Tyrosine 2,3-aminomutase
| tyrosine 2,3-aminomutase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 5.4.3.6 | ||||||||
| CAS no. | 9073-38-5 | ||||||||
| 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 tyrosine 2,3-aminomutase (EC 5.4.3.6) is an enzyme that catalyzes the chemical reaction[1]
- L-tyrosine 3-amino-3-(4-hydroxyphenyl)propanoate
Hence, this enzyme has one substrate, L-tyrosine, and one product, 3-amino-3-(4-hydroxyphenyl)propanoate.
This enzyme belongs to the family of isomerases, specifically those intramolecular transferases transferring amino groups. The systematic name of this enzyme class is L-tyrosine 2,3-aminomutase. This enzyme is also called tyrosine alpha,beta-mutase. This enzyme participates in tyrosine metabolism. It employs one cofactor, 5-methylene-3,5-dihydroimidazol-4-one (MIO) which is formed autocatalytic rearrangement of the internal tripeptide Ala-Ser-Gly.
Structural studies[edit]
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 2OHY.
References[edit]
- ^ Kurylo-Borowska Z, Abramsky T (1972). "Biosynthesis of β-tyrosine". Biochim. Biophys. Acta. 264 (1): 1–10. doi:10.1016/0304-4165(72)90110-9. PMID 5021987.
