3-Iodotyrosine
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3-Iodotyrosine

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3-Iodotyrosine is an inhibitor of tyrosine hydroxylase (Ki = 0.39 µM) and an intermediate in the synthesis of thyroid hormones.

Category
L-Amino Acids
Catalog number
BAT-008130
CAS number
70-78-0
Molecular Formula
C9H10INO3
Molecular Weight
307.09
3-Iodotyrosine
IUPAC Name
(2S)-2-amino-3-(4-hydroxy-3-iodophenyl)propanoic acid
Synonyms
Monoiodotyrosine; NSC 210787; L-Tyrosine, 3-iodo-
Related CAS
3078-39-5
Appearance
White to off-white powder
Purity
≥95%
Density
1.944 g/cm3
Melting Point
~ 205 °C
Boiling Point
391°C at 760 mmHg
Storage
Store at-20 °C
Solubility
3 mg/mL
InChI
InChI=1S/C9H10INO3/c10-6-3-5(1-2-8(6)12)4-7(11)9(13)14/h1-3,7,12H,4,11H2,(H,13,14)/t7-/m0/s1
InChI Key
UQTZMGFTRHFAAM-ZETCQYMHSA-N
Canonical SMILES
C1=CC(=C(C=C1CC(C(=O)O)N)I)O
1. Associative learning in larval and adult Drosophila is impaired by the dopamine-synthesis inhibitor 3-Iodo-L-tyrosine
Christian König, Juliane Thoener, Aliće Weiglein, Naoko Toshima, Nino Mancini, Fatima Amin, Michael Schleyer Biol Open . 2021 Jun 15;10(6):bio058198. doi: 10.1242/bio.058198.
Across the animal kingdom, dopamine plays a crucial role in conferring reinforcement signals that teach animals about the causal structure of the world. In the fruit fly Drosophila melanogaster, dopaminergic reinforcement has largely been studied using genetics, whereas pharmacological approaches have received less attention. Here, we apply the dopamine-synthesis inhibitor 3-Iodo-L-tyrosine (3IY), which causes acute systemic inhibition of dopamine signaling, and investigate its effects on Pavlovian conditioning. We find that 3IY feeding impairs sugar-reward learning in larvae while leaving task-relevant behavioral faculties intact, and that additional feeding of a precursor of dopamine (L-3,4-dihydroxyphenylalanine, L-DOPA), rescues this impairment. Concerning a different developmental stage and for the aversive valence domain. Moreover, we demonstrate that punishment learning by activating the dopaminergic neuron PPL1-γ1pedc in adult flies is also impaired by 3IY feeding, and can likewise be rescued by L-DOPA. Our findings exemplify the advantages of using a pharmacological approach in combination with the genetic techniques available in D. melanogaster to manipulate neuronal and behavioral function.
2. Genetic encoding of 3-iodo-L-tyrosine in Escherichia coli for single-wavelength anomalous dispersion phasing in protein crystallography
Takatsugu Kobayashi, Seiki Kuramitsu, Kazutaka Murayama, Fumie Iraha, Kenji Oki, Shigeyuki Yokoyama, Miyuki Kato-Murayama, Mikako Shirouzu, Kensaku Sakamoto, Kazumasa Ohtake, Masahiro Takahashi Structure . 2009 Mar 11;17(3):335-44. doi: 10.1016/j.str.2009.01.008.
We developed an Escherichia coli cell-based system to generate proteins containing 3-iodo-L-tyrosine at desired sites, and we used this system for structure determination by single-wavelength anomalous dispersion (SAD) phasing with the strong iodine signal. Tyrosyl-tRNA synthetase from Methanocaldococcus jannaschii was engineered to specifically recognize 3-iodo-L-tyrosine. The 1.7 A crystal structure of the engineered variant, iodoTyrRS-mj, bound with 3-iodo-L-tyrosine revealed the structural basis underlying the strict specificity for this nonnatural substrate; the iodine moiety makes van der Waals contacts with 5 residues at the binding pocket. E. coli cells expressing iodoTyrRS-mj and the suppressor tRNA were used to incorporate 3-iodo-L-tyrosine site specifically into the ribosomal protein N-acetyltransferase from Thermus thermophilus. The crystal structure of this enzyme with iodotyrosine was determined at 1.8 and 2.2 Angstroms resolutions by SAD phasing at CuK alpha and CrK alpha wavelengths, respectively. The native structure, determined by molecular replacement, revealed no significant structural distortion caused by iodotyrosine incorporation.
3. Update on intrathyroidal iodine metabolism
J T Dunn, A D Dunn Thyroid . 2001 May;11(5):407-14. doi: 10.1089/105072501300176363.
The thyroid concentrates iodide from the serum and oxidizes it at the apical membrane, attaching it to tyrosyl residues within thyroglobulin (Tg) to make diiodotyrosine and monoiodotyrosine. Major players in this process are Tg, thyroperoxidase (TPO), hydrogen peroxide, pendrin, and nicotinamide adenine dinucleotide phosphate (NADPH). Further action of TPO, hydrogen peroxide (H2O2), and iodinated Tg produce thyroxine (T4) and triiodothyronine (T3). Hormone-containing Tg is stored in the follicular lumen, then processed, most commonly by micropinocytosis. The lysosomal enzymes cathepsins B, L, and D are active in Tg proteolysis. Tg digestion leaves T4 and T3 intact, to be released from the cell, while the 3,5'-diiodotyrosine (DIT) and 3-iodotyrosine (MIT) are retained and deiodinated for recycling within the thyroid. Some areas of especially active recent research include: (1) the role of molecular chaperones in directing properly folded TPO and Tg to the apical membrane; (2) details of proteolytic pathways; (3) modulation of iodine metabolism, not only by thyrotropin (TSH) but by iodine supply and by feedback effects of Tg, glutathione, and inhibitory elements in the N-terminal region of Tg; and (4) details of Tg structure and iodotyrosyl coupling. Despite general agreement on the major steps in intrathyroidal iodine metabolism, new details of mechanisms are constantly being uncovered and are greatly improving understanding of the overall process.
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