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Information on EC 1.13.11.20 - cysteine dioxygenase
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1.13.11.20 cysteine dioxygenaseIUBMB Comments
Requires Fe2+ and NAD(P)H.
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Word Map
- 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
The enzyme appears in viruses and cellular organisms
Synonyms
cysteine dioxygenase, cysteine oxidase, cysteine dioxygenase type 1, bscdo, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
3MDO
Arg-type CDO
BsCDO
CDO
CDO1
CdoA
CdoB
cysteine dioxygenase
cysteine oxidase
-
-
-
-
H16_A1614
H16_B1863
NP_251292
oxygenase, cysteine di-
-
-
-
-
PA2602
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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.
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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
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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
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L-cysteine + O2 = 3-sulfinoalanine
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-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
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-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
L-cysteine:oxygen oxidoreductase
Requires Fe2+ and NAD(P)H.
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CAS REGISTRY NUMBER
COMMENTARY
37256-59-0
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
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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-mercaptopropanoate + O2
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
-
-
?
3-mercaptopropanoate + O2
3-sulfinopropanoate + H+
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
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+
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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
-
-
?
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
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
-
highly specific for L-cysteine
-
?
L-cysteine + O2
3-sulfino-L-alanine
-
probable role in the mycelial to yeast phase transition
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?
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
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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
-
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
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?
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
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key enzyme of cysteine catabolism, supplies substrate for taurine biosynthesis
-
-
?
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
-
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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-
-
?
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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-
?
additional information
?
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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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-
-
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
-
-
-
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
-
-
?
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
?
-
-
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
?
-
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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
-
-
?
additional information
?
-
formation of an active CDO:cysteine substrate complex
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-
?
additional information
?
-
homocysteine and D-Cys are no substrates
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-cysteine + O2
3-sulfino-L-alanine
-
probable role in the mycelial to yeast phase transition
-
?
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 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-sulfinoalanine
-
-
-
?
additional information
?
-
-
cysteine dioxygenase and methionine sulfoxide reductase are working in coordination to balance cellular antioxidant level
-
-
?
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
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADH
enzyme uses NAD+/NADH as pharmacological chaperone. Presence of 0.1 mM NADH increase activity 1.3fold
Cys-Tyr cofactor
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. Production of a Cys-Tyr cofactor-saturated enzyme and analysis of the Cys-Tyr cofactor on kinetic properties, overview. The Cys-Tyr cofactor strongly contributes to efficient iron coordination in the active center of CDO
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additional information
-
NAD+ does not appear to be a cofactor, the role of NAD+ in the stimulation of the enzyme is unclear
-
additional information
-
no requirement of NAD, NADP, NADH or NADPH for the enzymic activity of protein-B. The enzymic activity of protein-B alone is extremely low, protein-A alone does not exhibit catalytic activity, however a significant activity is observed in the presence of both fractions, requirement of protein-A for the catalytic activity of protein-B
-
additional information
-
NADPH or NADH do not act as cosubstrates, most of added NADPH disappears from the incubation mixture during the first 10 min, while cysteinesulfinic acid remains linear for up to 30 min, the role of NADHP or NADH may be one of stabilization, as allosteric activators or other type of activating agents
-
additional information
enzyme uses an amino acid cofactor in the active site consisting of two cross-linked residues, cysteine 93 and tyrosine 157. Formation of the Cys-Tyr cofactor requires a transition metal cofactor Fe2+ and O2. Biogenesis of the cofactor is also strictly dependent upon the presence of substrate. In the absence of the Cys-Tyr cofactor, the enzyme possesses appreciable catalytic activity. At physiologically relevant cysteine concentrations, cofactor formation increases catalytic efficiency 10-fold
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe