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Literature summary for 1.21.99.3 extracted from

  • Croteau, W.; Whittemore, S.L.; Schneider, M.J.; St Germain, D.L.
    Cloning and expression of a cDNA for a mammalian type III iodothyronine deiodinase (1995), J. Biol. Chem., 270, 16569-16575.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
screening of neonatal skin cDNA library, DNA sequence determination and analysis, isozyme type III, an in-frame TGA codon encodes a selenocysteine residue, functional translation in Xenopus laevis oocytes, catalytis properties of recombinant and native enzyme are identical Rattus norvegicus

Inhibitors

Inhibitors Comment Organism Structure
aurothioglucose no inhibition, isozyme type III Rattus norvegicus
additional information no inhibition of 5-deiodinase activity by propylthiouracil Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Rattus norvegicus P49897 selenoprotein
-
Rattus norvegicus P49897 isozyme type III
-

Source Tissue

Source Tissue Comment Organism Textmining
skin
-
Rattus norvegicus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3,3',5'-triiodo-L-thyronine + AH2 no activity Rattus norvegicus 3,3'-diiodo-L-thyronine + iodide + A + H+
-
?
3,3',5-triiodo-L-thyronine + AH2 best substrate Rattus norvegicus 3,3'-diiodo-L-thyronine + iodide + A + H+ hormonally inactive ?
3,3',5-triiodo-L-thyronine + AH2 isozyme type III Rattus norvegicus 3,3'-diiodo-L-thyronine + iodide + A + H+ hormonally inactive ?
L-thyroxine + AH2 preferred substrate Rattus norvegicus 3,3',5'-triiodo-L-thyronine + iodide + A + H+ hormonally inactive ?
L-thyroxine + AH2 isozyme type III Rattus norvegicus 3,3',5'-triiodo-L-thyronine + iodide + A + H+ hormonally inactive ?
L-thyroxine + AH2 5-deiodinase activity Rattus norvegicus 3,3',5'-triiodo-L-thyronine + iodide + A + H+ hormonally inactive ?
L-thyroxine + AH2 no activity Rattus norvegicus 3,3',5-triiodo-L-thyronine + iodide + A + H+
-
?