EC number:1.4.3.20
Enzyme
Download| EC Tree |
| 1. Oxidoreductases |
| 1.4 Acting on the CH-NH2 group of donors |
| 1.4.3 With oxygen as acceptor |
| ID: | 1.4.3.20 |
|---|---|
| Description: | L-lysine 6-oxidase. |
| Alternative Name: |
Marinocine. Lod. L-lysine-epsilon-oxidase. |
3D structure
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.References
External Links
| UniProtKB Enzyme Link: | UniProtKB 1.4.3.20 |
| BRENDA Enzyme Link: | BRENDA 1.4.3.20 |
| KEGG Enzyme Link: | KEGG1.4.3.20 |
| BioCyc Enzyme Link: | BioCyc 1.4.3.20 |
| ExPASy Enzyme Link: | ExPASy1.4.3.20 |
| EC2PDB Enzyme Link: | EC2PDB 1.4.3.20 |
| ExplorEnz Enzyme Link: | ExplorEnz 1.4.3.20 |
| PRIAM enzyme-specific profiles Link: | PRIAM 1.4.3.20 |
| IntEnz Enzyme Link: | IntEnz 1.4.3.20 |
| MEDLINE Enzyme Link: | MEDLINE 1.4.3.20 |
| RHEA:22548 | H2O + L-lysine + O2 = (S)-2-amino-6-oxohexanoate + H2O2 + NH4(+) |
| RULE(radius=1) | [*:1]-[CH2;+0:2]-[NH2;+0:3].[O;H0;+0:4]=[O;H0;+0:5].[OH2;+0:6]>>[*:1]-[CH;+0:2]=[O;H0;+0:6].[NH3;+0:3].[OH;+0:4]-[OH;+0:5] |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| A novel type of lysine oxidase: L-lysine-epsilon-oxidase. | Gómez D, Lucas-Elío P, Sanchez-Amat A, Solano F | 2006 Oct | 17030025 |
| The antimicrobial activity of marinocine, synthesized by Marinomonas mediterranea, is due to hydrogen peroxide generated by its lysine oxidase activity. | Lucas-Elío P, Gómez D, Solano F, Sanchez-Amat A | 2006 Apr | 16547036 |