EC number:1.4.3.1
Enzyme
Download| EC Tree |
| 1. Oxidoreductases |
| 1.4 Acting on the CH-NH2 group of donors |
| 1.4.3 With oxygen as acceptor |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 1.4.3.1 |
| BRENDA Enzyme Link: | BRENDA 1.4.3.1 |
| KEGG Enzyme Link: | KEGG1.4.3.1 |
| BioCyc Enzyme Link: | BioCyc 1.4.3.1 |
| ExPASy Enzyme Link: | ExPASy1.4.3.1 |
| EC2PDB Enzyme Link: | EC2PDB 1.4.3.1 |
| ExplorEnz Enzyme Link: | ExplorEnz 1.4.3.1 |
| PRIAM enzyme-specific profiles Link: | PRIAM 1.4.3.1 |
| IntEnz Enzyme Link: | IntEnz 1.4.3.1 |
| MEDLINE Enzyme Link: | MEDLINE 1.4.3.1 |
| RHEA:12512 | D-aspartate + H2O + O2 = H2O2 + NH4(+) + oxaloacetate |
| RULE(radius=1) | [*:1]-[CH;+0:2](-[*:3])-[NH2;+0:4].[O;H0;+0:5]=[O;H0;+0:6].[OH2;+0:7]>>[*:1]-[C;H0;+0:2](-[*:3])=[O;H0;+0:7].[NH3;+0:4].[OH;+0:5]-[OH;+0:6] |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Functional and structural characterization of D-aspartate oxidase from porcine kidney: non-Michaelis kinetics due to substrate activation. | Yamamoto A, Tanaka H, Ishida T, Horiike K | 2007 Mar | 17234685 |
| Comparative characterization of three D-aspartate oxidases and one D-amino acid oxidase from Caenorhabditis elegans. | Katane M, Saitoh Y, Seida Y, Sekine M, Furuchi T, Homma H | 2010 Jun | 20564561 |