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J. Biol. Chem., Vol. 266, Issue 22, 14155-14158, 08, 1991
MJ Berry, JD Kieffer, JW Harney and PR Larsen
The conversion of thyroxine to 3,5,3'-triiodothyronine (T3) is the first
step in thyroid hormone action, and the Type I iodothyronine deiodinase
supplies most of this extrathyroidal T3 in the rat. We found that the cDNA
coding for this enzyme contains an in-frame UGA encoding the rare amino
acid selenocysteine. Using site-directed mutagenesis, we have converted
selenocysteine to cysteine and expressed the wild-type and cysteine mutant
enzymes in JEG-3 cells by transient transfection. The kinetic properties of
the transiently expressed wild-type enzyme are nearly identical to those
reported for rat liver Type I deiodinase. Substitution of sulfur for
selenium causes a 10-fold increase in the Km of the enzyme for the favored
substrate 3,3',5'-triiodothyronine (rT3), a 100-fold decrease in the
sensitivity of rT3 deiodination to competitive inhibition by gold and a
300-fold increase in the apparent Ki for uncompetitive inhibition by
6-n-propylthiouracil. These results demonstrate that selenium is
responsible for the biochemical properties which characterize Type I
iodothyronine monodeiodination.
Selenocysteine confers the biochemical properties characteristic of the type I iodothyronine deiodinase
Howard Hughes Medical Institute Laboratory, Department of Medicine, Brigham and Women's Hospital, Boston, Massachusetts.
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