EC number:3.5.4.42
Enzyme
Download| EC Tree |
| 3. Hydrolases |
| 3.5 Acting on carbon-nitrogen bonds, other than peptide bonds |
| 3.5.4 In cyclic amidines |
| ID: | 3.5.4.42 |
|---|---|
| Description: | N-isopropylammelide isopropylaminohydrolase. |
| Cath: | 3.20.20.140; 2.30.40.10; |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 3.5.4.42 |
| BRENDA Enzyme Link: | BRENDA 3.5.4.42 |
| KEGG Enzyme Link: | KEGG3.5.4.42 |
| BioCyc Enzyme Link: | BioCyc 3.5.4.42 |
| ExPASy Enzyme Link: | ExPASy3.5.4.42 |
| EC2PDB Enzyme Link: | EC2PDB 3.5.4.42 |
| ExplorEnz Enzyme Link: | ExplorEnz 3.5.4.42 |
| PRIAM enzyme-specific profiles Link: | PRIAM 3.5.4.42 |
| IntEnz Enzyme Link: | IntEnz 3.5.4.42 |
| MEDLINE Enzyme Link: | MEDLINE 3.5.4.42 |
| RHEA:23608 | H(+) + H2O + N-isopropylammelide = cyanurate + isopropylamine |
| RULE(radius=1) | [*:1]-[NH;+0:2]-[c;H0;+0:3](:[*:4]):[*:5].[H+;H0:6].[OH2;+0:7]>>[*:1]-[NH2;+0:2].[*:4]:[c;H0;+0:3](:[*:5])-[OH;+0:7] |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| AtzC is a new member of the amidohydrolase protein superfamily and is homologous to other atrazine-metabolizing enzymes. | Sadowsky MJ, Tong Z, de Souza M, Wackett LP | 1998 Jan | 9422605 |
| X-Ray Structure and Mutagenesis Studies of the N-Isopropylammelide Isopropylaminohydrolase, AtzC. | Balotra S, Warden AC, Newman J, Briggs LJ, Scott C, Peat TS | 2015 | 26390431 |
| Purification, substrate range, and metal center of AtzC: the N-isopropylammelide aminohydrolase involved in bacterial atrazine metabolism. | Shapir N, Osborne JP, Johnson G, Sadowsky MJ, Wackett LP | 2002 Oct | 12218024 |