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
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taut
-
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
- 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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Engineering
Engineering on EC 1.13.11.20 - cysteine dioxygenase
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C93A
C93S
C93 mutation reduces activity to 50%, zinc content of about 45%, specific activity of Cys-93 mutants is proportional to the measured iron content.
Y157F
in the gel-filtration chromatography Y157F shows an additional peak with an estimated molecular weight equivalent to a cysteine dioxygenase dimer. The results for monomer and dimer are similar. Activity reduced to 5% of the wild type activity. Zinc content of about 45%
G95C
C93A
site-directed mutagenesis, mutation of the active site residue, no crosslink formation resulting in reduced activity compared to the wild-type enzyme. The mutant variant structure has a new chloride ion coordinating the active site iron. Cys binding is also different from wild-type CDO, and no Cys-persulfenate forms in the C93A active site at pH 6.2 or pH 8.0
C93E
mutation to the corresponding residue of cupin to reestablish the common 3-His/1-Glu metal ligand of the cupin superfamily. Mutant shows dioxygen consumption, which, is not coupled with L-cysteine oxidation. Substrate analogues (D-cysteine, cysteamine, and 3-mercaptopropionate) show variable coordinations to the iron center, but are not viable substrates for the variant
C93G
C93S
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mutant can not be converted to the mature form due to the loss of the cysteine residue involved in thioether crosslink formation
H86A
R60A
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mutant forms with low activity, which has a markedly decreased affinity for cysteine, probably due to the loss of the hydrogen bonding partner for the carboxylate of the substrate, forms the crosslink more slowly
Y157F
site-directed mutagenesis, mutation of the active site residue, no crosslink formation resulting in reduced activity compared to the wild-type enzyme. The mutant variant structure has a new chloride ion coordinating the active site iron. Cys binding is also different from wild-type CDO, and no Cys-persulfenate forms in the Y157F active site at pH 6.2 or pH 8.0
additional information
C93 mutation reduces activity to 50%, zinc content of about 45%, specific activity of Cys-93 mutants is proportional to the measured iron content.
C93A
site-directed mutagenesis, CDO activity of the C93A variant increases with a much lower rate of iron supplementation and consequently a much higher concentration is required to approximate saturation, it has a 18fold higher Kd value
variant is able to form a cysteine-tyrosine crosslink homologous to that found in mammalian cysteine dioxygenases. Activity of this variant is severely impaired
G95C
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variant is able to form a cysteine-tyrosine crosslink homologous to that found in mammalian cysteine dioxygenases. Activity of this variant is severely impaired
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C93G
site-directed mutagenesis, structure comparison to the wild-type enzyme
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expression of either the wild-type or a catalytically inactivated mutant H86A in HepG2/C3A cells which do not express endogenous cysteine dioxygenase protein and culture in different concentrations of extracellular cysteine. Wild-type enzyme, but not mutant H86A, is capable of reducing intracellular cysteine levels in cells incubated in physiologically relevant concentrations of cysteine. Wild-type enzyme also decreases the glutathione pool and potentiates the toxicity of CdCl2
H86A
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inactive mutant, leading to loss of the His that serves as a metal ligand in the active site does not form any crosslink
CDO-CSD fusion protein, cysteine dioxygenase and cysteine sulfinate decarboxylase
additional information
CDO-CSD fusion protein, cysteine dioxygenase and cysteine sulfinate decarboxylase
additional information
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CDO-CSD fusion protein, cysteine dioxygenase and cysteine sulfinate decarboxylase
additional information
enzyme contains a posttranslationally generated Cys93-Tyr157 crosslinked cofactor. Incorporating unnatural tyrosines in place of Tyr157 via a genetic method gives catalytically active variants with a thioether bond between Cys93 and the halogen-substituted Tyr157. Crystal structures and data of both wild-type and engineered CDO variants in the purely uncrosslinked form and with a mature cofactor indicate that the enzyme can catalyze oxidative C-F or C-Cl bond cleavage, resulting in a substantial conformational change of both Cys93 and Tyr157 during cofactor assembly
additional information
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enzyme contains a posttranslationally generated Cys93-Tyr157 crosslinked cofactor. Incorporating unnatural tyrosines in place of Tyr157 via a genetic method gives catalytically active variants with a thioether bond between Cys93 and the halogen-substituted Tyr157. Crystal structures and data of both wild-type and engineered CDO variants in the purely uncrosslinked form and with a mature cofactor indicate that the enzyme can catalyze oxidative C-F or C-Cl bond cleavage, resulting in a substantial conformational change of both Cys93 and Tyr157 during cofactor assembly
additional information
expression of purely uncross-linked human CDO due to site-specific incorporation of 3,5-difluoro-L-tyrosine Cys-Tyr at the cross-linking site through a genetic code expansion strategy
additional information
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expression of purely uncross-linked human CDO due to site-specific incorporation of 3,5-difluoro-L-tyrosine Cys-Tyr at the cross-linking site through a genetic code expansion strategy
additional information
a selenomethionine-substituted cysteine dioxygenase is produced
additional information
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recombinant cysteine dioxygenase protein with a thioredoxin sequence and 6 x His tagged, after purification the 6x His tag and the thioredoxin sequence are removed using factor Xa.
additional information
C93A and Y157F unliganded active site structures comparison