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Flavoprotein Iodotyrosine Deiodinase Functions without Cysteine Residues
Author(s) -
Watson James A.,
McTamney Patrick M.,
Adler Jennifer M.,
Rokita Steven E.
Publication year - 2008
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.200700562
Subject(s) - diiodotyrosine , flavin group , cysteine , deiodinase , chemistry , flavoprotein , biochemistry , enzyme , redox , thyroid hormones , organic chemistry , hormone , triiodothyronine
Iodotyrosine deiodinase provides a new precedent for flavin‐dependent dehalogenation. Iodotyrosine deiodinase requires no standard redox‐active amino acid to promote reductive deiodination of diiodotyrosine despite the precedence for such residues in other enzymes that catalyze analogous reactions. Three cysteines present in the native mammalian enzyme could be removed without significant loss of catalytic activity.