| EC Tree |
| 1. Oxidoreductases |
| 1.4 Acting on the CH-NH2 group of donors |
| 1.4.3 With oxygen as acceptor |
| ID: | 1.4.3.14 |
|---|---|
| Description: | L-lysine oxidase. |
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 1.4.3.14 |
| BRENDA Enzyme Link: | BRENDA 1.4.3.14 |
| KEGG Enzyme Link: | KEGG1.4.3.14 |
| BioCyc Enzyme Link: | BioCyc 1.4.3.14 |
| ExPASy Enzyme Link: | ExPASy1.4.3.14 |
| EC2PDB Enzyme Link: | EC2PDB 1.4.3.14 |
| ExplorEnz Enzyme Link: | ExplorEnz 1.4.3.14 |
| PRIAM enzyme-specific profiles Link: | PRIAM 1.4.3.14 |
| IntEnz Enzyme Link: | IntEnz 1.4.3.14 |
| MEDLINE Enzyme Link: | MEDLINE 1.4.3.14 |
| RHEA:14437 | H2O + L-lysine + O2 = 6-amino-2-oxohexanoate + 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 |
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| A new antitumor enzyme, L-lysine alpha-oxidase from Trichoderma viride. Purification and enzymological properties. | Kusakabe H, Kodama K, Kuninaka A, Yoshino H, Misono H, Soda K | 1980 Feb 10 | 6101334 |
| L-Lysine alpha-oxidase: physicochemical and biological properties. | Lukasheva EV, Berezov TT | 2002 Oct | 12460113 |