EC number:3.5.99.8
Enzyme
Download| EC Tree |
| 3. Hydrolases |
| 3.5 Acting on carbon-nitrogen bonds, other than peptide bonds |
| 3.5.99 In other compounds |
| ID: | 3.5.99.8 |
|---|---|
| Description: | 5-nitroanthranilic acid aminohydrolase. |
| Alternative Name: |
5NAA deaminase. |
| Cath: | 3.30.70.360; 3.40.630.10; |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 3.5.99.8 |
| BRENDA Enzyme Link: | BRENDA 3.5.99.8 |
| KEGG Enzyme Link: | KEGG3.5.99.8 |
| BioCyc Enzyme Link: | BioCyc 3.5.99.8 |
| ExPASy Enzyme Link: | ExPASy3.5.99.8 |
| EC2PDB Enzyme Link: | EC2PDB 3.5.99.8 |
| ExplorEnz Enzyme Link: | ExplorEnz 3.5.99.8 |
| PRIAM enzyme-specific profiles Link: | PRIAM 3.5.99.8 |
| IntEnz Enzyme Link: | IntEnz 3.5.99.8 |
| MEDLINE Enzyme Link: | MEDLINE 3.5.99.8 |
| RHEA:28166 | 5-nitroanthranilate + H(+) + H2O = 5-nitrosalicylate + NH4(+) |
| RULE(radius=1) | [*:1]:[c;H0;+0:2](:[*:3])-[NH2;+0:4].[H+;H0:5].[OH2;+0:6]>>[*:1]:[c;H0;+0:2](:[*:3])-[OH;+0:6].[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 and biochemical characterization of the 5-nitroanthranilic acid degradation pathway in Bradyrhizobium sp. strain JS329. | Qu Y, Spain JC | 2011 Jun | 21498645 |
| Biodegradation of 5-nitroanthranilic acid by Bradyrhizobium sp. strain JS329. | Qu Y, Spain JC | 2010 Mar | 20081004 |