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3-mercaptopropanoate + O2
3-sulfinopropanoate + H+
3-mercaptopropionate + O2
3-sulfinopropanoate
-
-
-
-
?
3-mercaptopropionate + O2
3-sulfinopropionate
beta-mercaptoethanol + O2
2-hydroxyethanesulfinate
-
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
-
-
?
L-cysteine + O2
3-sulfino-L-alanine
L-cysteine + O2
3-sulfinoalanine
N-terminal Cys of RGS4 + O2
N-terminal Cys-sulfinic acid of RGS4
i.e. regulator of G-protein signalling
-
-
?
N-terminal Cys of RGS5 + O2
N-terminal Cys-sulfinic acid of RGS5
i.e. regulator of G-protein signalling
-
-
?
S-carboxymethyl-L-cysteine + O2
?
-
-
-
?
additional information
?
-
3-mercaptopropanoate + O2
3-sulfinopropanoate + H+
-
reaction of EC 1.13.11.91
-
-
?
3-mercaptopropanoate + O2
3-sulfinopropanoate + H+
reaction of EC 1.13.11.91
-
-
?
3-mercaptopropanoate + O2
3-sulfinopropanoate + H+
reaction of EC 1.13.11.91
-
-
?
3-mercaptopropanoate + O2
3-sulfinopropanoate + H+
reaction of EC 1.13.11.91
-
-
?
3-mercaptopropanoate + O2
3-sulfinopropanoate + H+
reaction of EC 1.13.11.91
-
-
?
3-mercaptopropanoate + O2
3-sulfinopropanoate + H+
-
reaction of EC 1.13.11.91
-
-
?
3-mercaptopropanoate + O2
3-sulfinopropanoate + H+
reaction of EC 1.13.11.91
-
-
?
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
3fold higher activity compared to L-cysteine. 3-Mercaptopropionate does not occur naturally in cells of strain H16
-
-
?
3-mercaptopropionate + O2
3-sulfinopropionate
3fold higher activity compared to L-cysteine. 3-Mercaptopropionate does not occur naturally in cells of strain H16
-
-
?
cysteamine + O2
?
-
-
-
-
?
cysteamine + O2
?
-
-
-
-
?
L-cysteine + O2
3-sulfino-L-alanine
-
-
-
?
L-cysteine + O2
3-sulfino-L-alanine
-
-
-
?
L-cysteine + O2
3-sulfino-L-alanine
-
-
-
?
L-cysteine + O2
3-sulfino-L-alanine
-
-
-
?
L-cysteine + O2
3-sulfino-L-alanine
-
-
-
?
L-cysteine + O2
3-sulfino-L-alanine
-
highly specific for L-cysteine
-
?
L-cysteine + O2
3-sulfino-L-alanine
-
probable role in the mycelial to yeast phase transition
-
?
L-cysteine + O2
3-sulfino-L-alanine
-
-
-
?
L-cysteine + O2
3-sulfino-L-alanine
-
-
-
-
?
L-cysteine + O2
3-sulfino-L-alanine
-
-
-
?
L-cysteine + O2
3-sulfino-L-alanine
-
-
-
-
?
L-cysteine + O2
3-sulfino-L-alanine
-
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
-
-
?
L-cysteine + O2
3-sulfino-L-alanine
-
key enzyme of taurine biosynthesis
-
-
?
L-cysteine + O2
3-sulfino-L-alanine
-
-
-
-
?
L-cysteine + O2
3-sulfino-L-alanine
-
-
-
?
L-cysteine + O2
3-sulfino-L-alanine
-
-
-
?
L-cysteine + O2
3-sulfino-L-alanine
-
-
-
?
L-cysteine + O2
3-sulfino-L-alanine
-
-
-
?
L-cysteine + O2
3-sulfino-L-alanine
-
-
-
?
L-cysteine + O2
3-sulfino-L-alanine
-
-
-
?
L-cysteine + O2
3-sulfino-L-alanine
-
-
-
?
L-cysteine + O2
3-sulfino-L-alanine
-
-
-
?
L-cysteine + O2
3-sulfino-L-alanine
-
-
-
?
L-cysteine + O2
3-sulfino-L-alanine
-
-
-
?
L-cysteine + O2
3-sulfino-L-alanine
-
-
-
?
L-cysteine + O2
3-sulfino-L-alanine
-
-
-
?
L-cysteine + O2
3-sulfino-L-alanine
-
-
-
?
L-cysteine + O2
3-sulfino-L-alanine
-
-
-
-
?
L-cysteine + O2
3-sulfino-L-alanine
-
-
-
?
L-cysteine + O2
3-sulfino-L-alanine
-
highly specific for L-cysteine
-
?
L-cysteine + O2
3-sulfino-L-alanine
-
highly specific for L-cysteine
-
?
L-cysteine + O2
3-sulfino-L-alanine
-
key enzyme of cysteine metabolism
-
?
L-cysteine + O2
3-sulfino-L-alanine
-
key enzyme of cysteine metabolism
-
?
L-cysteine + O2
3-sulfino-L-alanine
-
liver enzyme responds to dietary protein contents, role in regulation of intracellular levels of methionine, cysteine and glutathione
-
?
L-cysteine + O2
3-sulfino-L-alanine
-
enzyme expression in the brain may have several possible functions, like the prevention of free radical production by the autooxidation of cysteine and dopamine
-
?
L-cysteine + O2
3-sulfino-L-alanine
-
key enzyme in sulfate production, critical regulator of cellular cysteine concentration and availability of cysteine for anabolic processes
-
-
?
L-cysteine + O2
3-sulfino-L-alanine
-
key enzyme of cysteine catabolism, supplies substrate for taurine biosynthesis
-
-
?
L-cysteine + O2
3-sulfino-L-alanine
-
key enzyme of taurine biosynthesis, provides substrate for transamination, regulation of intracellular cysteine level
-
-
?
L-cysteine + O2
3-sulfino-L-alanine
-
regulation of intracellular cysteine concentration
-
-
?
L-cysteine + O2
3-sulfino-L-alanine
-
-
-
?
L-cysteine + O2
3-sulfino-L-alanine
-
-
-
?
L-cysteine + O2
3-sulfino-L-alanine
-
-
-
?
L-cysteine + O2
3-sulfino-L-alanine
-
-
-
?
L-cysteine + O2
3-sulfino-L-alanine
-
-
-
?
L-cysteine + O2
3-sulfino-L-alanine
-
-
-
-
?
L-cysteine + O2
3-sulfinoalanine
-
-
-
-
?
L-cysteine + O2
3-sulfinoalanine
-
-
-
-
?
L-cysteine + O2
3-sulfinoalanine
-
-
-
?
L-cysteine + O2
3-sulfinoalanine
-
-
-
?
L-cysteine + O2
3-sulfinoalanine
-
-
-
-
?
L-cysteine + O2
3-sulfinoalanine
-
-
-
?
L-cysteine + O2
3-sulfinoalanine
-
-
-
?
L-cysteine + O2
3-sulfinoalanine
-
-
-
?
L-cysteine + O2
3-sulfinoalanine
-
-
-
-
?
L-cysteine + O2
3-sulfinoalanine
-
-
-
-
?
L-cysteine + O2
3-sulfinoalanine
-
-
-
?
