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Literature summary for 1.21.1.1 extracted from
- Characterization of a flavoprotein iodotyrosine deiodinase from bovine thyroid. Flavin nucleotide binding and oxidation-reduction properties (1979), J. Biol. Chem., 254, 12326-12330.
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| soluble | - |
Bos taurus | - |
- |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bos taurus | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| purification of stable aporptoein | Bos taurus |
Renatured (Commentary)
| Renatured (Comment) | Organism |
|---|---|
| apoprotein binds FMN with an almost complete restoration of enzymatic activity. It can also bind FAD with partial restoration of activity, but does not bind riboflavin | Bos taurus |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| thyroid gland | - |
Bos taurus | - |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| FAD | - |
Bos taurus |  |
| FMN | 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 | Bos taurus | |
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