| EC Tree |
| 1. Oxidoreductases |
| 1.10 Acting on diphenols and related substances as donors |
| 1.10.3 With oxygen as acceptor |
| ID: | 1.10.3.3 | ||
|---|---|---|---|
| Description: | L-ascorbate oxidase. | ||
| Alternative Name: |
Ascorbase. | ||
| Prosite: | PDOC00076; | ||
| PDB: |
|
||
| Cath: | 2.60.40.420; |
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 1.10.3.3 |
| BRENDA Enzyme Link: | BRENDA 1.10.3.3 |
| KEGG Enzyme Link: | KEGG1.10.3.3 |
| BioCyc Enzyme Link: | BioCyc 1.10.3.3 |
| ExPASy Enzyme Link: | ExPASy1.10.3.3 |
| EC2PDB Enzyme Link: | EC2PDB 1.10.3.3 |
| ExplorEnz Enzyme Link: | ExplorEnz 1.10.3.3 |
| PRIAM enzyme-specific profiles Link: | PRIAM 1.10.3.3 |
| IntEnz Enzyme Link: | IntEnz 1.10.3.3 |
| MEDLINE Enzyme Link: | MEDLINE 1.10.3.3 |
| RHEA:30243 | 4 L-ascorbate + O2 = 2 H2O + 4 monodehydro-L-ascorbate radical |
| RULE(radius=1) | [O;H0;+0:1]=[O;H0;+0:2]>>[OH2;+0:1].[OH2;+0:2] |
| Reaction | ![]() |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Refined crystal structure of ascorbate oxidase at 1.9 A resolution. | Messerschmidt A, Ladenstein R, Huber R, Bolognesi M, Avigliano L, Petruzzelli R, Rossi A, Finazzi-Agró A | 1992 Mar 5 | 1548698 |
| Mechanism of free radical formation and disappearance during the ascorbic acid oxidase and peroxidase reactions. | YAMAZAKI I, PIETTE LH | 1961 Jun 10 | 13787201 |