3-sulfino-L-alanine
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highly specific for L-cysteine
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?
L-cysteine + O2
3-sulfino-L-alanine
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highly specific for L-cysteine
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?
L-cysteine + O2
3-sulfino-L-alanine
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key enzyme of cysteine metabolism
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?
L-cysteine + O2
3-sulfino-L-alanine
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key enzyme of cysteine metabolism
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?
L-cysteine + O2
3-sulfino-L-alanine
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liver enzyme responds to dietary protein contents, role in regulation of intracellular levels of methionine, cysteine and glutathione
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?
L-cysteine + O2
3-sulfino-L-alanine
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enzyme expression in the brain may have several possible functions, like the prevention of free radical production by the autooxidation of cysteine and dopamine
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?
L-cysteine + O2
3-sulfino-L-alanine
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key enzyme in sulfate production, critical regulator of cellular cysteine concentration and availability of cysteine for anabolic processes
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-
?
L-cysteine + O2
3-sulfino-L-alanine
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key enzyme of cysteine catabolism, supplies substrate for taurine biosynthesis
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-
?
L-cysteine + O2
3-sulfino-L-alanine
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key enzyme of taurine biosynthesis, provides substrate for transamination, regulation of intracellular cysteine level
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-
?
L-cysteine + O2
3-sulfino-L-alanine
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regulation of intracellular cysteine concentration
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-
?
L-cysteine + O2
3-sulfinoalanine
structure of the sulfinato complex, overview
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-
?
L-cysteine + O2
3-sulfinoalanine
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-
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?
L-cysteine + O2
3-sulfinoalanine
anaerobic CDO reaction conditions
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-
?
L-cysteine + O2
3-sulfinoalanine
enzyme CDO-L-cysteine complex structure analysis and modeling, O2 binding structure, QM-MM simulations, detailed overview
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?
?
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enzyme exhibits a specificity for 3-mercaptopropanoate nearly 2 orders of magnitude greater than those for cysteine
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additional information
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no activity with 3-mercaptopropionate by CdoB
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?
additional information
?
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no activity with 3-mercaptopropionate by CdoB
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?
additional information
?
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3-mercaptopropanoate is preferred over cysteine. No substrate: cysteamine
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additional information
?
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3-mercaptopropanoate is preferred over cysteine. No substrate: cysteamine
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additional information
?
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3-mercaptopropanoate is preferred over cysteine. No substrate: cysteamine
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additional information
?
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Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
3-mercaptopropanoate is preferred over cysteine. No substrate: cysteamine
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-
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additional information
?
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Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
3-mercaptopropanoate is preferred over cysteine. No substrate: cysteamine
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-
-
additional information
?
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Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
no activity with 3-mercaptopropionate by CdoB
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-
?
additional information
?
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Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
no activity with 3-mercaptopropionate by CdoB
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-
?
additional information
?
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D-cysteine, cystine, taurine, cystamine, cysteinesulfinic acid, glutathione, cysteic acid, S-methylcysteine and pyruvic acid do not serve as substrates
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?
additional information
?
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prediction of a h2-O,O-binding mode for synthetic as well as the natural enzyme, modeling of the cysteine sulfinic product complex in the active site
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?
additional information
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enzyme is able to cleave C-F bonds. The oxidants produced at the center of the non-heme ferrite effectively oxidize adjacent coordination residues and oxidize C-Cl and even C-F bonds during the formation of dihalogen-substituted cofactors, via four elementary steps: H-abstraction, C-S bond formation, F-transfer, and C-F bond cleavage. C-F bond cleavage is the rate-determining step with an energy barrier of 18.8 kcal/mol
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additional information
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cysteine dioxygenase and methionine sulfoxide reductase are working in coordination to balance cellular antioxidant level
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?
additional information
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CDO cannot catalyze the oxidation of selenocysteine
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?
additional information
?
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CDO exhibits high specificity for L-cysteine, displaying little or no reactivity with D-cysteine, glutathione, L-cystine, or cysteamine
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?
additional information
?
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recombinant 3MDO is able to oxidize both cysteine and 3-mercaptopropionic acid in vitro, with a marked preference for 3-mercaptopropionic acid. Substrate binding to the ferrous iron is through the thiol but each substrate may adopt different coordination geometries
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additional information
?
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recombinant 3MDO is able to oxidize both cysteine and 3-mercaptopropionic acid in vitro, with a marked preference for 3-mercaptopropionic acid. Substrate binding to the ferrous iron is through the thiol but each substrate may adopt different coordination geometries
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additional information
?
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recombinant 3MDO is able to oxidize both cysteine and 3-mercaptopropionic acid in vitro, with a marked preference for 3-mercaptopropionic acid. Substrate binding to the ferrous iron is through the thiol but each substrate may adopt different coordination geometries
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additional information
?
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glutathione, dithiothreitol and cystine do not serve as substrates
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-
?
additional information
?
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L-cystine, D-cysteine, DL-homocysteine and cysteamine do not serve as substrates
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-
?
additional information
?
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L-cystine, D-cysteine, carboxymethyl-L-cysteine, carboxyethyl-L-cysteine, S-methyl-L-cysteine, N-acetyl-L-cysteine, DL-homocysteine and cysteamine do not serve as substrates
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-
?
additional information
?
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cysteamine does not serve as substrate, D-cysteine does not serve as substrate
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?
additional information
?
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cysteine catabolism in mammals is dependent upon cysteine dioxygenase. System for regulation of cellular cysteine levels. Evidence of abnormal or deficient CDO activity has been reported in individuals with a variety of autoimmune and neurodegenerative diseases, including rheumatoid arthritis, Parkinsons disease, Alzheimers disease, and motor neuron diseases
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?
additional information
?
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cysteine dioxygenase cannot catalyze the oxidation of selenocysteine. In the Cys-bound complexes, the change of the oxidation state for the Fe center is II to III to II, while the Fe center in the Sec-bound complexes remains in the II oxidation state throughout. The competition for donation of electron density with the iron ion determines the valence change and the reaction ability
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?
additional information
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formation of an active CDO:cysteine substrate complex
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?
additional information
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homocysteine and D-Cys are no substrates
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?