| EC Tree |
| 1. Oxidoreductases |
| 1.5 Acting on the CH-NH group of donors |
| 1.5.3 With oxygen as acceptor |
| ID: | 1.5.3.15 |
|---|---|
| Description: | N(8)-acetylspermidine oxidase (propane-1,3-diamine-forming). |
| Cath: | 3.50.50.60; 3.90.660.10; |
Click one PDB to see exact 3D structure provided by NGL.
Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.| UniProtKB Enzyme Link: | UniProtKB 1.5.3.15 |
| BRENDA Enzyme Link: | BRENDA 1.5.3.15 |
| KEGG Enzyme Link: | KEGG1.5.3.15 |
| BioCyc Enzyme Link: | BioCyc 1.5.3.15 |
| ExPASy Enzyme Link: | ExPASy1.5.3.15 |
| EC2PDB Enzyme Link: | EC2PDB 1.5.3.15 |
| ExplorEnz Enzyme Link: | ExplorEnz 1.5.3.15 |
| PRIAM enzyme-specific profiles Link: | PRIAM 1.5.3.15 |
| IntEnz Enzyme Link: | IntEnz 1.5.3.15 |
| MEDLINE Enzyme Link: | MEDLINE 1.5.3.15 |
| RHEA:25972 | H2O + N(8)-acetylspermidine + O2 = 4-acetamidobutanal + H2O2 + propane-1,3-diamine |
| RULE(radius=1) | [*:1]-[CH2;+0:2]-[NH;+0:3]-[*:4].[O;H0;+0:5]=[O;H0;+0:6].[OH2;+0:7]>>[*:1]-[CH;+0:2]=[O;H0;+0:7].[*:4]-[NH2;+0:3].[OH;+0:5]-[OH;+0:6] |
| Reaction | ![]() |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Polyamine oxidase from Acanthamoeba culbertsoni specific for N8-acetylspermidine. | Shukla OP, Müller S, Walter RD | 1992 Mar | 1565141 |
| Yeast Fms1 is a FAD-utilizing polyamine oxidase. | Landry J, Sternglanz R | 2003 Apr 11 | 12670477 |
| RHEA:25864 | H2O + N(1)-acetylspermidine + O2 = 4-acetamidobutanal + H2O2 + propane-1,3-diamine |
| RULE(radius=1) | ([*:1]-[C;H0;+0:2](=[*:3])-[NH;+0:4]-[*:5].[*:6]-[NH2;+0:7].[*:8]-[NH;+0:9]-[CH2;+0:10]-[*:11]).[O;H0;+0:12]=[O;H0;+0:13].[OH2;+0:14]>>([*:11]-[CH;+0:10]=[O;H0;+0:14].[*:6]-[NH;+0:7]-[C;H0;+0:2](-[*:1])=[*:3]).([*:5]-[NH2;+0:4].[*:8]-[NH2;+0:9]).[OH;+0:12]-[OH;+0:13] |
| Reaction | ![]() |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |