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
-
sulfinic
-
non-heme
- hypotaurine
-
cysteinesulfinate
- cysteamine
- cystathionine
- 3-mercaptopropionate
-
cys-tyr
-
taut
-
adenosyltransferase
-
desulfhydration
-
2-his-1-carboxylate
-
gamma-lyase
-
cupins
- 2-aminoethanethiol
- medicine
Reaction
Synonyms
3-mercaptopropionate dioxygenase, 3MDO, ADO, Arg-type CDO, BsCDO, CDO, CDO1, CDO2, CdoA, CdoB, cysteine dioxygenase, cysteine dioxygenase type 1, cysteine oxidase, Fe(II) cysteine dioxygenase, H16_A1614, H16_B1863, NP_251292, oxygenase, cysteine di-, PA2602, PCO1, PCO4
ECTree
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Metals Ions
Metals Ions on EC 1.13.11.20 - cysteine dioxygenase
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Fe
Fe2+
Iron
Mg
purified human cystein dioxygenase yields trace amounts of magnesium about 0.41%
Mn
purified human cystein dioxygenase yields trace amounts of manganese about 0.25%
Ni2+
Zn2+
additional information
Fe
-
Fe2+ required, 0.8-0.9 gatom of iron per 22500 g of purified protein
upon purification the protein is catalytically inactive, activity can be restored upon the addition of exogenous ferrous iron, with maximal activation at a ferrous iron concentration of 0.3 mM
Fe2+
YubC: Upon purification the protein is catalytically inactive, activity can be restored upon the addition of exogenous ferrous iron, with maximal activation at a ferrous iron concentration of 0.3 mM
Fe2+
a catalytic a non-heme iron is coordinated by three conserved residues His75, His77, and His125
Fe2+
purified human cystein dioxygenase yields a iron incorporation of about 68%
Fe2+
unsaturated distored tetragonal bipyramidal ferrous center with a vacant coordination site
Fe2+
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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. A Fe(III)-superoxo rather than a Fe(IV)-oxo intermediate facilitates substrate oxidation
Fe2+
non-heme iron enzyme. The enzyme contains an iron active site with an unusual 3-His ligation to the protein, which contrasts with the structural features of common nonheme iron dioxygenases
Fe2+
higher kcat and lower Km value, when the enzyme is expressed in medium containing extra iron and purified in buffers lacking EDTA.
Fe2+
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a a mononuclear nonheme iron(II)-dependent enzyme. It possesses both an unusual 3-His facial ligation sphere to the iron center and a rare Cys-Tyr crosslink near the active site
Fe2+
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additon of 0.2 or 0.3 mM Fe2+ yields near-optimal activity. Activity of fully purified enzyme in the absence of added Fe2+ is below 1% of that measured in the presence of 0.3 mM ferrous sulfate.
Fe2+
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required for catalysis, in the Cys-bound complexes, the change of the oxidation state for the Fe center is II to III to II. Binding involves coordination with His86, His88, and His140
Fe2+
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strongly bound high-spin iron(II) coordinates cysteine and homocysteine in cysteine dioxygenase, overview. CDO tightly binds iron(II) at a 3His active site. Although the cross-link between C93 and Y157 is close to the active site, it does not appear to affect iron binding. Stopped-flow measurements and Mössbauer spectral analysis, overview
Fe2+
required for activity, an iron-oxygen intermediate is formed during the catalytic cycle of cysteine dioxygenase, Moessbauer spectroscopy analysis resuting in three different species: CDO:FeII, CDO:FeII:cysteine site I, and CDO:FeII:cysteine site II, dissociation constants, absorptions spectra, and structure analysis, detailed overview
Fe2+
required, enzyme-bound. The iron ion is coordinated by H86, H88, H140 and a water molecule, and can further accept a coordinating L-cysteine molecule
Fe2+
upon purification the protein is catalytically inactive, activity can be restored upon the addition of exogenous ferrous iron, with maximal activation at a ferrous iron concentration of 0.3 mM
Iron
-
iron content is 0.8 mol of iron per mol of MDO. Addition of NO to 3-mercaptopropanoate-bound enzyme quantitatively yields an iron-nitrosyl species with EPR features consistent with a mononuclear (FeNO)7 site
Iron
active site iron is coordinated by 3 histidines and 3 water molecules
Iron
-
loosely bound to protein, only 10% of purified protein contains iron
Ni2+
the optimized structure of the dioxygen-bound active site features an S=2 quintet ground state, with a Ni(III)-superoxo species
Zn2+
purified human cystein dioxygenase yields a zinc incorporation of about 18.1%
Co2+ fails to restore significant activity to purified proteins
additional information
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Co2+ fails to restore significant activity to purified proteins
additional information
Mn2+ fails to restore significant activity to purified proteins
additional information
-
Mn2+ fails to restore significant activity to purified proteins
additional information
Ni2+ fails to restore significant activity to purified proteins
additional information
-
Ni2+ fails to restore significant activity to purified proteins
additional information
Zn2+ fails to restore significant activity to purified proteins
additional information
-
Zn2+ fails to restore significant activity to purified proteins
additional information
YubC: Co2+ fails to restore significant activity to purified proteins
additional information
-
YubC: Co2+ fails to restore significant activity to purified proteins
additional information
YubC: Mn2+ fails to restore significant activity to purified proteins
additional information
-
YubC: Mn2+ fails to restore significant activity to purified proteins
additional information
YubC: Ni2+ fails to restore significant activity to purified proteins
additional information
-
YubC: Ni2+ fails to restore significant activity to purified proteins
additional information
YubC: Zn2+ fails to restore significant activity to purified proteins
additional information
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YubC: Zn2+ fails to restore significant activity to purified proteins
additional information
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concentration of FeIII-CDO is highly variable and often does not exceed 5% relative to the catalytically active ferrous enzyme, ferric enzyme is catalytically inactive
additional information
Co2+ fails to restore significant activity to purified proteins
additional information
Co2+ fails to restore significant activity to purified proteins
additional information
Mn2+ fails to restore significant activity to purified proteins
additional information
Mn2+ fails to restore significant activity to purified proteins
additional information
Ni2+ fails to restore significant activity to purified proteins
additional information
Ni2+ fails to restore significant activity to purified proteins
additional information
Zn2+ fails to restore significant activity to purified proteins
additional information
Zn2+ fails to restore significant activity to purified proteins