L-cysteine + O2
3-sulfinoalanine
structure of the sulfinato complex, overview
-
-
?
L-cysteine + O2
3-sulfinoalanine
-
-
-
-
?
L-cysteine + O2
3-sulfinoalanine
-
-
-
-
?
L-cysteine + O2
3-sulfinoalanine
-
-
-
?
L-cysteine + O2
3-sulfinoalanine
-
-
-
-
?
L-cysteine + O2
3-sulfinoalanine
-
-
-
?
L-cysteine + O2
3-sulfinoalanine
-
-
-
-
?
L-cysteine + O2
3-sulfinoalanine
-
-
-
?
L-cysteine + O2
3-sulfinoalanine
anaerobic CDO reaction conditions
-
-
?
L-cysteine + O2
3-sulfinoalanine
enzyme CDO-L-cysteine complex structure analysis and modeling, O2 binding structure, QM-MM simulations, detailed overview
-
-
?
L-cysteine + O2
3-sulfinoalanine
-
-
-
-
?
L-cysteine + O2
3-sulfinoalanine
-
-
-
-
?
L-cysteine + O2
3-sulfinoalanine
-
-
-
-
?
additional information
?
-
-
enzyme exhibits a specificity for 3-mercaptopropanoate nearly 2 orders of magnitude greater than those for cysteine
-
-
-
additional information
?
-
no activity with 3-mercaptopropionate by CdoB
-
-
?
additional information
?
-
no activity with 3-mercaptopropionate by CdoB
-
-
?
additional information
?
-
3-mercaptopropanoate is preferred over cysteine. No substrate: cysteamine
-
-
-
additional information
?
-
3-mercaptopropanoate is preferred over cysteine. No substrate: cysteamine
-
-
-
additional information
?
-
3-mercaptopropanoate is preferred over cysteine. No substrate: cysteamine
-
-
-
additional information
?
-
3-mercaptopropanoate is preferred over cysteine. No substrate: cysteamine
-
-
-
additional information
?
-
3-mercaptopropanoate is preferred over cysteine. No substrate: cysteamine
-
-
-
additional information
?
-
no activity with 3-mercaptopropionate by CdoB
-
-
?
additional information
?
-
no activity with 3-mercaptopropionate by CdoB
-
-
?
additional information
?
-
-
D-cysteine, cystine, taurine, cystamine, cysteinesulfinic acid, glutathione, cysteic acid, S-methylcysteine and pyruvic acid do not serve as substrates
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
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
-
-
-
additional information
?
-
-
cysteine dioxygenase and methionine sulfoxide reductase are working in coordination to balance cellular antioxidant level
-
-
?
additional information
?
-
-
CDO cannot catalyze the oxidation of selenocysteine
-
-
?
additional information
?
-
-
CDO exhibits high specificity for L-cysteine, displaying little or no reactivity with D-cysteine, glutathione, L-cystine, or cysteamine
-
-
?
additional information
?
-
-
no activity with selenocysteine
-
-
?
additional information
?
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
-
glutathione, dithiothreitol and cystine do not serve as substrates
-
-
?
additional information
?
-
-
L-cystine, D-cysteine, DL-homocysteine and cysteamine do not serve as substrates
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
cysteamine does not serve as substrate, D-cysteine does not serve as substrate
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
formation of an active CDO:cysteine substrate complex
-
-
?
additional information
?
-
homocysteine and D-Cys are no substrates
-
-
?
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3,3'-thiodipropionic acid
-
-
3-Mercaptopropionate
complete inhibition at 0.05 mM
3-Mercaptopropionic acid
-
-
3-sulfanyl-propionic acid
3-sulfinopropionic acid
-
-
alpha-ketoglutarate
-
alpha-ketoglutarate inhibits cysteine dioxygenase with 50% inhibition at 6.8 mM
aspartic acid
-
aspartic acid decreases enzyme activity to 50% at a concentration of 1.5 mM. Replacing the sulfydryl by the uncharged hydroxyl group of serine does not affect enzyme activity.
bathophenanthroline sulfonate
Carboxyethyl-L-cysteine
-
53% inhibition at 1 mM
carboxymethyl-L-cysteine
-
37% inhibition at 1 mM
CdCl2
-
cells transfected with wild-type enzyme show an enhanced sensitivity to CdCl2 that is limited to cells cultured in medium with cysteine levels of 0.1 and 0.3mM
Cu2+
-
90% inhibition at 0.01 mM, 100% inhibition at 0.1 mM
cyanide
-
inhibits with a 50% activity reduction at 2.7 mM
cystine
-
42% inhibition at 5 mM
cytokine tumor necrosis factor-alpha
-
also TNF-alpha, down-regulation observed in hepatic and brain cells
-
D-Cys
competitive inhibitor, binding structure, overview
D-cysteinesulfinate
-
34.4% inhibition in hepatocytes from rats fed a low casein diet, 71.8% inhibition in hepatocytes from rats fed a moderate casein diet, 64.4% inhibition in hepatocytes from rats fed a high casein diet
DL-homocystine
-
47% inhibition at 5 mM
ethyl xanthate
44% inhibition at 0.004 mM
ethylxanthate
0.002 mM, 110% of initial activity, 0.004 mM, 89% of initial activity
L-cysteine
-
concentrations of cysteine of 2 mM and above are inhibitory in assays of purified cysteine dioxygenase
Mercaptopropionic acid
-
mercaptopropionic acid at a concentration of 1.2 mM inhibits cysteine dioxygenase activity by 50%
N-acetyl-L-cysteine
-
35% inhibition at 10 mM
Neocuproine
-
with protein-A: 18% inhibition at 0.1 mM, without protein-A: slight activation at 0.1 mM
S-carboxymethylcysteine
-
S-carboxymethylcysteine exhibits 50% inhibition at a concentration of 2.3 mM
S-methyl-L-cysteine
-
34% inhibition at 1 mM
sodium ethylxanthate
11% inhibition at 0.004 mM
thiosulfate
competitive inhibitor, binding structure, overview
transforming growth factor-beta
-
also TGF-beta, down-regulation observed in hepatic and brain cells
-
2,2'-dipyridyl
-
92% inhibition at 0.1 mM
2,2'-dipyridyl
-
non preincubated protein-B: 76% inhibition at 1 mM, with cysteine preincubated protein-B: no inhibition
2,2'-dipyridyl
-
with protein-A: 100% inhibition at 0.1 mM, without protein-A: 58% inhibition at 0.1 mM
2-amino-ethanethiol
1 x the Km for cysteine = -2.5% inhibition, 10 x the Km for cysteine = 20% inhibition
2-amino-ethanethiol
YubC: 1 x the Km for cysteine = 12% inhibition, 10 x the Km for cysteine = 19% inhibition
2-amino-ethanethiol
1 x the Km for cysteine = 8.7% inhibition, 10 x the Km for cysteine = 30% inhibition
2-amino-ethanethiol
SCO3035: 1 x the Km for cysteine = 7.5% inhibition, 10 x the Km for cysteine = 27% inhibition; SCO5772: 1 x the Km for cysteine = 0.9% inhibition, 10 x the Km for cysteine = 28% inhibition
2-sulfanyl-ethanol
1 x the Km for cysteine = 4.8% inhibition, 10 x the Km for cysteine = 11% inhibition
2-sulfanyl-ethanol
YubC: 1 x the Km for cysteine = -0.7% inhibition, 10 x the Km for cysteine = 6.6% inhibition
2-sulfanyl-ethanol
1 x the Km for cysteine = 5.9% inhibition, 10 x the Km for cysteine = 13% inhibition
2-sulfanyl-ethanol
SCO3035: 1 x the Km for cysteine = 8.6% inhibition, 10 x the Km for cysteine = 15% inhibition; SCO5772: 1 x the Km for cysteine = 2.6% inhibition, 10 x the Km for cysteine = 13% inhibition
3-sulfanyl-propionic acid
1 x the Km for cysteine = 3.2% inhibition, 10 x the Km for cysteine = 12% inhibition
3-sulfanyl-propionic acid
YubC: 1 x the Km for cysteine = 4.7% inhibition, 10 x the Km for cysteine = 11% inhibition
3-sulfanyl-propionic acid
1 x the Km for cysteine = 4.9% inhibition, 10 x the Km for cysteine = 26% inhibition
3-sulfanyl-propionic acid
SCO3035: 1 x the Km for cysteine = 2.9% inhibition, 10 x the Km for cysteine = 11% inhibition; SCO5772: 1 x the Km for cysteine = 5.6% inhibition, 10 x the Km for cysteine = 16% inhibition
8-hydroxyquinoline
-
59% inhibition at 0.1 mM
8-hydroxyquinoline
-
with protein-A: 100% inhibition at 0.1 mM, without protein-A: 99% inhibition at 0.1 mM
