EC number:3.5.3.24
Enzyme
Download| EC Tree |
| 3. Hydrolases |
| 3.5 Acting on carbon-nitrogen bonds, other than peptide bonds |
| 3.5.3 In linear amidines |
| ID: | 3.5.3.24 |
|---|---|
| Description: | N(1)-aminopropylagmatine ureohydrolase. |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 3.5.3.24 |
| BRENDA Enzyme Link: | BRENDA 3.5.3.24 |
| KEGG Enzyme Link: | KEGG3.5.3.24 |
| BioCyc Enzyme Link: | BioCyc 3.5.3.24 |
| ExPASy Enzyme Link: | ExPASy3.5.3.24 |
| EC2PDB Enzyme Link: | EC2PDB 3.5.3.24 |
| ExplorEnz Enzyme Link: | ExplorEnz 3.5.3.24 |
| PRIAM enzyme-specific profiles Link: | PRIAM 3.5.3.24 |
| IntEnz Enzyme Link: | IntEnz 3.5.3.24 |
| MEDLINE Enzyme Link: | MEDLINE 3.5.3.24 |
| RHEA:35827 | H2O + N(1)-aminopropylagmatine = spermidine + urea |
| RULE(radius=1) | [*:1]-[C;H0;+0:2](=[NH;+0:3])-[NH;+0:4]-[*:5].[OH2;+0:6]>>[*:1]-[C;H0;+0:2](-[NH2;+0:3])=[O;H0;+0:6].[*:5]-[NH2;+0:4] |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| N1-aminopropylagmatine, a new polyamine produced as a key intermediate in polyamine biosynthesis of an extreme thermophile, Thermus thermophilus. | Ohnuma M, Terui Y, Tamakoshi M, Mitome H, Niitsu M, Samejima K, Kawashima E, Oshima T | 2005 Aug 26 | 15983049 |
| Dual biosynthesis pathway for longer-chain polyamines in the hyperthermophilic archaeon Thermococcus kodakarensis. | Morimoto N, Fukuda W, Nakajima N, Masuda T, Terui Y, Kanai T, Oshima T, Imanaka T, Fujiwara S | 2010 Oct | 20675472 |