| Type I thyroxine 5'-deiodinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.21.99.4 | ||||||||
| CAS no. | 70712-46-8 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
| Type II thyroxine 5-deiodinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.21.99.3 | ||||||||
| CAS no. | 74506-30-2 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
| Type III thyroxine 5-deiodinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Mouse iodothyronine deiodinase 3 catalytic core rendered from PDB entry 4TR3 [1] | |||||||||
| Identifiers | |||||||||
| EC no. | 1.97.1.11 | ||||||||
| CAS no. | 74506-30-2 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
Iodothyronine deiodinases (EC 1.21.99.4 and EC 1.21.99.3) are a subfamily of deiodinase enzymes important in the activation and deactivation of thyroid hormones. Thyroxine (T4), the precursor of 3,5,3'-triiodothyronine (T3) is transformed into T3 by deiodinase activity. T3, through binding a nuclear thyroid hormone receptor, influences the expression of genes in practically every vertebrate cell.[2][3] Iodothyronine deiodinases are unusual in that these enzymes contain selenium, in the form of an otherwise rare amino acid selenocysteine.[4][5][6]
These enzymes are not to be confused with the iodotyrosine deiodinases that are also deiodinases, but not members of the iodothyronine family. The iodotyrosine deiodinases (unlike the iodothyronine deiodinases) do not use selenocysteine or selenium. The iodotyrosine enzymes work on iodinated single tyrosine residue molecules to scavenge iodine, and do not use as substrates the double-tyrosine residue molecules of the various iodothyronines.
- ^ Schweizer U, Schlicker C, Braun D, Köhrle J, Steegborn C (July 2014). "Crystal structure of mammalian selenocysteine-dependent iodothyronine deiodinase suggests a peroxiredoxin-like catalytic mechanism". Proceedings of the National Academy of Sciences of the United States of America. 111 (29): 10526–31. Bibcode:2014PNAS..11110526S. doi:10.1073/pnas.1323873111. PMC 4115520. PMID 25002520.
- ^ Bianco AC, Kim BW (October 2006). "Deiodinases: implications of the local control of thyroid hormone action". The Journal of Clinical Investigation. 116 (10): 2571–9. doi:10.1172/JCI29812. PMC 1578599. PMID 17016550.
- ^ Wu Y, Koenig RJ (August 2000). "Gene regulation by thyroid hormone". Trends in Endocrinology and Metabolism. 11 (6): 207–11. doi:10.1016/s1043-2760(00)00263-0. PMID 10878749. S2CID 44602986.
- ^ Köhrle J (January 2000). "The selenoenzyme family of deiodinase isozymes controls local thyroid hormone availability". Reviews in Endocrine & Metabolic Disorders. 1 (1–2): 49–58. doi:10.1023/A:1010012419869. PMID 11704992. S2CID 42616219.
- ^ Köhrle J (May 1999). "Local activation and inactivation of thyroid hormones: the deiodinase family". Molecular and Cellular Endocrinology. 151 (1–2): 103–19. doi:10.1016/S0303-7207(99)00040-4. PMID 10411325. S2CID 11333443.
- ^ Köhrle J (December 2000). "The deiodinase family: selenoenzymes regulating thyroid hormone availability and action". Cellular and Molecular Life Sciences. 57 (13–14): 1853–63. doi:10.1007/PL00000667. PMC 11147027. PMID 11215512. S2CID 40148034.