EC number:5.3.3.7
| ID: | 5.3.3.7 |
|---|---|
| Description: | Aconitate Delta-isomerase. |
| Alternative Name: |
Aconitate isomerase. |
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 5.3.3.7 |
| BRENDA Enzyme Link: | BRENDA 5.3.3.7 |
| KEGG Enzyme Link: | KEGG5.3.3.7 |
| BioCyc Enzyme Link: | BioCyc 5.3.3.7 |
| ExPASy Enzyme Link: | ExPASy5.3.3.7 |
| EC2PDB Enzyme Link: | EC2PDB 5.3.3.7 |
| ExplorEnz Enzyme Link: | ExplorEnz 5.3.3.7 |
| PRIAM enzyme-specific profiles Link: | PRIAM 5.3.3.7 |
| IntEnz Enzyme Link: | IntEnz 5.3.3.7 |
| MEDLINE Enzyme Link: | MEDLINE 5.3.3.7 |
| RHEA:17265 | trans-aconitate = cis-aconitate |
| RULE(radius=1) | |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Mechanism of the aconitate isomerase reaction. | Klinman JP, Rose IA | 1971 Jun 8 | 5114988 |
| Purification and kinetic properties of aconitate isomerase from Pseudomonas putida. | Klinman JP, Rose IA | 1971 Jun 8 | 5114987 |
| Enzymatic characterization and gene identification of aconitate isomerase, an enzyme involved in assimilation of trans-aconitic acid, from Pseudomonas sp. WU-0701. | Yuhara K, Yonehara H, Hattori T, Kobayashi K, Kirimura K | 2015 Nov | 26293748 |