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In enzymology, a diiodotyrosine transaminase (EC 2.6.1.24) is an enzyme that catalyzes the chemical reaction

3,5-diiodo-L-tyrosine + 2-oxoglutarate ${\displaystyle \rightleftharpoons }$ 4-hydroxy-3,5-diiodophenylpyruvate + L-glutamate

Thus, the two substrates of this enzyme are 3,5-diiodo-L-tyrosine and 2-oxoglutarate, whereas its two products are 4-hydroxy-3,5-diiodophenylpyruvate and L-glutamate.

This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is 3,5-diiodo-L-tyrosine:2-oxoglutarate aminotransferase. Other names in common use include diiodotyrosine aminotransferase, halogenated tyrosine aminotransferase, and halogenated tyrosine transaminase. It employs one cofactor, pyridoxal phosphate.

References

• Nakano M (January 1967). "Purification and properties of halogenated tyrosine and thyroid hormone transaminase from rat kidney mitochondria". The Journal of Biological Chemistry. 242 (1): 73–81. doi:10.1016/S0021-9258(18)96320-9. PMID 4381052.
• Nakano M, Danowski TS (April 1964). "Thyroid-hormone transaminase and oxidase in rat-kidney mitochondria". Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects. 85: 18–28. doi:10.1016/0926-6569(64)90163-4. PMID 14159298.

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