KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | rapid kinetics of dehalogenation promoted by iodotyrosine deiodinase from human thyroid, substrates chloro-, bromo-, and iodotyrosine bind with similar rate constants, overview. Standard two-state model, no intermediate complex accumulates during closure of the active site lid induced by substrate | Homo sapiens |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-tyrosine + 2 NADP+ + 2 iodide | Homo sapiens | - |
3,5-diiodo-L-tyrosine + 2 NADPH + 2 H+ | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
- |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
thyroid | - |
Homo sapiens | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-tyrosine + 2 NADP+ + 2 bromide | halide elimination does not appear to limit reactions of bromo- and iodotyrosine since both fully oxidize the reduced enzyme with nearly equivalent second-order rate constants despite the differing strength of their carbon-halogen bonds | Homo sapiens | 3,5-dibromo-L-tyrosine + 2 NADPH + 2 H+ | - |
r | |
L-tyrosine + 2 NADP+ + 2 chloride | chlorotyrosine reacts with the reduced enzyme approximately 20fold more slowly than bromo- and iodotyrosine and reveals a spectral intermediate that forms at approximately the same rate as the bromo- and iodotyrosine reactions | Homo sapiens | 3,5-dichloro-L-tyrosine + 2 NADPH + 2 H+ | - |
r | |
L-tyrosine + 2 NADP+ + 2 iodide | - |
Homo sapiens | 3,5-diiodo-L-tyrosine + 2 NADPH + 2 H+ | - |
? | |
L-tyrosine + 2 NADP+ + 2 iodide | halide elimination does not appear to limit reactions of bromo- and iodotyrosine since both fully oxidize the reduced enzyme with nearly equivalent second-order rate constants despite the differing strength of their carbon-halogen bonds | Homo sapiens | 3,5-diiodo-L-tyrosine + 2 NADPH + 2 H+ | - |
r | |
additional information | fluorotyrosine is an inert substrate analogue | Homo sapiens | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
IYD | - |
Homo sapiens |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
flavin | dependent on | Homo sapiens | |
NADPH | - |
Homo sapiens |
General Information | Comment | Organism |
---|---|---|
metabolism | reductive dehalogenation such as that catalyzed by iodotyrosine deiodinase is highly unusual in aerobic organisms but necessary for iodide salvage from iodotyrosine generated during thyroxine biosynthesis | Homo sapiens |
physiological function | reductive dehalogenation such as that catalyzed by iodotyrosine deiodinase is highly unusual in aerobic organisms but necessary for iodide salvage from iodotyrosine generated during thyroxine biosynthesis | Homo sapiens |