| EC Tree |
| 1. Oxidoreductases |
| 1.3 Acting on the CH-CH group of donors |
| 1.3.3 With oxygen as acceptor |
| ID: | 1.3.3.3 |
|---|---|
| Description: | Coproporphyrinogen oxidase. |
| Alternative Name: |
Coproporphyrinogenase. Coproporphyrinogen-III oxidase. Coprogen oxidase. |
| Prosite: | PDOC00783; |
| PDB: |
» show all » hide |
| Cath: | 1.10.10.920; 3.80.30.20; 3.40.1500.10; |
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 1.3.3.3 |
| BRENDA Enzyme Link: | BRENDA 1.3.3.3 |
| KEGG Enzyme Link: | KEGG1.3.3.3 |
| BioCyc Enzyme Link: | BioCyc 1.3.3.3 |
| ExPASy Enzyme Link: | ExPASy1.3.3.3 |
| EC2PDB Enzyme Link: | EC2PDB 1.3.3.3 |
| ExplorEnz Enzyme Link: | ExplorEnz 1.3.3.3 |
| PRIAM enzyme-specific profiles Link: | PRIAM 1.3.3.3 |
| IntEnz Enzyme Link: | IntEnz 1.3.3.3 |
| MEDLINE Enzyme Link: | MEDLINE 1.3.3.3 |
| RHEA:18257 | coproporphyrinogen III + 2 H(+) + O2 = 2 CO2 + 2 H2O + protoporphyrinogen IX |
| RULE(radius=1) | ([*:1]-[CH2;+0:2]-[CH2;+0:3]-[C;H0;+0:4](=[*:5])-[OH;+0:6].[*:7]=[C;H0;+0:8](-[OH;+0:9])-[CH2;+0:10]-[CH2;+0:11]-[*:12]).[H+;H0:13].[H+;H0:14].[O;H0;+0:15]=[O;H0;+0:16]>>([*:1]-[CH;+0:2]=[CH2;+0:3].[*:12]-[CH;+0:11]=[CH2;+0:10]).[*:7]=[C;H0;+0:8]=[O;H0;+0:9].[*:5]=[C;H0;+0:4]=[O;H0;+0:6].[OH2;+0:15].[OH2;+0:16] |
| Reaction | ![]() |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Human coproporphyrinogen oxidase is not a metalloprotein. | Medlock AE, Dailey HA | 1996 Dec 20 | 8955072 |
| Coproporphyrinogen oxidase. Purification, molecular cloning, and induction of mRNA during erythroid differentiation. | Kohno H, Furukawa T, Yoshinaga T, Tokunaga R, Taketani S | 1993 Oct 5 | 8407975 |
| Purification and properties of coproporphyrinogenase. | del Batlle AM, Benson A, Rimington C | 1965 Dec | 5881662 |