EC number:3.5.1.68
Enzyme
Download| EC Tree |
| 3. Hydrolases |
| 3.5 Acting on carbon-nitrogen bonds, other than peptide bonds |
| 3.5.1 In linear amides |
| ID: | 3.5.1.68 |
|---|---|
| Description: | N-formylglutamate deformylase. |
| Alternative Name: |
Beta-citryl-L-glutamate hydrolase. |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 3.5.1.68 |
| BRENDA Enzyme Link: | BRENDA 3.5.1.68 |
| KEGG Enzyme Link: | KEGG3.5.1.68 |
| BioCyc Enzyme Link: | BioCyc 3.5.1.68 |
| ExPASy Enzyme Link: | ExPASy3.5.1.68 |
| EC2PDB Enzyme Link: | EC2PDB 3.5.1.68 |
| ExplorEnz Enzyme Link: | ExplorEnz 3.5.1.68 |
| PRIAM enzyme-specific profiles Link: | PRIAM 3.5.1.68 |
| IntEnz Enzyme Link: | IntEnz 3.5.1.68 |
| MEDLINE Enzyme Link: | MEDLINE 3.5.1.68 |
| RHEA:12476 | H2O + N-formyl-L-glutamate = formate + L-glutamate |
| RULE(radius=1) | [*:1]=[CH;+0:2]-[NH;+0:3]-[*:4].[OH2;+0:5]>>[*:4]-[NH2;+0:3].[*:1]=[CH;+0:2]-[OH;+0:5] |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| A beta-citryl-L-glutamate-hydrolysing enzyme in rat testes. | Miyake M, Innami T, Kakimoto Y | 1983 Oct 18 | 6414521 |
| Purification and properties of formylglutamate amidohydrolase from Pseudomonas putida. | Hu L, Mulfinger LM, Phillips AT | 1987 Oct | 3308850 |