azide
-
inhibits with a 50% activity reduction at 1.4 mM
azide
competitive inhibitor, binding structure, overview. Azide does not bind in the enzyme crystal as a superoxide mimic
Bathocuproine sulfonate
-
80% inhibition at 0.01 mM, 83% inhibition at 0.1 mM
Bathocuproine sulfonate
-
with protein-A: 5% inhibition at 0.1 mM, without protein-A: 38% inhibition at 0.1 mM
bathophenanthroline sulfonate
-
68% inhibition at 0.01 mM, 100% inhibition at 0.1 mM
bathophenanthroline sulfonate
-
with protein-A: 88% inhibition, without protein-A: 100% inhibition
cysteamine
-
cysteamine
-
39% inhibition at 10 mM
D-cysteine
-
inhibition at 1 mM
D-cysteine
-
20% inhibition at 10 mM
D-cysteine
-
47% inhibition at 1 mM
diethyldithiocarbamate
-
no significant inhibition
diethyldithiocarbamate
-
with protein-A: not inhibitory at 0.1 mM
DL-homocysteine
-
-
DL-homocysteine
-
47% inhibition at 10 mM
DL-homocysteine
-
87% inhibition at 10 mM
DL-propargylglycine
-
45.5% inhibition in hepatocytes from rats fed a high casein diet
DL-propargylglycine
-
reduces the enzyme activity in methionine-supplemented medium to the basal level, does not reduce the enzyme activity in cysteine-supplemented medium, no effect in hepatocytes cultured in basal medium
EDTA
0.05 mM, 80% of initial activity, 0.1 mM, 61% of initial activity; 40% inhibition at 0.1 mM, 65% inhibition at 0.2 mM; complete inhibition at 0.05 mM
EDTA
-
totally inhibits at very low concentrations
EDTA
an EDTA:cysteine dioxygenase molar ratio of about 1000:1 abolish`s cysteine oxidase activity
EDTA
enzyme activity is completely abolished at EDTA concentrations above 0.5 mM
EDTA
higher kcat and lower Km value, when the enzyme is expressed in medium containing extra iron and purified in buffers lacking EDTA.
EDTA
-
59% inhibition at 0.01 mM, 100% inhibition at 0.1 mM
EDTA
-
non preincubated protein-B: 91% inhibition at 1 mM, with cysteine preincubated protein-B: 51% inhibition at 1 mM
EDTA
-
with protein-A: 97% inhibition at 0.1 mM, with protein-A: 99% inhibition at 0.1 mM
EGTA
-
totally inhibits at very low concentrations
EGTA
-
with protein-A: 100% inhibition at 0.1 mM, without protein-A: 95% inhibition at 0.1 mM
Fe2+
-
50% inhibition at 0.01 mM, 100% inhibition at 0.1 mM
Fe2+
-
inhibits the enzyme activity of both preactivated and non-preactivated protein-B
homocysteine
cysteine dioxygenase activity is reduced by 50% only when the molar ratio of homocysteine:cysteine dioxygenase reach about 30000:1
homocysteine
-
50% inhibition at 6.5 mM
homocysteine
competitive inhibitor, binding structure, overview
o-phenanthroline
-
totally inhibits at very low concentrations
o-phenanthroline
-
13% inhibition at 0.01 mM, 88% inhibition at 0.1 mM
o-phenanthroline
-
non-preincubated protein-B: 91% inhibition at 1 mM, with cysteine preincubated protein-B: 67% inhibition at 1 mM
o-phenanthroline
-
without protein-A: 96% inhibition at 0.1 mM, with protein A: 100% inhibition at 0.1 mM
additional information
metal ions are inhibitory above 0.2 mM
-
additional information
metal ions are inhibitory above 0.2 mM
-
additional information
not inhibitory: S-carboxymethyl-L-cysteine
-
additional information
-
not inhibitory: S-carboxymethyl-L-cysteine
-
additional information
-
iodoacetamide has no effect on the enzyme activity; S-methylcysteine does not inhibit cysteine dioxygenase
-
additional information
-
inhibitors of the 26S proteasome (e.g., proteasome inhibitor 1 and lactacystin) block CDO degradation in cysteine-deficient cells but had little or no effect on CDO concentration in hepatocytes cultured with excess cysteine
-
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evolution
-
the enzyme belongs to the 2-His-1-carboxylate family of non-heme iron containing oxidases and oxygenases
evolution
analysis of examples for two structural genomics groups of CDOs: a Bacillus subtilis Arg-type enzyme that has cysteine dioxygenase activity (BsCDO), and a Ralstonia eutropha Gln-type CDO homologue of uncharacterized activity (ReCDOhom), overview. The BsCDO active site is well conserved with mammalian CDO, and a cysteine complex captured in the active site confirms that the cysteine binding mode is also similar. The Arg position is not compatible with the mode of Cys binding seen in both Rattus norvegicus CDO and Bacillus subtilis CDO. Gln-type CDO homologues are not authentic CDOs but have substrate specificity more similar to 3-mercaptopropionate dioxygenases
evolution
structure and catalytic mechanism comparisons of nonheme iron enzymes cysteine dioxygenase with sulfoxide synthase EgtB, EC 1.14.99.50, quantum mechanics/molecular mechanics calculations, overview
evolution
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analysis of examples for two structural genomics groups of CDOs: a Bacillus subtilis Arg-type enzyme that has cysteine dioxygenase activity (BsCDO), and a Ralstonia eutropha Gln-type CDO homologue of uncharacterized activity (ReCDOhom), overview. The BsCDO active site is well conserved with mammalian CDO, and a cysteine complex captured in the active site confirms that the cysteine binding mode is also similar. The Arg position is not compatible with the mode of Cys binding seen in both Rattus norvegicus CDO and Bacillus subtilis CDO. Gln-type CDO homologues are not authentic CDOs but have substrate specificity more similar to 3-mercaptopropionate dioxygenases
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malfunction
deletion of cdoA might enable increased synthesis of polythioesters
malfunction
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deletion of cdoA might enable increased synthesis of polythioesters
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malfunction
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deletion of cdoA might enable increased synthesis of polythioesters
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metabolism
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in mammals, excess cysteine is generally degraded by oxygenation to 3-sulfino-L-alanine. The majority of cysteine sulphinic acid is then deaminated to sulphinylpyruvate, which decomposes spontaneously byreleasing inorganic sulphite. The latter compound is then further oxidized to sulphate, which is excreted for the most part from the cell. In parallel, a variable proportion of cysteine sulphinic acid is decarboxylated to hypotaurine, then further oxidized to taurine. Although cysteine can be catabolized by some non-oxidative pathways, they are of minor importance. CDO activity is regulated by concentration of cysteine, and in mammals, both have been demonstrated to be important vital factors
metabolism
active-site cluster models and comparison of CDO and 3-mercaptopropionate dioxygenase MDO, EC 1.13.11.91. The enzymes have different iron(III)-superoxo-bound structures due to differences in ligand coordination. The differences in the second-coordination sphere and the position of a positively charged Arg residue result in changes in substrate positioning, mobility and enzymatic turnover. For both enzymes, the second oxygen atom transfer has the highest barriers with magnitudes of 14.2 and 15.8 kcal/mol, respectively. In CDO with its 3-His ligand system, there are close-lying singlet, triplet and quintet spin-state surfaces along the mechanism, and the reaction will be influenced by the equilibration between these spin states and the ease of spin state change
