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Updated: Jan 24, 2026

Author Spotlight: Developing Tools to Tune the Activity of Tyrosine Phosphatases
Published on: September 6, 2024
Effect of the phosphonic analogue of tyrosine on tyrosine iodination
A Iron1, E Neuzil, A Cassaigne
1Département de Biochimie Médicale et Biologie Moléculaire, Université de Bordeaux 2, 146, rue Léo-Saignat, F-33076, Bordeaux Cedex, France.
Abstract:
Depositing ofDL-1-amino-2-(p-hydroxyphenyl)-ethylphosphonic acid (Tyr-P) on the chicken embryo induced a dose dependent decrease of the iodine uptake by the embryonic thyroid. Tyr-P interfered on iodination of tyrosine when tested with hog thyroid peroxidase (TPO) and with bovine lactoperoxidase (LPO); the analogue was recognized by the two enzymes but its affinity for TPO and LPO was respectively 3 and 7 fold higher compared with that of the natural substrate, suggesting that Tyr-P may act as an iodine trap.
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