EC |
1.3.3.3 |
Accepted name: |
coproporphyrinogen oxidase |
Reaction: |
coproporphyrinogen III + O2 + 2 H+ = protoporphyrinogen-IX + 2 CO2 + 2 H2O |
|
For diagram of the later stages of porphyrin biosynthesis, click here |
Other name(s): |
coproporphyrinogen III oxidase; coproporphyrinogenase |
Systematic name: |
coproporphyrinogen:oxygen oxidoreductase (decarboxylating) |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9076-84-0 |
References: |
1. |
Battle, A.M., Benson, A. and Rimington, C. Purification and properties of coproporphyrinogenase. Biochem. J. 97 (1965) 731–740. [PMID: 5881662] |
2. |
Medlock, A.E. and Dailey, H.A. Human coproporphyrinogen oxidase is not a metalloprotein. J. Biol. Chem. 271 (1996) 32507–32510. [DOI] [PMID: 8955072] |
3. |
Kohno, H., Furukawa, T., Yoshinaga, T., Tokunaga, R. and Taketani, S. Coproporphyrinogen oxidase. Purification, molecular cloning, and induction of mRNA during erythroid differentiation. J. Biol. Chem. 268 (1993) 21359–21363. [PMID: 8407975] |
|
[EC 1.3.3.3 created 1972, modified 2003] |
|
|
|
|