EC number:4.3.2.8
| ID: | 4.3.2.8 |
|---|---|
| Description: | Gamma-glutamylamine cyclotransferase. |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 4.3.2.8 |
| BRENDA Enzyme Link: | BRENDA 4.3.2.8 |
| KEGG Enzyme Link: | KEGG4.3.2.8 |
| BioCyc Enzyme Link: | BioCyc 4.3.2.8 |
| ExPASy Enzyme Link: | ExPASy4.3.2.8 |
| EC2PDB Enzyme Link: | EC2PDB 4.3.2.8 |
| ExplorEnz Enzyme Link: | ExplorEnz 4.3.2.8 |
| PRIAM enzyme-specific profiles Link: | PRIAM 4.3.2.8 |
| IntEnz Enzyme Link: | IntEnz 4.3.2.8 |
| MEDLINE Enzyme Link: | MEDLINE 4.3.2.8 |
| RHEA:16961 | epsilon-(gamma-L-glutamyl)-L-lysine = 5-oxo-L-proline + L-lysine |
| RULE(radius=1) | ([*:1]-[NH2;+0:2].[*:3]-[NH;+0:4]-[C;H0;+0:5](-[*:6])=[*:7])>>[*:3]-[NH2;+0:4].[*:1]-[NH;+0:2]-[C;H0;+0:5](-[*:6])=[*:7] |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| gamma-Glutamylamine cyclotransferase: specificity toward epsilon-(L-gamma-glutamyl)-L-lysine and related compounds. | Fink ML, Chung SI, Folk JE | 1980 Aug | 6107907 |
| Identification and characterization of gamma-glutamylamine cyclotransferase, an enzyme responsible for gamma-glutamyl-epsilon-lysine catabolism. | Oakley AJ, Coggan M, Board PG | 2010 Mar 26 | 20110353 |