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Literature summary for 1.21.1.1 extracted from

  • Hu, J.; Chuenchor, W.; Rokita, S.E.
    A switch between one- and two-electron chemistry of the human flavoprotein iodotyrosine deiodinase is controlled by substrate (2015), J. Biol. Chem., 290, 590-600.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
gene DEHAL1, recombinant expression of N-terminally SUMO-tagged enzyme in Escherichia coli strain Rosetta 2(DE3) Homo sapiens

Crystallization (Commentary)

Crystallization (Comment) Organism
purified enzyme in complex with substrate 3-iodo-L-tyrosine, method optimization, hanging drop diffusion method, mixing of 0.001 ml of 12 mg/ml protein in 50mM sodium phosphate, pH 7.4, 100 mM NaCl, 1 mM DTT, and 10% glycerol with 0.001 ml of precipitant solution containing 0.05 M ammonium sulfate, 50 mM BisTris, pH 6.5, and 25% pentaerythritol ethoxylate, 2 days, 20°C. To generate co-crystals the enzyme is treated with 1.5 mM 3-iodo-L-tyrosine overnight and then subjected to the same hanging drop procedure using a well solution of 0.15 M sodium acetate, 85mM Tris-HCl, pH 8.5, 25.5% w/v PEG 4000, and 15% glycerol at 20 °C, 24 h, X-ray diffraction structure determination and analysis at 2.45-2.65 A resolution, molecular replacement Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information Michaelis-Menten steady-state kinetics. Dissociation constants for different substrate analogues, overview Homo sapiens
0.031
-
3-iodo-L-tyrosine pH 7.6, temperature not specified in the publication, recombinant enzyme Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane transmembrane enzyme Homo sapiens 16020
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
30000
-
two identical subunits of human IYD form an alphabeta fold, 2 * 30000, recombinant enzyme, SDS-PAGE Homo sapiens

Natural Substrates/ Products (Substrates)

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+
-
r

Organism

Organism UniProt Comment Textmining
Homo sapiens Q6PHW0 gene DEHAL1
-

Purification (Commentary)

Purification (Comment) Organism
recombinant SUMO-tagged enzyme from Escherichia coli strain Rosetta 2(DE3) by nickel affinity chromatography, tag removal, and gel filtration Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining
thyroid gland
-
Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3-iodo-L-tyrosine + NADPH + H+
-
Homo sapiens L-tyrosine + NADP+ + iodide
-
r
L-tyrosine + 2 NADP+ + 2 iodide
-
Homo sapiens 3,5-diiodo-L-tyrosine + 2 NADPH + 2 H+
-
r
L-tyrosine + 2 NADP+ + 2 iodide
-
Homo sapiens 3,5-diiodo-L-tyrosine + 2 NADPH + 2 H+ stepwise single electron transfer involving FMN, ferredoxin, and NADPH, overview. Ability of the substrate to provide multiple interactions with the isoalloxazine system ofFMN that are usually provided by protein side chains. Ligand binding acts to template the active site geometry and significantly stabilize the one-electron-reduced semiquinone form of FMN r
L-tyrosine + NADP+ + iodide
-
Homo sapiens 3-iodo-L-tyrosine + NADPH + H+
-
r
additional information a synergy between substrate selectivity and catalytic activity is created by the enzyme. No activity with the substrate analog 3-fluoro-L-tyrosine Homo sapiens ?
-
?

Subunits

Subunits Comment Organism
heterodimer two identical subunits of human IYD form an alphabeta fold, 2 * 30000, recombinant enzyme, SDS-PAGE Homo sapiens
More the enzyme contains three domains: an N-terminal transmembrane region, an intermediate domain, and a catalytic domain Homo sapiens

Synonyms

Synonyms Comment Organism
IYD
-
Homo sapiens

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.208
-
3-iodo-L-tyrosine pH 7.6, temperature not specified in the publication, recombinant enzyme Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.6
-
assay at Homo sapiens

pH Range

pH Minimum pH Maximum Comment Organism
6 9 pH dependence of IYD binding and turnover, tightest binding was measured near a neutral pH of 7.6–7.7 Homo sapiens

Cofactor

Cofactor Comment Organism Structure
FMN FMN binds non-covalently at the dimer interface established by a helix from each of the two identical subunits involving residues Ser102 and Ser128. Iodotyrosine deiodinase utilizes FMN to maintain iodide homeostasis by reductive deiodination of iodotyrosine. In the absence of an active site ligand, only the oxidized and two-electron-reduced forms of FMN are detected Homo sapiens

General Information

General Information Comment Organism
evolution domain swaps at each N and C terminus consistent with the nitro-FMN reductase superfamily Homo sapiens
additional information a synergy between substrate selectivity and catalytic activity is created by the enzyme, active site and cofactor and substrate binding structures, overview Homo sapiens
physiological function iodotyrosine deiodinase utilizes FMN to maintain iodide homeostasis by reductive deiodination of iodotyrosine Homo sapiens

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
6.72
-
3-iodo-L-tyrosine pH 7.6, temperature not specified in the publication, recombinant enzyme Homo sapiens