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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

Crystallization

Crystallization on EC 1.21.99.3 - thyroxine 5-deiodinase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
structure of the catalytic domain of mouse deiodinase Dio3, to 1.9 A resolution. The catalytic Sec170 is positioned in the loop connecting beta1 to alpha1. It points toward an elongated cleft that likely represents the iodothyronine binding site. The deiodination step follows a selenolate inline attack on the iodine delta-hole weakening the carbon-iodine bond. The abstracted iodonium is replaced by a proton approaching from the opposite side of the ring. The proton is conveyed to the 5-position of the iodothyronine along a triad His219, Glu200, and Ser167, with residues Tyr197 and Thr169 participating in the organization of an intricate H-bond network
using 20% (wtv) PEG 3350 and 0.2 M ammonium citrate (pH 7.0)