metabolism
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design of biomimetic model complexes where the 3-His coordination of theiron ion is simulated by three pyrazole donors of a trispyrazolyl borate ligand and protected cysteine represent substrate ligands. Replacement of phenyl groups attached at the 3-positions of the pyrazole units in a previous model by mesityl residues has massive consequences, as the latter arrange to a more spacious reaction pocket. The reaction with O2 proceeds much faster and the structural characterization of an iron(II) eta2-O,O-sulfinate product became possible
metabolism
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iron(II) complexes [Fe(L)(MeCN)3](SO3CF3)2 (L are two derivatives of tris(2-pyridyl)-based ligands) as models for cysteine dioxygenase. The molecular structure of one of the complexes exhibits octahedral coordination geometry, and the Fe-Npy bond lengths are similar to those in the Cys-bound FeII-CDO. The iron(II) centers of the complexes exhibit relatively high FeIII/II redox potentials E1/2 0.988-1.380 V vs. ferrocene/ferrocenium electrode. The reaction of in situ generated [Fe(L)(MeCN)(SPh)]+ with excess O2 in acetonitrile yields selectively the doubly oxygenated phenylsulfinic acid product. Both oxygen atoms of O2 are incorporated into the product. A FeIII peroxido intermediate with a rhombic S=1=2 FeIII center is involved in the reaction
metabolism
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mononuclear Co(II) complexes with the general formula [Co2+(TpR2)(CysOEt)] (R = Ph or Me, TpR2 = hydrotris(pyrazol-1-yl)borate substituted with R-groups at the 3- and 5-positions, and CysOEt is the anion of L-cysteine ethyl ester) mimic the active-site structure of substrate-bound CDO and are analogous to functional iron-based CDO models. The complexes possess five-coordinate structures featuring facially-coordinatingTpR2 and S,N-bidentate CysOEt ligands. The air-stability of the Ph-variant replicates the inactivity of cobalt-substituted CDO. The Me-variant reversibly binds O2 at reduced temperatures to yield an orange chromophore. Both are high-spin (S = 3/2) complexes. The orange chromophore is a S = 1/2 species featuring a low-spin Co(III) center bound to an end-on (eta1) superoxo ligand
metabolism
-
nonheme FE(II) complex [Fe(TpMe2)(2-ATP)] , where 2-ATP is 2-aminothiophenolate, models substrate-bound cysteine dioxygenase. The complex reacts with O2 at -80°C to yield a purple intermediat that features a thiolate-ligated Fe(III) center bound to a superoxide radical, mimicking the putative structure of a key CDO intermediate
metabolism
the first target to oxidize during the iron-assisted Cys-Tyr cofactor biogenesis is Cys93
metabolism
the O2 activation mechanism suggests the binding of O2 to the metal ion followed by the attack of the distal oxygen atom on the cysteine sulfur. An alternative mechanism entails the attack of the cysteine sulfur on the proximal oxygen atom of the dioxygen moiety to form a persulfenate intermediate without any redox exchange between the metal ion and the O2 ligand. The O2 activation mechanism with a Ni-substituted active site follows the same pattern as native CDOs albeit with much higher energy barriers for the formation of the intermediates. The immediate cleavage of the persulfenate S-O bond in the alternative mechanism suggests that cysteine persulfenate might not be a true intermediate
physiological function
cysteine metabolism
physiological function
-
CDO is crucial for oxidation of cysteine to cysteine sulfinic acid and therefore for sulfite production and secretion
physiological function
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CDO is crucial for oxidation of cysteine to cysteine sulfinic acid and therefore for sulfite production and secretion
physiological function
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CDO is crucial for oxidation of cysteine to cysteine sulfinic acid and therefore for sulfite production and secretion. In dermatophytes, CDO is a virulence factor crucial for keratin degradation, role of cysteine dioxygenase in the degradation of keratinized tissues by dermatophytes, overview
physiological function
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CDO is crucial for oxidation of cysteine to cysteine sulfinic acid and therefore for sulfite production and secretion. In dermatophytes, CDO is a virulence factor crucial for keratin degradation, role of cysteine dioxygenase in the degradation of keratinized tissues by dermatophytes, overview
physiological function
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CDO is crucial for oxidation of cysteine to cysteine sulfinic acid and therefore for sulfite production and secretion. In dermatophytes, CDO is a virulence factor crucial for keratin degradation, role of cysteine dioxygenase in the degradation of keratinized tissues by dermatophytes, overview. In Candida albicans upregulated expression of CDO is detected in the switch from white to opaque phenotypes [18]. In the latter, a reversible transition has been described between smooth white, dome-shaped yeast colonies (white) to circular or irregular-shaped colonies, composed of a mixture of yeast and fi lamentous cells (opaque)
physiological function
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cysteine dioxygenase is a key enzyme involved in the homeostatic regulation of cysteine level and in production of important oxidized metabolites of cysteine such as pyruvate, sulphite, sulphate, hypotaurine, and taurine in all eukaryotic cells, CDO is crucial for oxidation of cysteine to cysteine sulphinic acid and therefore for sulphite production and secretion
physiological function
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cysteine dioxygenase is a mononuclear nonheme iron(II)-dependent enzyme critical for maintaining appropriate cysteine and taurine levels in eukaryotic systems
physiological function
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cysteine dioxygenase is a non-heme mononuclear iron enzyme that catalyzes the O2-dependent oxidation of L-cysteine to produce cysteine sulfinic acid
physiological function
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in Histoplasma capsulatum, the enzyme is a key factor in the transition from the mycelial to yeast phase. CDO is crucial for oxidation of cysteine to cysteine sulfinic acid and therefore for sulfite production and secretion
physiological function
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mammalian cysteine dioxygenase is a non-heme iron protein, in its ferrous form [Fe(II)-CDO] it catalyzes the conversion of cysteine to cysteine sulfinic acid by incorporating both oxygen atoms of molecular oxygen to form the product
physiological function
cysteine dioxygenase (CDO) helps regulate Cys levels through converting Cys to Cys sulfinic acid. 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
physiological function
importance of CdoA for the metabolism of the sulfur compounds 3,3'-thiodipropionic acid and 3,3'-dithiodipropionic acid by further converting their degradation product, 3-mercaptopropionate
physiological function
