Iodine peroxidase

Iodide is the compound in which iodine is present in the -1 oxidation state and which is easily absorbed from the gastrointestinal tract and distributed to extracellular water in the human body. It is also in this form that it is pushed into the cells of the thyroid gland. Once inside the cell, it is activated by iodine peroxidase for the eventual synthesis of thyroxin. Since iodine is easily oxidized to elemental iodine, use of this form of iodine in foods could result in a change of color and affect organoleptic properties. The other commonly used form of iodine for fortification purposes is iodate, a form in which the element is present in the -I- 5 oxidation state. While this form is stable in various foods and is bioavailable (after being reduced to... 

Thiocyanate ion, SCN , inhibits formation of thyroid hormones by inhibiting the iodination of tyrosine residues in thyroglobufin by thyroid peroxidase. This ion is also responsible for the goitrogenic effect of cassava (manioc, tapioca). Cyanide, CN , is liberated by hydrolysis from the cyanogenic glucoside finamarin it contains, which in turn is biodetoxified to SCN. 

Isoflavones have been implicated in goiter induction. Soybean extracts inhibit reactions catalyzed by thyroid peroxidase (TPO), essential to the synthesis of thyroid hormones (Divi et al., 1997). Genistein and daidzein (at about 1-10 p,M of IC50) may act as alternative substrates for tyrosine iodination (Divi et al., 1997). Furthermore, genistein and daidzein have also been shown to cause the irreversible inactivation of TPO in the presence of hydrogen peroxide. Genistein also inhibits thyroxine synthesis in the presence of iodinated... 

Another important example of catalytic oxidation of inorganic compounds by peroxidases is the catalysis of iodide oxidation by TPO. TPO is involved in the biosynthesis of thyroid hormone and catalyzes the reactions of iodination and coupling in the thyroid gland. Magnusson et al. [215] considered two possible pathways of iodination the formation of enzyme-bound hypoiodite and the formation of free hypoiodide (Reactions (17) and (18)) ... 

Taurog et al. [216] showed that contrary to previous suggestions, both iodination and coupling are catalyzed by the oxoferryl porphyrin Tr-cation radical of TPO Compound I and not the oxoferryl protein radical. HRP catalyzed the oxidation of bisulfite to sulfate with the intermediate formation of sulfur trioxide radical anion S03 [217] HPO, MPO, LPO, chloroperoxidase, NADH peroxidase, and methemoglobin oxidized cyanide to cyanyl radical [218],... 

The answer is c. (Katzung, pp 651-652.) Propylthiouracil is a thioamide that interferes with the production of thyroid hormone. Its primary action is prevention of thyroid hormone synthesis by blocking thyroid peroxidase catalysis leading to interference with iodine organification. 

The concentration of Li+ in the thyroid is three to four times that in serum [179]. It is thought that Li+ may be concentrated in the thyroid gland by a mechanism similar to the incorporation of iodide, I-, resulting in competition between Li+ and I the levels of intracellular 1 decrease when those of Li+ increase, and vice versa [182]. Li+ inhibits both the ability of the gland to accumulate 1 and the release of iodine from the gland. In vitro, Li+ has no effect on thyroid peroxidase, the enzyme that catalyzes the incorporation of I" into tyrosyl residues leading to thyroidal hormone synthesis, but does increase the activity of iodotyrosine-deio-dinase, which catalyzes the reductive deiodination of iodotyrosyls, thus maintaining the levels of intracellular I [182]. The increase in iodoty-rosine-deiodinase activity is probably a response to the Li+-induced decrease in the concentration of thyroidal I". Li+ has no effect on the conversion of thyroxine to triiodothyronine. The overall effect of this competition between Li+ and 1 is, therefore, reduced levels of thyroid hormone in the presence of Li+. 

