Deiodinase refers to a family of enzymes that are essential for the activation and inactivation of thyroid hormones by selectively removing iodine atoms from the thyronine molecule. These enzymes are pivotal in regulating the local concentration of the biologically active hormone, triiodothyronine (T3), within specific tissues, irrespective of circulating thyroid-stimulating hormone (TSH) or thyroxine (T4) levels. Clinically, deiodinase activity is a key determinant of thyroid hormone action and tissue-specific metabolism, playing a central role in energy expenditure, thermogenesis, and growth. Understanding their function is vital for interpreting thyroid health beyond simple blood tests.
Origin
The term is a scientific compound word combining the chemical action “deiodin-” (removing iodine) with the suffix “-ase,” which is the standard nomenclature for an enzyme. This name accurately describes the catalytic function of this group of proteins. Deiodinases were identified as the critical regulatory points where the relatively inactive T4 precursor is converted into the potent T3 hormone or into the inactive reverse T3 (rT3) metabolite.
Mechanism
There are three main types of deiodinases: Type 1 (D1), Type 2 (D2), and Type 3 (D3), each exhibiting distinct tissue distribution and functional roles. D1 and D2 primarily catalyze the removal of an iodine atom from the outer ring of T4, converting it into the highly active T3, thus acting as activating enzymes. Conversely, D3 is the primary inactivating enzyme, removing an iodine atom from the inner ring to produce the metabolically inert reverse T3. The localized and regulated expression of these enzymes allows different organs, such as the brain, liver, and muscle, to precisely fine-tune their cellular response to thyroid signals based on specific physiological needs or metabolic demands.
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