EC number:3.5.5.1
Enzyme
Download| EC Tree |
| 3. Hydrolases |
| 3.5 Acting on carbon-nitrogen bonds, other than peptide bonds |
| 3.5.5 In nitriles |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 3.5.5.1 |
| BRENDA Enzyme Link: | BRENDA 3.5.5.1 |
| KEGG Enzyme Link: | KEGG3.5.5.1 |
| BioCyc Enzyme Link: | BioCyc 3.5.5.1 |
| ExPASy Enzyme Link: | ExPASy3.5.5.1 |
| EC2PDB Enzyme Link: | EC2PDB 3.5.5.1 |
| ExplorEnz Enzyme Link: | ExplorEnz 3.5.5.1 |
| PRIAM enzyme-specific profiles Link: | PRIAM 3.5.5.1 |
| IntEnz Enzyme Link: | IntEnz 3.5.5.1 |
| MEDLINE Enzyme Link: | MEDLINE 3.5.5.1 |
| RHEA:45784 | 2 H2O + phenylpropanonitrile = 3-phenylpropanoate + NH4(+) |
| RULE(radius=1) | [*:1]-[C;H0;+0:2]#[N;H0;+0:3].[OH2;+0:4].[OH2;+0:5]>>[*:1]-[C;H0;+0:2](=[O;H0;+0:5])-[OH;+0:4].[NH3;+0:3] |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Pseudomonas syringae pv. syringae B728a hydrolyses indole-3-acetonitrile to the plant hormone indole-3-acetic acid. | Howden AJ, Rico A, Mentlak T, Miguet L, Preston GM | 2009 Nov | 19849791 |
| RHEA:45776 | (indol-3-yl)acetonitrile + 2 H2O = (indol-3-yl)acetate + NH4(+) |
| RULE(radius=1) | [*:1]-[C;H0;+0:2]#[N;H0;+0:3].[OH2;+0:4].[OH2;+0:5]>>[*:1]-[C;H0;+0:2](=[O;H0;+0:5])-[OH;+0:4].[NH3;+0:3] |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Characterization of a nitrilase and a nitrile hydratase from Pseudomonas sp. strain UW4 that converts indole-3-acetonitrile to indole-3-acetic acid. | Duca D, Rose DR, Glick BR | 2014 Aug | 24837382 |
| Pseudomonas syringae pv. syringae B728a hydrolyses indole-3-acetonitrile to the plant hormone indole-3-acetic acid. | Howden AJ, Rico A, Mentlak T, Miguet L, Preston GM | 2009 Nov | 19849791 |
| RHEA:21724 | a nitrile + 2 H2O = a carboxylate + NH4(+) |
| RULE(radius=1) | [*:1]-[C;H0;+0:2]#[N;H0;+0:3].[OH2;+0:4].[OH2;+0:5]>>[*:1]-[C;H0;+0:2](=[O;H0;+0:5])-[OH;+0:4].[NH3;+0:3] |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Cloning of a nitrilase gene from the cyanobacterium Synechocystis sp. strain PCC6803 and heterologous expression and characterization of the encoded protein. | Heinemann U, Engels D, Bürger S, Kiziak C, Mattes R, Stolz A | 2003 Aug | 12902216 |
| The nitrilase superfamily: classification, structure and function. | Pace HC, Brenner C | 2001 | 11380987 |