in the ferrous form, CDO catalyzes irreversibly the conversion of cysteine to cysteine sulfinate, incorporating both atoms of dioxygen into the product. Cysteine sulfinate is an intermediate of several pathways related to pyruvate and sulfurated metabolites, such as sulfate, taurine, and hypotaurine. The CDO performance increases in response to high cysteine levels,either through the formation of a C93-Y157 crosslink, or a diminished degradation by the ubiquitin-proteasome system
physiological function
the enzyme is involved in the metabolism of L-cysteine in the body
physiological function
the monoprotonated ES complexes with 3-mercaptopropionic acid and cysteine have different pKs. At higher pH, kcat decreases sigmoidally with a similar pK regardless of substrate. Loss of reactivity at high pH is attributed to deprotonation of tyrosine 159 and its influence on dioxygen binding. A mechanism model shows deprotonation of tyrosine 159 both blocks oxygen binding and concomitantly promotes cystine formation
physiological function
ADO catalyzes conversion of N-terminal cysteine to cysteine sulfinic acid and is related to the plant cysteine oxidases that mediate responses to hypoxia by an identical post-translational modification. In human cells ADO regulates the RGS4/5 (regulator of G-protein signalling) N-degron substrates, modulates G-protein coupled Ca2+ signals and MAPK activity, and acts on N-terminal cysteine proteins including the angiogenic cytokine IL-32. Inactivation of ADO leads to constitutive upregulation of endogenous and transfected RGS4 and RGS5 proteins irrespective of oxygen levels
physiological function
CDO knockout female mice exhibit severe defects in mammary branching morphogenesis and ductal elongation, resulting in poor lactation. CDO contributes to the luminal epithelial cell differentiation, proliferation, and apoptosis mainly through its downstream product cysteine sulfinic acid. Exogenous supplementation of cysteine sulfinic acid rescues the defects in CDO knockout mice and enhances ductal growth in wild-type mice
physiological function
CDO-/- mouse sperm demonstrates a severe lack of in vitro fertilization ability. Acrosome exocytosis and tyrosine phosphorylation profiles in response to stimuli are normal. CDO-/- sperm has a slight increase in head abnormalities. Taurine and hypotaurine concentrations in CDO-/- sperm decrease in the epididymal intraluminal fluid and sperm cytosol. No evidence of antioxidant protection against lipid peroxidation is found. CDO-/- sperm exhibits severe defects in volume regulation, swelling in response to the relatively hypo-osmotic conditions found in the female reproductive tract
physiological function
CDO1 gene is expressed in both the mold and yeast morphotypes and both morphotypes show significant CDO activity. Intracellular cysteine levels are significantly higher in the mold form of two Panamanian strains, 184AS and 186AS, equal in both mold and yeast in the class 1 Downs strain and significantly higher in yeast of the more pathogenic class 2 G217B strain
physiological function
hepatic cytosolic fraction cysteine dioxygenase activity is not responsible for the S-oxidation of the substituted cysteine, S-carboxymethyl-L-cysteine
physiological function
PCO dioxygenase activity produces Cys-sulfinic acid at the N-terminus of ERF-VII peptide, which then undergoes efficient arginylation by arginyl transferase ATE1
physiological function
transcription factor NRF2, i.e. nuclear factor-erythroid 2 p45-related factor two, promotes the accumulation of intracellular cysteine and engages the cysteine homeostatic control mechanism mediated by cysteine dioxygenase 1
physiological function
transcription factor NRF2, i.e. nuclear factor-erythroid 2 p45-related factor two, promotes the accumulation of intracellular cysteine and engages the cysteine homeostatic control mechanism mediated by cysteine dioxygenase 1
physiological function
-
CDO1 gene is expressed in both the mold and yeast morphotypes and both morphotypes show significant CDO activity. Intracellular cysteine levels are significantly higher in the mold form of two Panamanian strains, 184AS and 186AS, equal in both mold and yeast in the class 1 Downs strain and significantly higher in yeast of the more pathogenic class 2 G217B strain
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physiological function
-
the monoprotonated ES complexes with 3-mercaptopropionic acid and cysteine have different pKs. At higher pH, kcat decreases sigmoidally with a similar pK regardless of substrate. Loss of reactivity at high pH is attributed to deprotonation of tyrosine 159 and its influence on dioxygen binding. A mechanism model shows deprotonation of tyrosine 159 both blocks oxygen binding and concomitantly promotes cystine formation
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physiological function
-
importance of CdoA for the metabolism of the sulfur compounds 3,3'-thiodipropionic acid and 3,3'-dithiodipropionic acid by further converting their degradation product, 3-mercaptopropionate
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physiological function
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importance of CdoA for the metabolism of the sulfur compounds 3,3'-thiodipropionic acid and 3,3'-dithiodipropionic acid by further converting their degradation product, 3-mercaptopropionate
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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
additional information
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cysteine dioxygenase crystal structures from pH 4-9: Cys binding is minimal at below pH 5 and persulfenate formation is consistently seen at pH values between pH 5.5 and pH 7. At above pH 8, the active-site iron shifts from 4- to 5-coordinate, and Cys is bound, while dioxygen is not
additional information
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intracellular CDO concentration is regulated at both transcriptional and posttranslational levels, supplementation of growth medium with L-cystine induces a persistent increase in the CDO mRNA transcript level, whereas the concentration of intracellular CDO protein changes over time. Mechanism of cysteine oxygenation from iron(II)-superoxo complex, via cis- and trans-sulfoxide structure formation, to iron(IV)-oxo complex and the final product cysteine sulphinic acid
additional information
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intracellular CDO concentration is regulated at both transcriptional and posttranslational levels. Mechanism of cysteine oxygenation from iron(II)-superoxo complex, via cis- and trans-sulfoxide structure formation, to iron(IV)-oxo complex and the final product cysteine sulphinic acid
additional information
-
intracellular CDO concentration is regulated at both transcriptional and posttranslational levels. Mechanism of cysteine oxygenation from iron(II)-superoxo complex, via cis- and trans-sulfoxide structure formation, to iron(IV)-oxo complex and the final product cysteine sulphinic acid
additional information
-
intracellular CDO concentration is regulated at both transcriptional and posttranslational levels. Mechanism of cysteine oxygenation from iron(II)-superoxo complex, via cis- and trans-sulfoxide structure formation, to iron(IV)-oxo complex and the final product cysteine sulphinic acid
additional information
-