The iodinated tyrosine residues monoiodotyrosine (MIT) and diiodoty-rosine (DIT) combine (couple) to form iodothyronines in reactions catalyzed by thyroid peroxidase. Thus, two molecules of DIT combine to form T4, and MIT and DIT join to form T3. 

Thyroiditis/hypothyroidism 4600 83 % 17 alpha-hydroxylase, thyroid peroxidase Iodine... 

Thyroxine synthesis begins when iodide (I-) is transferred from the blood stream to the thyroid follicle cell by an active ATP-driven membrane pump mechanism this process is stimulated by cAMP following TSH stimulation of the gland. Iodide is transported through the follicular cell and secreted into the lumen of the follicle where it is oxidized to iodine and incorporated in to tyrosine residues by the enzyme thyroid peroxidase (TPO). 

Thyroid peroxidase (TPO) oxidises iodide and incorporates iodine into tyrosine residues within Tgb. 

This enzyme [EC 1.11.1.10], also called chloride peroxidase, catalyzes the reaction of hydrogen peroxide with two RH and two Cl to produce two R—Cl and two water molecules. A heme group is one of the cofactors. This enzyme can also catalyze bromination and iodin-ation, but not fluorination. 

This enzyme [EC 1.11.1.8], also known as iodotyrosine deiodase, iodinase, and thyroid peroxidase, catalyzes the reaction of iodide with hydrogen peroxide to produce iodine and two water. The cofactor for this enzyme is heme. M. Morrison (1970) Meth. Enzymol. 17A, 653 and 658. 

Thioamides are reducing agents. They inhibit thyroid hormone synthesis by inhibiting the peroxidase enzymatic system, which catalyzes oxidation of iodide ions and iodine that are consumed in food, which is necessary for iodination of tyrosine derivatives. Thus they reduce the concentration of free iodine necessary to react with tyrosine derivatives, and they can also block oxidative addition reactions of mono- and diiodtyrosines, which form L-thyroxine and L-triiodothyronin. 

This drug has a pronounced thyrostatic effect and canses reduced thyroxine synthesis in the thyroid gland. It inhibits the process of iodination of thyroglobnUn, reduces formation of the active form of iodine in the thyroid gland, and blocks the peroxidase system. Propylthionracil is nsed for hyperthyrosis, thyrotoxic crises, and on thyrodectomia. Synonyms of this dmg are propycil and tireostat. 

The available agents with antithyroid activity are the thioamides propylthiouracil, carbimazole and methimazole also known as thiamazole. Their thio-carbamide group is indispensable for antithyroid activity. The mechanism of action is complex. The most important action is the prevention of hormone synthesis by an inhibition of the thyroid peroxidase-catalyzed reactions involved in iodine organification. These agents also block the coupling of the iodoty-rosines. 

As indicator enzymes horseradish peroxidase (HRP or HRPO), alkaline phosphatase (AP), or /i-galactosidase, are favored, since they are relatively robust, have a high product-forming rate, are easy to purify, and are cheap. The most used colloids are from gold, silver, and iron, and iodine isotopes are mostly taken as radioactive labels in immunoassays. 

Diets rich in millet have been associated with endemic goiter in parts of West Africa where millet is a staple. The damage has been attributed to vitexin, a C-glycosyl flavone, that in rats has antithyroid activity and that in vitro inhibits thyroid peroxidase and the free radical iodination step in thyroid hormone biosynthesis. Isoflavones have produced similar antithyroid effects in rats, but clinical studies in adults have not. " However, this remains a possible concern in infants fed soya-based milk-replacers, especially if iodine supply is compromised. 

Although toxicity from isoflavones may arise from their action as alternative substrates for the enzyme thyroid peroxidase and people in southeast Asia would be protected by the dietary inclusion of iodine-rich seaweed products, a recent study has shown that isoflavone supplements do not affect thyroid function in iodine-replete postmenopausal women. Considerations of the safety of soy isoflavones is an area of great interest in relation to their potential benefits to human health and has recently been comprehensively reviewed. ... 

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