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1.21.99.3: thyroxine 5-deiodinase

This is an abbreviated version!
For detailed information about thyroxine 5-deiodinase, go to the full flat file.

Word Map on EC 1.21.99.3

Reaction

3,3',5'-triiodo-L-thyronine
+
Iodide
 +
acceptor
 +
H+
=
L-thyroxine
 +
reduced acceptor

Synonyms

5'-deiodinase, D3, deiodinase, deiodinase 3, deiodinase, thyroxine 5-, deiodinase-3, diiodothyronine 5'-deiodinase, Dio, Dio3, Dio3a, Dio3b, EC 1.97.1.11, ID-3, iodothyronine 5-deiodinase, iodothyronine deiodinase type III, iodothyronine inner ring monodeiodinase, iodothyronine monodeiodinase, ITHD, T4-5'-deiodinase, T4-5-deiodinase, thyroxine 5-deiodinase, type 3 deiodinase, type 3 iodothyronine 5-deiodinase, type 3 iodothyronine deiodinase, type III deiodinase, type III iodothyronine deiodinase, type-3 deiodinase, zD3

ECTree

     1 Oxidoreductases
         1.21 Catalysing the reaction X-H + Y-H = X-Y
             1.21.99 With unknown physiological acceptors
                1.21.99.3 thyroxine 5-deiodinase

Engineering

Engineering on EC 1.21.99.3 - thyroxine 5-deiodinase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SeC144A
site-directed mutagenesis, exchange of the selenocysteine residue in the highly conserved active site sequence, enzymatically inactive
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
E200T
R275A
the mutant shows sharply reduced activity compared to the wild type enzyme
S167A
Sec170C
mutation in active site, crystallization data
T169A
T169S
U170A
inactive
Y197F
additional information
generation of enzyme knockout mice