| EC Tree |
| 3. Hydrolases |
| 3.5 Acting on carbon-nitrogen bonds, other than peptide bonds |
| 3.5.1 In linear amides |
| ID: | 3.5.1.123 |
|---|---|
| Description: | Gamma-glutamylanilide 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 3.5.1.123 |
| BRENDA Enzyme Link: | BRENDA 3.5.1.123 |
| KEGG Enzyme Link: | KEGG3.5.1.123 |
| BioCyc Enzyme Link: | BioCyc 3.5.1.123 |
| ExPASy Enzyme Link: | ExPASy3.5.1.123 |
| EC2PDB Enzyme Link: | EC2PDB 3.5.1.123 |
| ExplorEnz Enzyme Link: | ExplorEnz 3.5.1.123 |
| PRIAM enzyme-specific profiles Link: | PRIAM 3.5.1.123 |
| IntEnz Enzyme Link: | IntEnz 3.5.1.123 |
| MEDLINE Enzyme Link: | MEDLINE 3.5.1.123 |
| MSA: | |
|---|---|
| Phylogenetic Tree: | |
| Uniprot: | |
| M-CSA: |
| RHEA:50684 | H2O + N(5)-phenyl-L-glutamine = aniline + H(+) + L-glutamate |
| RULE(radius=1) | [*:1]-[NH;+0:2]-[C;H0;+0:3](-[*:4])=[*:5].[OH2;+0:6]>>[*:4]-[C;H0;+0:3](=[*:5])-[OH;+0:6].[*:1]-[NH2;+0:2] |
| Reaction | ![]() |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Function of a glutamine synthetase-like protein in bacterial aniline oxidation via γ-glutamylanilide. | Takeo M, Ohara A, Sakae S, Okamoto Y, Kitamura C, Kato D, Negoro S | 2013 Oct | 23893114 |