EC number:5.1.99.8
| ID: | 5.1.99.8 |
|---|---|
| Description: | 7,8-dihydroneopterin epimerase. |
| Cath: | 3.20.20.20; 3.30.1130.10; 3.30.1300.20; 3.30.70.560; |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 5.1.99.8 |
| BRENDA Enzyme Link: | BRENDA 5.1.99.8 |
| KEGG Enzyme Link: | KEGG5.1.99.8 |
| BioCyc Enzyme Link: | BioCyc 5.1.99.8 |
| ExPASy Enzyme Link: | ExPASy5.1.99.8 |
| EC2PDB Enzyme Link: | EC2PDB 5.1.99.8 |
| ExplorEnz Enzyme Link: | ExplorEnz 5.1.99.8 |
| PRIAM enzyme-specific profiles Link: | PRIAM 5.1.99.8 |
| IntEnz Enzyme Link: | IntEnz 5.1.99.8 |
| MEDLINE Enzyme Link: | MEDLINE 5.1.99.8 |
| RHEA:45328 | 7,8-dihydroneopterin = 7,8-dihydromonapterin |
| RULE(radius=1) | |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Biosynthesis of pteridines in Escherichia coli. Structural and mechanistic similarity of dihydroneopterin-triphosphate epimerase and dihydroneopterin aldolase. | Haussmann C, Rohdich F, Schmidt E, Bacher A, Richter G | 1998 Jul 10 | 9651328 |
| One substrate, five products: reactions catalyzed by the dihydroneopterin aldolase from Mycobacterium tuberculosis. | Czekster CM, Blanchard JS | 2012 Dec 5 | 23150985 |