| EC Tree |
| 1. Oxidoreductases |
| 1.1 Acting on the CH-OH group of donors |
| 1.1.3 With oxygen as acceptor |
| ID: | 1.1.3.14 |
|---|---|
| Description: | Catechol oxidase (dimerizing). |
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 1.1.3.14 |
| BRENDA Enzyme Link: | BRENDA 1.1.3.14 |
| KEGG Enzyme Link: | KEGG1.1.3.14 |
| BioCyc Enzyme Link: | BioCyc 1.1.3.14 |
| ExPASy Enzyme Link: | ExPASy1.1.3.14 |
| EC2PDB Enzyme Link: | EC2PDB 1.1.3.14 |
| ExplorEnz Enzyme Link: | ExplorEnz 1.1.3.14 |
| PRIAM enzyme-specific profiles Link: | PRIAM 1.1.3.14 |
| IntEnz Enzyme Link: | IntEnz 1.1.3.14 |
| MEDLINE Enzyme Link: | MEDLINE 1.1.3.14 |
| RHEA:12809 | 4 catechol + 3 O2 = 2 dibenzo[1,4]dioxin-2,3-dione + 6 H2O |
| RULE(radius=1) | [O;H0;+0:1]=[O;H0;+0:2].[O;H0;+0:3]=[O;H0;+0:4].[O;H0;+0:5]=[O;H0;+0:6].[OH;+0:7]-[*:8]:[*:9]-[OH;+0:10].[OH;+0:11]-[*:12]:[*:13]-[OH;+0:14].[OH;+0:15]-[c;H0;+0:16]1:[*:17]:[cH;+0:18]:[cH;+0:19]:[*:20]:[c;H0;+0:21]:1-[OH;+0:22].[OH;+0:23]-[c;H0;+0:24]1:[*:25]:[cH;+0:26]:[cH;+0:27]:[*:28]:[c;H0;+0:29]:1-[OH;+0:30]>>[O;H0;+0:15]=[c;H0;+0:16]1:[*:17]:[c;H0;+0:18]2:[o;H0;+0:7]:[*:8]:[*:9]:[o;H0;+0:10]:[c;H0;+0:19]-2:[*:20]:[c;H0;+0:21]:1=[O;H0;+0:22].[O;H0;+0:23]=[c;H0;+0:24]1:[*:25]:[c;H0;+0:26]2:[o;H0;+0:14]:[*:13]:[*:12]:[o;H0;+0:11]:[c;H0;+0:27]-2:[*:28]:[c;H0;+0:29]:1=[O;H0;+0:30].[OH2;+0:1].[OH2;+0:2].[OH2;+0:3].[OH2;+0:4].[OH2;+0:5].[OH2;+0:6] |
| Reaction | ![]() |
| Core-to-Core |
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| ENZYMIC OXIDATION OF CATECHOL TO DIPHENYLENEDIOXIDE-2,3-QUINONE. | NAIR PM, VINING LC | 1964 Jul 20 | 14217190 |