EC number:3.5.1.111
Enzyme
Download| EC Tree |
| 3. Hydrolases |
| 3.5 Acting on carbon-nitrogen bonds, other than peptide bonds |
| 3.5.1 In linear amides |
| ID: | 3.5.1.111 |
|---|---|
| Description: | 2-oxoglutaramate amidase. |
| Alternative Name: |
Omega-amidase. |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 3.5.1.111 |
| BRENDA Enzyme Link: | BRENDA 3.5.1.111 |
| KEGG Enzyme Link: | KEGG3.5.1.111 |
| BioCyc Enzyme Link: | BioCyc 3.5.1.111 |
| ExPASy Enzyme Link: | ExPASy3.5.1.111 |
| EC2PDB Enzyme Link: | EC2PDB 3.5.1.111 |
| ExplorEnz Enzyme Link: | ExplorEnz 3.5.1.111 |
| PRIAM enzyme-specific profiles Link: | PRIAM 3.5.1.111 |
| IntEnz Enzyme Link: | IntEnz 3.5.1.111 |
| MEDLINE Enzyme Link: | MEDLINE 3.5.1.111 |
EC number:3.5.1.111
| MSA: | |
|---|---|
| Phylogenetic Tree: | |
| Uniprot: | |
| M-CSA: |
| RHEA:32963 | 2-oxoglutaramate + H2O = 2-oxoglutarate + NH4(+) |
| RULE(radius=1) | [*:1]-[C;H0;+0:2](=[*:3])-[NH2;+0:4].[OH2;+0:5]>>[*:1]-[C;H0;+0:2](=[*:3])-[OH;+0:5].[NH3;+0:4] |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Molecular identification of omega-amidase, the enzyme that is functionally coupled with glutamine transaminases, as the putative tumor suppressor Nit2. | Jaisson S, Veiga-da-Cunha M, Van Schaftingen E | 2009 Sep | 19596042 |
| Homologous gene clusters of nicotine catabolism, including a new ω-amidase for α-ketoglutaramate, in species of three genera of Gram-positive bacteria. | Cobzaru C, Ganas P, Mihasan M, Schleberger P, Brandsch R | 2011 Apr | 21288482 |