EC number:5.4.3.6
Enzyme
Download| EC Tree |
| 5. Isomerases |
| 5.4 Intramolecular transferases |
| 5.4.3 Transferring amino groups |
| ID: | 5.4.3.6 |
|---|---|
| Description: | Tyrosine 2,3-aminomutase. |
| Alternative Name: |
Tyrosine alpha,beta-mutase. |
| Cath: | 1.10.275.10; 1.20.200.10; |
3D structure
Click one PDB to see exact 3D structure provided by NGL.
Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.References
External Links
| UniProtKB Enzyme Link: | UniProtKB 5.4.3.6 |
| BRENDA Enzyme Link: | BRENDA 5.4.3.6 |
| KEGG Enzyme Link: | KEGG5.4.3.6 |
| BioCyc Enzyme Link: | BioCyc 5.4.3.6 |
| ExPASy Enzyme Link: | ExPASy5.4.3.6 |
| EC2PDB Enzyme Link: | EC2PDB 5.4.3.6 |
| ExplorEnz Enzyme Link: | ExplorEnz 5.4.3.6 |
| PRIAM enzyme-specific profiles Link: | PRIAM 5.4.3.6 |
| IntEnz Enzyme Link: | IntEnz 5.4.3.6 |
| MEDLINE Enzyme Link: | MEDLINE 5.4.3.6 |
| RHEA:15781 | L-tyrosine = 3-amino-3-(4-hydroxyphenyl)propanoate |
| RULE(radius=1) | [*:1]-[CH;+0:2](-[NH2;+0:3])-[CH2;+0:4]-[*:5]>>[*:1]-[CH2;+0:2]-[CH;+0:4](-[*:5])-[NH2;+0:3] |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| A bacterial tyrosine aminomutase proceeds through retention or inversion of stereochemistry to catalyze its isomerization reaction. | Wanninayake U, Walker KD | 2013 Jul 31 | 23800193 |
| Probing the active site of MIO-dependent aminomutases, key catalysts in the biosynthesis of beta-amino acids incorporated in secondary metabolites. | Cooke HA, Bruner SD | 2010 Sep | 20577998 |
| Discovery of additional members of the tyrosine aminomutase enzyme family and the mutational analysis of CmdF. | Krug D, Müller R | 2009 Mar 2 | 19222035 |