intracellular CDO concentration is regulated at both transcriptional and posttranslational levels. Mechanism of cysteine oxygenation from iron(II)-superoxo complex, via cis- and trans-sulfoxide structure formation, to iron(IV)-oxo complex and the final product cysteine sulphinic acid
additional information
-
intracellular CDO concentration is regulated at both transcriptional and posttranslational levels. Mechanism of cysteine oxygenation from iron(II)-superoxo complex, via cis- and trans-sulfoxide structure formation, to iron(IV)-oxo complex and the final product cysteine sulphinic acid
additional information
-
intracellular CDO concentration is regulated at both transcriptional and posttranslational levels. Mechanism of cysteine oxygenation from iron(II)-superoxo complex, via cis- and trans-sulfoxide structure formation, to iron(IV)-oxo complex and the final product cysteine sulphinic acid
additional information
-
NO as a substrate analogue for O2 is used to prepare a species that mimics the geometric and electronic structures of an early reaction intermediate, analysis by magnetic circular dichroism, electron paramagnetic resonance, and electronic absorption spectroscopies as well as computational methods including density functional theory and semiempirical calculations, quantum mechanics/molecular mechanics calculations, overview. The NO adducts of Cys- and selenocysteine (Sec)-bound Fe(II)CDO exhibit virtually identical electronic properties
additional information
persulfenate and persulfide binding in the active site of cysteine dioxygenase, overview
additional information
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structures of iron-containing CDO model complexes, modeling, overview
additional information
-
the catalytic cycle of CDO can be primed by one electron through chemical oxidation to produce CDO with ferric iron in the active site. The C93-Y157 pair of mammalian CDO is catalytically essential. The monoanionic active site contains a 5- or 6-coordinate ferrous iron with solvent molecules serving as the non-protein ligands. In the absence of substrate and/or cofactor, the reduced active site is unreactive toward O2
additional information
modeling the pH-dependence of cysteine dioxygenation
additional information
structure and mechanism leading to formation of the cysteine sulfinate product complex of a biomimetic cysteine dioxygenase model, i.e. trispyrazolylborato iron(II) cysteinato complex, overview. The enzyme contains an iron active site with an unusual 3-His ligation to the protein, which contrasts with the structural features of common non-heme iron dioxygenases
additional information
structure modeling of cysteine dioxygenase in complex with L-cysteine dianion
additional information
the BsCDO active site has a non-heme iron coordinated by three conserved residues His75, His77, and His125. Ser137, His139, andTyr141 form the catalytic triad. The bound L-Cys coordinates the iron in a bidentate fashion via its Sgamma and N atoms. Structure comparisons, overview
additional information
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the BsCDO active site has a non-heme iron coordinated by three conserved residues His75, His77, and His125. Ser137, His139, andTyr141 form the catalytic triad. The bound L-Cys coordinates the iron in a bidentate fashion via its Sgamma and N atoms. Structure comparisons, overview
additional information
the CDO enzyme active site structure comprises residues Tyr58, Arg60, His86, His88, Cys93, His140, and Tyr157, structure model
additional information
the structure of CDO, which is highly conserved across multiple species, is built on a small alpha-helical domain containing three alpha-helices at the N-terminus, followed by 13 beta-strands. These are subdivided into a main beta-sandwich domain and two beta-hairpins at the C terminus. The entire beta-sandwich is composed of seven anti-parallel beta-strands on the lower side and six anti-parallel beta-strands on the upper side. The active site comprises an iron ion, which is located in the central portion of the cupin beta-sandwhich, and is connected to the bulk solvent through a solvent-filled channel
additional information
wild-type and mutant active site structures, overview
additional information
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the BsCDO active site has a non-heme iron coordinated by three conserved residues His75, His77, and His125. Ser137, His139, andTyr141 form the catalytic triad. The bound L-Cys coordinates the iron in a bidentate fashion via its Sgamma and N atoms. Structure comparisons, overview
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no activity in Nostoc sp., Bacillus subtilis (O32085), Bacillus subtilis, Streptomyces coelicolor (O50490), Streptomyces coelicolor (Q9KZL0), Rattus norvegicus (P21816), Bacillus cereus (Q81CX4), Bacillus cereus, Streptomyces coelicolor A3(2) SCO3035 (Q9KZL0), Bacillus cereus DSM 31 (Q81CX4), Streptomyces coelicolor A3(2) SCO5772 (O50490)
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2006
Rattus norvegicus
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Dominy, J.E.; Hwang, J.; Stipanuk, M.H.
Overexpression of cysteine dioxygenase reduces intracellular cysteine and glutathione pools in HepG2/C3A cells
Am. J. Physiol. Endocrinol. Metab.
293
E62-E69
2007
Rattus norvegicus
brenda
Oien, D.B.; Moskovitz, J.
Ablation of the mammalian methionine sulfoxide reductase A affects the expression level of cysteine dioxygenase
Biochem. Biophys. Res. Commun.
352
556-559
2007
Mus musculus
brenda
Pierce, B.S.; Gardner, J.D.; Bailey, L.J.; Brunold, T.C.; Fox, B.G.
Characterization of the nitrosyl adduct of substrate-bound mouse cysteine dioxygenase by electron paramagnetic resonance: electronic structure of the active site and mechanistic implications
Biochemistry
46
8569-8578
2007
Mus musculus (P60334), Mus musculus
brenda
Dominy, J.E.; Hwang, J.; Guo, S.; Hirschberger, L.L.; Zhang, S.; Stipanuk, M.H.
Synthesis of amino acid cofactor in cysteine dioxygenase is regulated by substrate and represents a novel post-translational regulation of activity
J. Biol. Chem.
283
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2008
Rattus norvegicus (P21816)
brenda
Ueki, I.; Stipanuk, M.H.
3T3-L1 adipocytes and rat adipose tissue have a high capacity for taurine synthesis by the cysteine dioxygenase/cysteinesulfinate decarboxylase and cysteamine dioxygenase pathways
J. Nutr.
139
207-214
2009
Rattus norvegicus
brenda
Stipanuk, M.H.; Ueki, I.; Dominy, J.E.; Simmons, C.R.; Hirschberger, L.L.
Cysteine dioxygenase: a robust system for regulation of cellular cysteine levels
Amino Acids
37
55-63
2009
Rattus norvegicus
brenda
Honjoh, K.I.; Matsuura, K.; Machida, T.; Nishi, K.; Nakao, M.; Yano, T.; Miyamoto, T.; Iio, M.
Enhancement of menadione stress tolerance in yeast by accumulation of hypotaurine and taurine: co-expression of cDNA clones, from Cyprinus carpio, for cysteine dioxygenase and cysteine sulfinate decarboxylase in Saccharomyces cerevisiae
Amino Acids
38
1173-1183
2009
Cyprinus carpio (Q2PFL1), Cyprinus carpio (Q2PFL2), Cyprinus carpio
brenda
de Visser, S.
Elucidating enzyme mechanism and intrinsic chemical properties of short-lived intermediates in the catalytic cycles of cysteine dioxygenase and taurine/alpha-ketoglutarate dioxygenase
Coord. Chem. Rev.
253
754-768
2009
Homo sapiens (Q16878)
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brenda
Bruland, N.; Wuebbeler, J.H.; Steinbuechel, A.
