1.21.1.1: iodotyrosine deiodinase
This is an abbreviated version!
For detailed information about iodotyrosine deiodinase, go to the full flat file.
Word Map on EC 1.21.1.1
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1.21.1.1
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thyroid
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iodide
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deiodination
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hypothyroidism
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diiodotyrosine
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thyroglobulin
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dehalogenation
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halotyrosines
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iodothyronine
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nitroreductase
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goiter
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bromo
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chlorotyrosine
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organification
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diagnostics
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synthesis
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medicine
- 1.21.1.1
- thyroid
- iodide
-
deiodination
- hypothyroidism
- diiodotyrosine
- thyroglobulin
-
dehalogenation
-
halotyrosines
-
iodothyronine
- nitroreductase
- goiter
-
bromo
-
chlorotyrosine
-
organification
- diagnostics
- synthesis
- medicine
Reaction
Synonyms
DEHAL1, Dehal1 protein, DEHAL1B, EC 1.22.1.1, iodotyrosine dehalogenase 1, iodotyrosine deiodinase, IYD, lyd, NADH oxidase/flavin reductase, SUP-18, SUP-18 IYD, TDH
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Cofactor
Cofactor on EC 1.21.1.1 - iodotyrosine deiodinase
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flavin
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presence of a neutral flavin radical during the reaction. Radical is stable and persists at 4°C under aerobic conditions for many days
FMN
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enzyme is reduced in two successive 1-electron oxidation-reduction steps. The oxidation-reduction potential of the couple semiquinone/fully reduced enzyme is -0.412 V at pH 7 and 25°C. The value for the oxidized/semiquinone couple is -0.190 V at pH 7 and 25°C
FMN
FMN binds non-covalently at the dimer interface established by a helix from each of the two identical subunits involving residues Ser102 and Ser128. Iodotyrosine deiodinase utilizes FMN to maintain iodide homeostasis by reductive deiodination of iodotyrosine. In the absence of an active site ligand, only the oxidized and two-electron-reduced forms of FMN are detected
FMN
the FMN-binding site of mammalian IYD is conserved in SUP-18, FMN appears to require catalytic activity to function
the cofactors form a redox electron transport chain, overview
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additional information
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the cofactors form a redox electron transport chain, overview
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