| diiodotyrosine transaminase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.6.1.24 | ||||||||
| CAS no. | 9033-18-5 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
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 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. 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.
| diiodotyrosine transaminase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.6.1.24 | ||||||||
| CAS no. | 9033-18-5 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
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 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. 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.