3-mercaptopropionate dioxygenase, a cysteine dioxygenase homologue, catalyzes the initial step of 3-mercaptopropionate catabolism in the 3,3-thiodipropionic acid-degrading bacterium variovorax paradoxus
J. Biol. Chem.
284
660-672
2009
Variovorax paradoxus
brenda
Kleffmann, T.; Jongkees, S.A.; Fairweather, G.; Wilbanks, S.M.; Jameson, G.N.
Mass-spectrometric characterization of two posttranslational modifications of cysteine dioxygenase
J. Biol. Inorg. Chem.
14
913-921
2009
Rattus norvegicus
brenda
Siakkou, E.; Wilbanks, S.M.; Jameson, G.N.
Simplified cysteine dioxygenase activity assay allows simultaneous quantitation of both substrate and product
Anal. Biochem.
405
127-131
2010
Rattus norvegicus
brenda
Gardner, J.D.; Pierce, B.S.; Fox, B.G.; Brunold, T.C.
Spectroscopic and computational characterization of substrate-bound mouse cysteine dioxygenase: nature of the ferrous and ferric cysteine adducts and mechanistic implications
Biochemistry
49
6033-6041
2010
Mus musculus
brenda
Kasperova, A.; Kunert, J.; Horynova, M.; Weigl, E.; Sebela, M.; Lenobel, R.; Raska, M.
Isolation of recombinant cysteine dioxygenase protein from Trichophyton mentagrophytes
Mycoses
54
e456-462
2011
Trichophyton mentagrophytes (D1MF76), Trichophyton mentagrophytes, Trichophyton mentagrophytes TM-10 (D1MF76)
brenda
Crawford, J.A.; Li, W.; Pierce, B.S.
Single turnover of substrate-bound ferric cysteine dioxygenase with superoxide anion: enzymatic reactivation, product formation, and a transient intermediate
Biochemistry
50
10241-10253
2011
Mus musculus
brenda
Tchesnokov, E.P.; Wilbanks, S.M.; Jameson, G.N.L.
A strongly bound high-spin iron(II) coordinates cysteine and homocysteine in cysteine dioxygenase
Biochemistry
51
257-264
2012
Rattus norvegicus
brenda
Blaesi, E.J.; Gardner, J.D.; Fox, B.G.; Brunold, T.C.
Spectroscopic and computational characterization of the NO adduct of substrate-bound Fe(II) cysteine dioxygenase: insights into the mechanism of O2 activation
Biochemistry
52
6040-6051
2013
Mus musculus
brenda
Souness, R.J.; Kleffmann, T.; Tchesnokov, E.P.; Wilbanks, S.M.; Jameson, G.B.; Jameson, G.N.
Mechanistic implications of persulfenate and persulfide binding in the active site of cysteine dioxygenase
Biochemistry
52
7606-7617
2013
Rattus norvegicus (P21816)
brenda
Siakkou, E.; Rutledge, M.T.; Wilbanks, S.M.; Jameson, G.N.L.
Correlating crosslink formation with enzymatic activity in cysteine dioxygenase
Biochim. Biophys. Acta
1814
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2011
Rattus norvegicus
brenda
Che, X.; Gao, J.; Liu, Y.; Liu, C.
Metal vs. chalcogen competition in the catalytic mechanism of cysteine dioxygenase
J. Inorg. Biochem.
122
1-7
2013
Rattus norvegicus
brenda
Driggers, C.M.; Cooley, R.B.; Sankaran, B.; Hirschberger, L.L.; Stipanuk, M.H.; Karplus, P.A.
Cysteine dioxygenase structures from pH 4 to 9: consistent Cys-persulfenate formation at intermediate pH and a Cys-bound enzyme at higher pH
J. Mol. Biol.
425
3121-3136
2013
Homo sapiens
brenda
Kasperova, A.; Kunert, J.; Raska, M.
The possible role of dermatophyte cysteine dioxygenase in keratin degradation
Med. Mycol.
51
449-454
2013
Histoplasma capsulatum, Bacillus sp. (in: Bacteria), Candida albicans, Streptomyces sp., Mammalia, Trichophyton rubrum, Trichophyton mentagrophytes
brenda
Arjune, S.; Schwarz, G.; Belaidi, A.A.
Involvement of the Cys-Tyr cofactor on iron binding in the active site of human cysteine dioxygenase
Amino Acids
47
55-63
2015
Homo sapiens (Q16878), Homo sapiens
brenda
Wenning, L.; Stoeveken, N.; Wuebbeler, J.H.; Steinbuechel, A.
Substrate and cofactor range differences of two cysteine dioxygenases from Ralstonia eutropha H16
Appl. Environ. Microbiol.
82
910-921
2015
Cupriavidus necator (Q0K029), Cupriavidus necator (Q0KB75), Cupriavidus necator DSM 428 (Q0K029), Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1 (Q0K029), Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1 (Q0KB75)
brenda
Davies, C.G.; Fellner, M.; Tchesnokov, E.P.; Wilbanks, S.M.; Jameson, G.N.
The Cys-Tyr cross-link of cysteine dioxygenase changes the optimal pH of the reaction without a structural change
Biochemistry
53
7961-7968
2014
Rattus norvegicus (P21816)
brenda
Pietra, F.
On the dynamical behavior of the cysteine dioxygenase-L-cysteine complex in the presence of free dioxygen and L-cysteine
Chem. Biodivers.
14
e1700290
2017
Rattus norvegicus (P21816)
brenda
Tchesnokov, E.P.; Faponle, A.S.; Davies, C.G.; Quesne, M.G.; Turner, R.; Fellner, M.; Souness, R.J.; Wilbanks, S.M.; de Visser, S.P.; Jameson, G.N.
An iron-oxygen intermediate formed during the catalytic cycle of cysteine dioxygenase
Chem. Commun. (Camb.)
52
8814-8817
2016
Rattus norvegicus (P21816)
brenda
Sallmann, M.; Kumar, S.; Chernev, P.; Nehrkorn, J.; Schnegg, A.; Kumar, D.; Dau, H.; Limberg, C.; de Visser, S.P.
Structure and mechanism leading to formation of the cysteine sulfinate product complex of a biomimetic cysteine dioxygenase model
Chemistry
21
7470-7479
2015
Homo sapiens (Q16878)
brenda
Faponle, A.S.; Seebeck, F.P.; de Visser, S.P.
Sulfoxide synthase versus cysteine dioxygenase reactivity in a nonheme iron enzyme
J. Am. Chem. Soc.
139
9259-9270
2017
Rattus norvegicus (P21816)
brenda
Driggers, C.M.; Kean, K.M.; Hirschberger, L.L.; Cooley, R.B.; Stipanuk, M.H.; Karplus, P.A.
Structure-based insights into the role of the Cys-Tyr crosslink and inhibitor recognition by mammalian cysteine dioxygenase
J. Mol. Biol.
428
3999-4012
2016
Rattus norvegicus (P21816)
brenda
Driggers, C.M.; Hartman, S.J.; Karplus, P.A.
Structures of Arg- and Gln-type bacterial cysteine dioxygenase homologs
Protein Sci.
24
154-161
2015
Bacillus subtilis (O32085), Bacillus subtilis, Bacillus subtilis 168 (O32085)
brenda
Pierce, B.S.; Subedi, B.P.; Sardar, S.; Crowell, J.K.
