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Literature summary extracted from
- Expression of a soluble form of iodotyrosine deiodinase for active site characterization by engineering the native membrane protein from Mus musculus (2012), Protein Sci., 21, 351-361.
Application
| EC Number | Application | Comment | Organism |
|---|---|---|---|
| 1.21.1.1 | synthesis | high expression of a truncated derivative lacking the membrane domain, residues 2-33, at its N-terminal is observed in Sf9 cells, whereas expression in Pichia pastoris remains low despite codon optimization. The desired expression in Escherichia coli can be achieved after replacing the two conserved Cys residues of the deiodinase with Ala and fusing the resulting protein to thioredoxin. This construct provides abundant enzyme for crystallography and mutagenesis | Mus musculus |
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 1.21.1.1 | expressed in Sf9 insect cells and in Escherichia coli | Mus musculus |
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 1.21.1.1 | hanging dop vapor diffusion method, using 0.2 M ammonium acetate, 0.1 M BisTris (pH 6.5), and 45% v/v 2-methyl-2,4-pentanediol | Mus musculus |
| 1.21.1.1 | structure of a truncated derivative lacking the membrane domain, residues 2-33, at its N-terminal, and its complex with substrate monoiodotyrosine. In the absence of substrate, the active site appears very accessible to solvent due to a lack of detectable structure in two surrounding regions of the polypeptide. In the presence of substrate, an active site lid comprised of a helix and loop is detected from the diffraction data. This lid effectively sequesters the substrate-flavin complex from solvent | Mus musculus |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 1.21.1.1 | E153Q | the mutant exhibits no measurable binding affinity for 3-chloro-L-tyrosine | Mus musculus |
| 1.21.1.1 | E153Q | mutation reduces the deiodinase activity to an undetectable level. Mutant exhibits no measurable binding affinity for the substrate | Mus musculus |
| 1.21.1.1 | K178Q | upon expression in Escherichia coli, inactive and insoluble | Mus musculus |
| 1.21.1.1 | Y157F | the mutation weakens the binding of 3-chloro-L-tyrosine by 20fold | Mus musculus |
| 1.21.1.1 | Y157F | lack of the phenolic -OH of Y157F increases the kcat and KM values for deiodination by more than sevenfold and decreases the kcat/KM value more modestly by less than 40% | Mus musculus |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.21.1.1 | 0.019 | - |
3,5-diiodo-L-tyrosine | enzyme expressed in Pichia pastoris, pH not specified in the publication, temperature not specified in the publication | Mus musculus |  |
| 1.21.1.1 | 0.04 | - |
3,5-diiodo-L-tyrosine | enzyme expressed in Escherichia coli and lacking the transmembrane domain, pH not specified in the publication, temperature not specified in the publication | Mus musculus | |
| 1.21.1.1 | 0.44 | - |
3,5-diiodo-L-tyrosine | mutant Y157F, expressed in Escherichia coli and lacking the transmembrane domain, pH not specified in the publication, temperature not specified in the publication | Mus musculus | |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 1.21.1.1 | soluble | - |
Mus musculus | - |
- |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 1.21.1.1 | 30000 | - |
x * 30000, SDS-PAGE | Mus musculus |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.21.1.1 | 3,5-diiodo-L-tyrosine + NADPH + H+ | Mus musculus | - |
3-iodo-L-tyrosine + NADP+ + I- | - |
? | |
| 1.21.1.1 | 3-iodo-L-tyrosine + NADPH + H+ | Mus musculus | - |
L-tyrosine + NADP+ + I- | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.21.1.1 | Mus musculus | Q9DCX8 | - |
- |
| 1.21.1.1 | Mus musculus | Q9DCX8 | isoform iodotyrosine dehalogenase 1 | - |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 1.21.1.1 | HiTrap column chromatography | Mus musculus |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.21.1.1 | 3,5-diiodo-L-tyrosine + NADPH + H+ | - |
Mus musculus | 3-iodo-L-tyrosine + NADP+ + I- | - |
? | |
| 1.21.1.1 | 3-iodo-L-tyrosine + NADPH + H+ | - |
Mus musculus | L-tyrosine + NADP+ + I- | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 1.21.1.1 | ? | x * 30000, SDS-PAGE | Mus musculus |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.21.1.1 | iodotyrosine dehalogenase 1 | - |
Mus musculus |
| 1.21.1.1 | iodotyrosine deiodinase | - |
Mus musculus |
| 1.21.1.1 | IYD | - |
Mus musculus |
| 1.21.1.1 | lyd | - |
Mus musculus |
Turnover Number [1/s]
| EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.21.1.1 | 0.12 | - |
3,5-diiodo-L-tyrosine | enzyme expressed in Pichia pastoris, pH not specified in the publication, temperature not specified in the publication | Mus musculus | |
| 1.21.1.1 | 0.16 | - |
3,5-diiodo-L-tyrosine | enzyme expressed in Escherichia coli and lacking the transmembrane domain, pH not specified in the publication, temperature not specified in the publication | Mus musculus | |
| 1.21.1.1 | 1.08 | - |
3,5-diiodo-L-tyrosine | mutant Y157F, expressed in Escherichia coli and lacking the transmembrane domain, pH not specified in the publication, temperature not specified in the publication | Mus musculus | |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.21.1.1 | FMN | - |
Mus musculus | |
| 1.21.1.1 | FMNH2 | - |
Mus musculus | |
kcat/KM [mM/s]
| EC Number | kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.21.1.1 | 2.5 | - |
3,5-diiodo-L-tyrosine | mutant Y157F, expressed in Escherichia coli and lacking the transmembrane domain, pH not specified in the publication, temperature not specified in the publication | Mus musculus | |
| 1.21.1.1 | 3.83 | - |
3,5-diiodo-L-tyrosine | enzyme expressed in Escherichia coli and lacking the transmembrane domain, pH not specified in the publication, temperature not specified in the publication | Mus musculus | |
| 1.21.1.1 | 6 | - |
3,5-diiodo-L-tyrosine | enzyme expressed in Pichia pastoris, pH not specified in the publication, temperature not specified in the publication | Mus musculus | |
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