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Article

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

Endocrinology - 1 Oct 1992

Berry M J, Maia A L, Kieffer J D, Harney J W, Larsen P R

Abstract excerpt

Type I iodothyronine 5' deiodinase (5'DI) contains selenocysteine, encoded by a UGA codon, and this amino acid is essential for maximum catalytic efficiency in this enzyme. We recently showed that translation of UGA as selenocysteine in this protein requires a specific sequence of about 250 nucleotides in the 3' untranslated region of the messenger RNA. Translation of a 5'DI cysteine mutant does not require the...

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Identifiers

PMID: 1396330
DOI: 10.1210/endo.131.4.1396330

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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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Substitution of cysteine for selenocysteine in type I iodothyronine deiodinase reduces the catalytic efficiency of the protein but enhances its translation.PMID 1396330Read ↗

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

Mechanism and regulation of selenoprotein synthesis.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 ↗

The 3′-Untranslated Region of Human Type 2 Iodothyronine Deiodinase mRNA Contains a Functional Selenocysteine Insertion Sequence ElementSemantic proximity Read ↗

Efficient incorporation of multiple selenocysteines involves an inefficient decoding step serving as a potential translational checkpoint and ribosome bottleneck.Semantic proximity Read ↗

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

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

Regulation of selenocysteine incorporation into the selenium transport protein, selenoprotein P.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 ↗

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

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

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