EC number:2.3.2.2
| ID: | 2.3.2.2 |
|---|---|
| Description: | Gamma-glutamyltransferase. |
| Alternative Name: |
Glutamyl transpeptidase. Gamma-glutamyltranspeptidase. Gamma-glutamyl transpeptidase. |
| Prosite: | PDOC00404; |
| PDB: |
» show all » hide |
| Cath: | 1.10.246.130; 3.60.20.40; |
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 2.3.2.2 |
| BRENDA Enzyme Link: | BRENDA 2.3.2.2 |
| KEGG Enzyme Link: | KEGG2.3.2.2 |
| BioCyc Enzyme Link: | BioCyc 2.3.2.2 |
| ExPASy Enzyme Link: | ExPASy2.3.2.2 |
| EC2PDB Enzyme Link: | EC2PDB 2.3.2.2 |
| ExplorEnz Enzyme Link: | ExplorEnz 2.3.2.2 |
| PRIAM enzyme-specific profiles Link: | PRIAM 2.3.2.2 |
| IntEnz Enzyme Link: | IntEnz 2.3.2.2 |
| MEDLINE Enzyme Link: | MEDLINE 2.3.2.2 |
| RHEA:23904 | an alpha-amino acid + an N-terminal (5-L-glutamyl)-[peptide] = 5-L-glutamyl amino acid + a [peptide] N-terminus |
| 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 |
|---|---|---|---|
| Autoprocessing of Helicobacter pylori gamma-glutamyltranspeptidase leads to the formation of a threonine-threonine catalytic dyad. | Boanca G, Sand A, Okada T, Suzuki H, Kumagai H, Fukuyama K, Barycki JJ | 2007 Jan 5 | 17107958 |
| Crystal structures of gamma-glutamyltranspeptidase from Escherichia coli, a key enzyme in glutathione metabolism, and its reaction intermediate. | Okada T, Suzuki H, Wada K, Kumagai H, Fukuyama K | 2006 Apr 25 | 16618936 |