EC number:5.4.3.11
Enzyme
Download| EC Tree |
| 5. Isomerases |
| 5.4 Intramolecular transferases |
| 5.4.3 Transferring amino groups |
| ID: | 5.4.3.11 |
|---|---|
| Description: | Phenylalanine aminomutase (D-beta-phenylalanine forming). |
| Cath: | 1.10.274.20; 1.10.275.10; 1.20.200.10; |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 5.4.3.11 |
| BRENDA Enzyme Link: | BRENDA 5.4.3.11 |
| KEGG Enzyme Link: | KEGG5.4.3.11 |
| BioCyc Enzyme Link: | BioCyc 5.4.3.11 |
| ExPASy Enzyme Link: | ExPASy5.4.3.11 |
| EC2PDB Enzyme Link: | EC2PDB 5.4.3.11 |
| ExplorEnz Enzyme Link: | ExplorEnz 5.4.3.11 |
| PRIAM enzyme-specific profiles Link: | PRIAM 5.4.3.11 |
| IntEnz Enzyme Link: | IntEnz 5.4.3.11 |
| MEDLINE Enzyme Link: | MEDLINE 5.4.3.11 |
| RHEA:34527 | L-phenylalanine = (S)-3-amino-3-phenylpropanoate |
| 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 |
|---|---|---|---|
| Stereochemistry and mechanism of a microbial phenylalanine aminomutase. | Ratnayake ND, Wanninayake U, Geiger JH, Walker KD | 2011 Jun 8 | 21561099 |