The ''Gln-Type'' thiol dioxygenase from Azotobacter vinelandii is a 3-mercaptopropionic acid dioxygenase
Biochemistry
54
7477-7490
2015
Azotobacter vinelandii
brenda
Fellner, M.; Aloi, S.; Tchesnokov, E.P.; Wilbanks, S.M.; Jameson, G.N.
Substrate and pH-dependent kinetic profile of 3-mercaptopropionate dioxygenase from Pseudomonas aeruginosa
Biochemistry
55
1362-1371
2016
Pseudomonas aeruginosa (Q9I0N5), Pseudomonas aeruginosa DSM 22644 (Q9I0N5)
brenda
Tchesnokov, E.P.; Fellner, M.; Siakkou, E.; Kleffmann, T.; Martin, L.W.; Aloi, S.; Lamont, I.L.; Wilbanks, S.M.; Jameson, G.N.
The cysteine dioxygenase homologue from Pseudomonas aeruginosa is a 3-mercaptopropionate dioxygenase
J. Biol. Chem.
290
24424-24437
2015
Pseudomonas aeruginosa (Q9I0N5), Pseudomonas aeruginosa, Pseudomonas aeruginosa DSM 22644 (Q9I0N5)
brenda
White, M.D.; Klecker, M.; Hopkinson, R.J.; Weits, D.A.; Mueller, C.; Naumann, C.; O'Neill, R.; Wickens, J.; Yang, J.; Brooks-Bartlett, J.C.; Garman, E.F.; Grossmann, T.N.; Dissmeyer, N.; Flashman, E.
Plant cysteine oxidases are dioxygenases that directly enable arginyl transferase-catalysed arginylation of N-end rule targets
Nat. Commun.
8
14690
2017
Arabidopsis thaliana (Q9LXG9), Arabidopsis thaliana (Q9SJI9)
brenda
Li, J.; Koto, T.; Davis, I.; Liu, A.
Probing the Cys-Tyr cofactor biogenesis in cysteine dioxygenase by the genetic incorporation of fluorotyrosine
Biochemistry
58
2218-2227
2019
Homo sapiens (Q16878), Homo sapiens
brenda
Forbes, D.L.; Meneely, K.M.; Chilton, A.S.; Lamb, A.L.; Ellis, H.R.
The 3-His metal coordination site promotes the coupling of oxygen activation to cysteine oxidation in cysteine dioxygenase
Biochemistry
59
2022-2031
2020
Rattus norvegicus (P21816)
brenda
Fischer, A.A.; Lindeman, S.V.; Fiedler, A.T.
A synthetic model of the nonheme iron-superoxo intermediate of cysteine dioxygenase
Chem. Commun. (Camb.)
54
11344-11347
2018
synthetic construct
brenda
Song, Z.; Yue, Y.; Feng, S.; Sun, H.; Li, Y.; Xu, F.; Zhang, Q.; Wang, W.
Cysteine dioxygenase catalyzed C-F bond cleavage An in silico approach
Chem. Phys. Lett.
750
137449
2020
Homo sapiens (Q16878)
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brenda
Anandababu, K.; Ramasubramanian, R.; Wadepohl, H.; Comba, P.; Johnee Britto, N.; Jaccob, M.; Mayilmurugan, R.
A structural and functional model for the tris-histidine motif in cysteine dioxygenase
Chemistry
25
9540-9547
2019
synthetic construct
brenda
Mueller, L.; Hoof, S.; Keck, M.; Herwig, C.; Limberg, C.
Enhancing tris(pyrazolyl)borate-based models of cysteine/cysteamine dioxygenases through steric effects increased reactivities, full product characterization and hints to initial superoxide formation
Chemistry
26
11851-11861
2020
synthetic construct
brenda
Yeh, C.G.; Pierides, C.; Jameson, G.N.L.; de Visser, S.P.
Structure and functional differences of cysteine and 3-mercaptopropionate dioxygenases A computational study
Chemistry
27
13793-13806
2021
Homo sapiens (Q16878)
brenda
Kang, Y.P.; Torrente, L.; Falzone, A.; Elkins, C.M.; Liu, M.; Asara, J.M.; Dibble, C.C.; DeNicola, G.
Correction Cysteine dioxygenase 1 is a metabolic liability for non-small cell lung cancer
eLife
8
e45572
2019
Mus musculus (P60334), Homo sapiens (Q16878)
brenda
Asano, A.; Roman, H.B.; Hirschberger, L.L.; Ushiyama, A.; Nelson, J.L.; Hinchman, M.M.; Stipanuk, M.H.; Travis, A.J.
Cysteine dioxygenase is essential for mouse sperm osmoadaptation and male fertility
FEBS J.
285
1827-1839
2018
Mus musculus (P60334), Mus musculus
brenda
Fischer, A.A.; Miller, J.R.; Jodts, R.J.; Ekanayake, D.M.; Lindeman, S.V.; Brunold, T.C.; Fiedler, A.T.
Spectroscopic and computational comparisons of thiolate-ligated ferric nonheme complexes to cysteine dioxygenase second-sphere effects on substrate (analogue) positioning
Inorg. Chem.
58
16487-16499
2019
synthetic construct
brenda
Attia, A.; Silaghi-Dumitrescu, R.
Nickel-substituted iron-dependent cysteine dioxygenase Implications for the dioxygenation activity of nickel model compounds
Int. J. Quantum Chem.
118
e25564
2018
Rattus norvegicus (P21816)
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brenda
Zhao, J.; Han, Y.; Ma, X.; Zhou, Y.; Yuan, S.; Shen, Q.; Ye, G.; Liu, H.; Fu, P.; Zhang, G.; Qiao, B.; Liu, A.
Cysteine dioxygenase regulates the epithelial morphogenesis of mammary gland via cysteine sulfinic acid
iScience
13
173-189
2019
Mus musculus (P60334), Mus musculus
brenda
Adams, M.A.; Shearer, G.
Cysteine dioxygenase enzyme activity and gene expression in the dimorphic pathogenic fungus Histoplasma capsulatum is in both the mold and yeast morphotypes and exhibits substantial strain variation
J. Fungi (Basel)
6
24
2020
Histoplasma capsulatum (Q5RLY7), Histoplasma capsulatum, Histoplasma capsulatum ATCC MYA-2454 (Q5RLY7)
brenda
Steventon, G.B.; Khan, S.; Mitchell, S.C.
Comparison of the sulfur-oxygenation of cysteine and S-carboxymethyl-l-cysteine in human hepatic cytosol and the role of cysteine dioxygenase
J. Pharm. Pharmacol.
70
1069-1077
2018
Homo sapiens (Q16878), Homo sapiens
brenda
Li, J.; Griffith, W.P.; Davis, I.; Shin, I.; Wang, J.; Li, F.; Wang, Y.; Wherritt, D.J.; Liu, A.
Cleavage of a carbon-fluorine bond by an engineered cysteine dioxygenase
Nat. Chem. Biol.
14
853-860
2018
Homo sapiens (Q16878), Homo sapiens
brenda
Puerta, M.; Perata, P.; Hopkinson, R.; Flashman, E.; Licausi, F.; Ratcliffe, P.
Conserved N-terminal cysteine dioxygenases transduce responses to hypoxia in animals and plants
Science
364
65-69
2019
Homo sapiens (Q96SZ5), Homo sapiens
brenda