1.21.1.1: iodotyrosine deiodinase
This is an abbreviated version!
For detailed information about iodotyrosine deiodinase, go to the full flat file.
Word Map on EC 1.21.1.1
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1.21.1.1
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thyroid
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iodide
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deiodination
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hypothyroidism
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diiodotyrosine
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thyroglobulin
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dehalogenation
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halotyrosines
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iodothyronine
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nitroreductase
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goiter
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bromo
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chlorotyrosine
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organification
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diagnostics
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synthesis
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medicine
- 1.21.1.1
- thyroid
- iodide
-
deiodination
- hypothyroidism
- diiodotyrosine
- thyroglobulin
-
dehalogenation
-
halotyrosines
-
iodothyronine
- nitroreductase
- goiter
-
bromo
-
chlorotyrosine
-
organification
- diagnostics
- synthesis
- medicine
Reaction
Synonyms
DEHAL1, Dehal1 protein, DEHAL1B, EC 1.22.1.1, iodotyrosine dehalogenase 1, iodotyrosine deiodinase, IYD, lyd, NADH oxidase/flavin reductase, SUP-18, SUP-18 IYD, TDH
ECTree
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Engineering
Engineering on EC 1.21.1.1 - iodotyrosine deiodinase
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E154Q
the mutation diminishes the affinity of the enzyme for 3,5-diiodo-L-tyrosine by 30fold
K179Q
the mutation diminishes the affinity of the enzyme for 3,5-diiodo-L-tyrosine by 46fold
Y158F
the mutation results in a 7fold decrease in the enzyme's affinity for 3,5-diiodo-L-tyrosine
I116T
naturally occuring mutation involved in iodotyrosine deiodinase deficiency, the mutant shows highly reduced activity compared to te wild-type enzyme
R101W
naturally occuring mutation involved in iodotyrosine deiodinase deficiency, the mutant shows highly reduced activity compared to te wild-type enzyme
E153Q
Y157F
additional information
the mutant exhibits no measurable binding affinity for 3-chloro-L-tyrosine
E153Q
mutation reduces the deiodinase activity to an undetectable level. Mutant exhibits no measurable binding affinity for the substrate
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%
naturally occuring sup-18 loss-of-function mutations, e.g. splice-junction mutants and spontaneaous mutations, overview
additional information
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naturally occuring sup-18 loss-of-function mutations, e.g. splice-junction mutants and spontaneaous mutations, overview
additional information
mutations occuring in enzyme deficiency include homozygous one inframe-deletion of three base pairs (F105-I106L) and two missense (R101W, I116T). The mutations are located in close vicinity of each other within exon 2 of the gene encoding a putative FMN-binding site at the nitroreductase catalytic domain of the protein. All three mutations dramatically reduce the in vitro activity of the enzyme, one is also prematurely degraded
additional information
-
mutations occuring in enzyme deficiency include homozygous one inframe-deletion of three base pairs (F105-I106L) and two missense (R101W, I116T). The mutations are located in close vicinity of each other within exon 2 of the gene encoding a putative FMN-binding site at the nitroreductase catalytic domain of the protein. All three mutations dramatically reduce the in vitro activity of the enzyme, one is also prematurely degraded