Catalysis leads to posttranslational inactivation of the type 1 deiodinase and alters its conformation

Previously, it was shown that the type 1 deiodinase (D1) is subject to substrate-dependent inactivation that is blocked by pretreatment with the inhibitor of D1 catalysis, propylthiouracil (PTU). Using HepG2 cells with endogenous D1 activity, we found that while considerable D1-mediated catalysis of...

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Veröffentlicht in:	Journal of endocrinology 2012-07, Vol.214 (1), p.87-94
Hauptverfasser:	Zhu, Bo, Shrivastava, Ashutosh, Luongo, Cristina, Chen, Ting, Harney, John W, Marsili, Alessandro, Tran, Thuy-Van, Bhadouria, Anulika, Mopala, Radhika, Steen, Amanda I, Larsen, P Reed, Zavacki, Ann Marie
Format:	Artikel
Sprache:	eng
Schlagworte:	Biocatalysis - drug effects Biological and medical sciences Dose-Response Relationship, Drug Enzyme Activation - drug effects Fluorescence Resonance Energy Transfer Fundamental and applied biological sciences. Psychology HEK293 Cells Hep G2 Cells Humans Iodide Peroxidase - chemistry Iodide Peroxidase - genetics Iodide Peroxidase - metabolism Luciferases - genetics Luciferases - metabolism Luminescent Proteins - genetics Luminescent Proteins - metabolism Mutation Propylthiouracil - pharmacology Protein Conformation Protein Multimerization Protein Processing, Post-Translational - drug effects Regular papers Reverse Transcriptase Polymerase Chain Reaction Sonication Substrate Specificity Triiodothyronine - metabolism Triiodothyronine - pharmacology Vertebrates: endocrinology
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