| EC Tree |
| 3. Hydrolases |
| 3.4 Acting on peptide bonds (peptidases) |
| 3.4.19 Omega peptidases |
| ID: | 3.4.19.13 |
|---|---|
| Description: | Glutathione gamma-glutamate hydrolase. |
| Alternative Name: |
Glutathionase. Gamma-glutamyltranspeptidase. |
| Cath: | 1.10.246.130; 3.60.20.40; |
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.| UniProtKB Enzyme Link: | UniProtKB 3.4.19.13 |
| BRENDA Enzyme Link: | BRENDA 3.4.19.13 |
| KEGG Enzyme Link: | KEGG3.4.19.13 |
| BioCyc Enzyme Link: | BioCyc 3.4.19.13 |
| ExPASy Enzyme Link: | ExPASy3.4.19.13 |
| EC2PDB Enzyme Link: | EC2PDB 3.4.19.13 |
| ExplorEnz Enzyme Link: | ExplorEnz 3.4.19.13 |
| PRIAM enzyme-specific profiles Link: | PRIAM 3.4.19.13 |
| IntEnz Enzyme Link: | IntEnz 3.4.19.13 |
| MEDLINE Enzyme Link: | MEDLINE 3.4.19.13 |
| MSA: | |
|---|---|
| Phylogenetic Tree: | |
| Uniprot: | |
| M-CSA: |
| RHEA:28807 | glutathione + H2O = L-cysteinylglycine + L-glutamate |
| RULE(radius=1) | [*:1]=[C;H0;+0:2](-[*:3])-[NH;+0:4]-[*:5].[OH2;+0:6]>>[*:5]-[NH2;+0:4].[*:1]=[C;H0;+0:2](-[*:3])-[OH;+0:6] |
| Reaction | ![]() |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| gamma-Glutamyl transpeptidase GGT4 initiates vacuolar degradation of glutathione S-conjugates in Arabidopsis. | Grzam A, Martin MN, Hell R, Meyer AJ | 2007 Jul 10 | 17561001 |
| Crystal structure of the gamma-glutamyltranspeptidase precursor protein from Escherichia coli. Structural changes upon autocatalytic processing and implications for the maturation mechanism. | Okada T, Suzuki H, Wada K, Kumagai H, Fukuyama K | 2007 Jan 26 | 17135273 |
| Autocatalytic processing of gamma-glutamyltranspeptidase. | Suzuki H, Kumagai H | 2002 Nov 8 | 12207027 |
| Escherichia coli K-12 can utilize an exogenous gamma-glutamyl peptide as an amino acid source, for which gamma-glutamyltranspeptidase is essential. | Suzuki H, Hashimoto W, Kumagai H | 1993 Sep | 8104180 |
| Extracellular glutathione is a source of cysteine for cells that express gamma-glutamyl transpeptidase. | Hanigan MH, Ricketts WA | 1993 Jun 22 | 8099811 |
| Gamma-glutamyl compounds: substrate specificity of gamma-glutamyl transpeptidase enzymes. | Wickham S, West MB, Cook PF, Hanigan MH | 2011 Jul 15 | 21447318 |
| 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 |