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Article

Conserved cysteines in the type 1 deiodinase selenoprotein are not essential for catalytic activity.

The Journal of biological chemistry - 25 Sept 1998

Croteau W, Bodwell J E, Richardson J M, St Germain D L

Abstract excerpt

The iodothyronine deiodinases are a family of oxidoreductases that catalyze the removal of iodide from thyroid hormones. Each of the three isoforms contain selenocysteine at its active site and several cysteine residues that may be important for catalytic activity. Of particular interest in the type I deiodinase (D1) is Cys124, which is vicinal to the selenocysteine at position 126, and Cys194, which has been...

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Identifiers

PMID: 9737986
DOI: 10.1074/jbc.273.39.25230

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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Conserved cysteines in the type 1 deiodinase selenoprotein are not essential for catalytic activity.PMID 9737986Read ↗

The role of the active site cysteine in catalysis by type 1 iodothyronine deiodinase.Semantic proximity Read ↗

Substitution of cysteine for selenocysteine in type I iodothyronine deiodinase reduces the catalytic efficiency of the protein but enhances its translation.Semantic proximity Read ↗

Substitution of cysteine for a conserved alanine residue in the catalytic center of type II iodothyronine deiodinase alters interaction with reducing cofactor.Semantic proximity Read ↗

In vivo dimerization of types 1, 2, and 3 iodothyronine selenodeiodinases.Semantic proximity Read ↗

Catalysis leads to posttranslational inactivation of the type 1 deiodinase and alters its conformation.Semantic proximity Read ↗

Characterization of recombinant Xenopus laevis type I iodothyronine deiodinase: substitution of a proline residue in the catalytic center by serine (Pro132Ser) restores sensitivity to 6-propyl-2-thiouracil.Semantic proximity Read ↗

Identification of critical amino acids for 3,5,3'-triiodothyronine deiodination by human type 1 deiodinase based on comparative functional-structural analyses of the human, dog, and rat enzymes.Semantic proximity Read ↗

Iodothyronine deiodinase structure and function: from ascidians to humans.Semantic proximity Read ↗

The iodothyronine selenodeiodinases are thioredoxin-fold family proteins containing a glycoside hydrolase clan GH-A-like structure.Semantic proximity Read ↗

Biochemical mechanisms of thyroid hormone deiodination.Semantic proximity Read ↗

Insights into the role of deiodinases from studies of genetically modified animals.Semantic proximity Read ↗

Identification of the key residues responsible for the assembly of selenodeiodinases.Semantic proximity Read ↗

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