EC number:1.4.3.25
Enzyme
Download| EC Tree |
| 1. Oxidoreductases |
| 1.4 Acting on the CH-NH2 group of donors |
| 1.4.3 With oxygen as acceptor |
| ID: | 1.4.3.25 |
|---|---|
| Description: | L-arginine oxidase. |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 1.4.3.25 |
| BRENDA Enzyme Link: | BRENDA 1.4.3.25 |
| KEGG Enzyme Link: | KEGG1.4.3.25 |
| BioCyc Enzyme Link: | BioCyc 1.4.3.25 |
| ExPASy Enzyme Link: | ExPASy1.4.3.25 |
| EC2PDB Enzyme Link: | EC2PDB 1.4.3.25 |
| ExplorEnz Enzyme Link: | ExplorEnz 1.4.3.25 |
| PRIAM enzyme-specific profiles Link: | PRIAM 1.4.3.25 |
| IntEnz Enzyme Link: | IntEnz 1.4.3.25 |
| MEDLINE Enzyme Link: | MEDLINE 1.4.3.25 |
| RHEA:51404 | H2O + L-arginine + O2 = 5-guanidino-2-oxopentanoate + H2O2 + NH4(+) |
| 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 |
|---|---|---|---|
| L-Arginine oxidase from Pseudomonas sp. TPU 7192: Characterization, gene cloning, heterologous expression, and application to L-arginine determination. | Matsui D, Terai A, Asano Y | 2016 Jan | 26672462 |
| L-amino acid oxidases with specificity for basic L-amino acids in cyanobacteria. | Gau AE, Heindl A, Nodop A, Kahmann U, Pistorius EK | 2007 Mar-Apr | 17542496 |