| EC Tree |
| 3. Hydrolases |
| 3.5 Acting on carbon-nitrogen bonds, other than peptide bonds |
| 3.5.1 In linear amides |
| ID: | 3.5.1.94 |
|---|---|
| Description: | Gamma-glutamyl-gamma-aminobutyrate hydrolase. |
| Alternative Name: |
Gamma-glutamyl-GABA hydrolase. |
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 3.5.1.94 |
| BRENDA Enzyme Link: | BRENDA 3.5.1.94 |
| KEGG Enzyme Link: | KEGG3.5.1.94 |
| BioCyc Enzyme Link: | BioCyc 3.5.1.94 |
| ExPASy Enzyme Link: | ExPASy3.5.1.94 |
| EC2PDB Enzyme Link: | EC2PDB 3.5.1.94 |
| ExplorEnz Enzyme Link: | ExplorEnz 3.5.1.94 |
| PRIAM enzyme-specific profiles Link: | PRIAM 3.5.1.94 |
| IntEnz Enzyme Link: | IntEnz 3.5.1.94 |
| MEDLINE Enzyme Link: | MEDLINE 3.5.1.94 |
| RHEA:19737 | 4-(gamma-L-glutamylamino)butanoate + H2O = 4-aminobutanoate + L-glutamate |
| RULE(radius=1) | [*:1]-[C;H0;+0:2](=[*:3])-[NH;+0:4]-[*:5].[OH2;+0:6]>>[*:1]-[C;H0;+0:2](=[*:3])-[OH;+0:6].[*:5]-[NH2;+0:4] |
| Reaction | ![]() |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| A novel putrescine utilization pathway involves gamma-glutamylated intermediates of Escherichia coli K-12. | Kurihara S, Oda S, Kato K, Kim HG, Koyanagi T, Kumagai H, Suzuki H | 2005 Feb 11 | 15590624 |