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Literature summary for 1.21.99.4 extracted from
- Modeling of the 5'-deiodination of thyroxine by iodothyronine deiodinase: Chemical corroboration of a selenenyl iodide intermediate (2010), Angew. Chem., 49, 545-547.
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| L-thyroxine + AH2 | - |
Homo sapiens | 3,5,3'-triiodo-L-thyronine + iodide + A + H+ | - |
? |  |
| additional information | the catalytic cycle of ID-1 involves a ping-pong bisubstrate reaction in which the selenol form of the enzyme (ESeH) reacts with L-thyroxine to form a selenenyl iodide intermediate (ESeI) with release of the deiodinated compound 3,5,3'-triiodo-L-thyronine, and a subsequent reaction between the selenenyl iodide intermediate and possibly a thiol cofactor regenerates the selenol form | Homo sapiens | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| ID-1 | - |
Homo sapiens |
| type I iodothyronine deiodinase | - |
Homo sapiens |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| dithioerythritol | - |
Homo sapiens | |
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Release 2023.1 (January 2023)
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