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Literature summary for 1.21.99.3 extracted from

  • Kuiper, G.G.; Klootwijk, W.; Visser, T.J.
    Substitution of cysteine for selenocysteine in the catalytic center of type III iodothyronine deiodinase reduces catalytic efficiency and alters substrate preference (2003), Endocrinology, 144, 2505-2513.
    View publication on PubMed
Search for more literature for 1.21.99.3

Cloned(Commentary)

Cloned (Comment) Organism
isozyme type III, expression of wild-type and active site mutants in COS cells, 50fold higher expression level for the mutants than for the wild-type enzyme Homo sapiens

Protein Variants

Protein Variants Comment Organism
SeC144A site-directed mutagenesis, exchange of the selenocysteine residue in the highly conserved active site sequence, enzymatically inactive Homo sapiens
SeC144C site-directed mutagenesis, exchange of the selenocysteine residue in the highly conserved active site sequence, 5fold increased Km for 3,3',5-triiodo-L-thyronine and 100fold increased Km for 3,3',5,5'-tetraiodo-L-thyronine compared to the wild-type, 2-6fold reduced turnover Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0000028
-
 3,3',5-triiodo-L-thyronine native wild-type, pH 7.2, 37°C, in presence of 1 mM DTT Homo sapiens
0.0000031
-
 3,3',5-triiodo-L-thyronine recombinant wild-type, pH 7.2, 37°C, in presence of 0.3 mM DTT Homo sapiens
0.0000035
-
 L-thyroxine recombinant wild-type, pH 7.2, 37°C, in presence of 3 mM DTT Homo sapiens
0.0000042
-
 3,3',5-triiodo-L-thyronine recombinant mutant SeC144C, pH 7.2, 37°C, in presence of 0.3 mM DTT Homo sapiens
0.000008
-
 L-thyroxine native wild-type, pH 7.2, 37°C, in presence of 10 mM DTT Homo sapiens
0.000265
-
 L-thyroxine recombinant mutant SeC144C, pH 7.2, 37°C, in presence of 1 mM DTT Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
microsome isozyme type III Homo sapiens
-
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
32000
-
 x * 32000, isozyme type III, SDS-PAGE Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3,3',5-triiodo-L-thyronine + AH2 Homo sapiens selenocysteine residue in the active site is essential for efficient inner ring deiodination 3,3'-diiodo-L-thyronine + iodide + A + H+ i.e. 3,3'-diiodo-L-thyronine ?
3,3',5-triiodo-L-thyronine + AH2 Homo sapiens enzyme plays a critical role in regulating and maintaining the local 3,3',5-triiodo-L-thyronine content 3,3'-diiodo-L-thyronine + iodide + A + H+ i.e. 3,3'-diiodo-L-thyronine ?
L-thyroxine + AH2 Homo sapiens 5-deiodinase activity 3,3',5'-triiodo-L-thyronine + iodide + A + H+ enzyme plays a critical role in regulating and maintaining the local 3,3',5-triiodo-L-thyronine content ?
L-thyroxine + AH2 Homo sapiens selenocysteine residue in the active site is absolutely essential for efficient inner ring deiodination 3,3',5'-triiodo-L-thyronine + iodide + A + H+ enzyme plays a critical role in regulating and maintaining the local 3,3',5-triiodo-L-thyronine content ?

Organism

Organism UniProt Comment Textmining
Homo sapiens P55073
-
-
Homo sapiens P55073 isozyme type III
-

Reaction

Reaction Comment Organism Reaction ID
3,3',5'-triiodo-L-thyronine + iodide + acceptor + H+ = L-thyroxine + reduced acceptor all 3 isozyme types contain a selenocysteine residue at the active site Homo sapiens
a
3,3',5'-triiodo-L-thyronine + iodide + acceptor + H+ = L-thyroxine + reduced acceptor inner ring deiodination Homo sapiens
a

Source Tissue

Source Tissue Comment Organism Textmining
placenta isozyme type III Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3,3',5-triiodo-L-thyronine + AH2 isozyme type III Homo sapiens 3,3'-diiodo-L-thyronine + iodide + A + H+
-
 ?
3,3',5-triiodo-L-thyronine + AH2 selenocysteine residue in the active site is essential for efficient inner ring deiodination Homo sapiens 3,3'-diiodo-L-thyronine + iodide + A + H+ i.e. 3,3'-diiodo-L-thyronine ?
3,3',5-triiodo-L-thyronine + AH2 enzyme plays a critical role in regulating and maintaining the local 3,3',5-triiodo-L-thyronine content Homo sapiens 3,3'-diiodo-L-thyronine + iodide + A + H+ i.e. 3,3'-diiodo-L-thyronine ?
L-thyroxine + AH2 isozyme type III Homo sapiens 3,3',5'-triiodo-L-thyronine + iodide + A + H+
-
 ?
L-thyroxine + AH2 5-deiodinase activity Homo sapiens 3,3',5'-triiodo-L-thyronine + iodide + A + H+
-
 ?
L-thyroxine + AH2 5-deiodinase activity Homo sapiens 3,3',5'-triiodo-L-thyronine + iodide + A + H+ enzyme plays a critical role in regulating and maintaining the local 3,3',5-triiodo-L-thyronine content ?
L-thyroxine + AH2 selenocysteine residue in the active site is absolutely essential for efficient inner ring deiodination Homo sapiens 3,3',5'-triiodo-L-thyronine + iodide + A + H+ enzyme plays a critical role in regulating and maintaining the local 3,3',5-triiodo-L-thyronine content ?

Subunits

Subunits Comment Organism
? x * 32000, isozyme type III, SDS-PAGE Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.2
-
 assay at Homo sapiens

Cofactor

Cofactor Comment Organism Structure
dithiothreitol
-
 Homo sapiens
dithiothreitol reducing cofactor Homo sapiens