EC number:4.3.2.7
| ID: | 4.3.2.7 |
|---|---|
| Description: | Glutathione-specific gamma-glutamylcyclotransferase. |
| Alternative Name: |
Gamma-glu-GCG. |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 4.3.2.7 |
| BRENDA Enzyme Link: | BRENDA 4.3.2.7 |
| KEGG Enzyme Link: | KEGG4.3.2.7 |
| BioCyc Enzyme Link: | BioCyc 4.3.2.7 |
| ExPASy Enzyme Link: | ExPASy4.3.2.7 |
| EC2PDB Enzyme Link: | EC2PDB 4.3.2.7 |
| ExplorEnz Enzyme Link: | ExplorEnz 4.3.2.7 |
| PRIAM enzyme-specific profiles Link: | PRIAM 4.3.2.7 |
| IntEnz Enzyme Link: | IntEnz 4.3.2.7 |
| MEDLINE Enzyme Link: | MEDLINE 4.3.2.7 |
| RHEA:47724 | glutathione = 5-oxo-L-proline + L-cysteinylglycine |
| RULE(radius=1) | ([*:1]-[NH2;+0:2].[*:3]=[C;H0;+0:4](-[*:5])-[NH;+0:6]-[*:7])>>[*:7]-[NH2;+0:6].[*:3]=[C;H0;+0:4](-[*:5])-[NH;+0:2]-[*:1] |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Mammalian proapoptotic factor ChaC1 and its homologues function as γ-glutamyl cyclotransferases acting specifically on glutathione. | Kumar A, Tikoo S, Maity S, Sengupta S, Sengupta S, Kaur A, Bachhawat AK | 2012 Dec | 23070364 |