Phthalate 4,5-dioxygenase
| Phthalate 4,5-dioxygenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.14.12.7 | ||||||||
| CAS no. | 63626-44-8 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
Phthalate 4,5-dioxygenase (EC 1.14.12.7) is an enzyme that catalyzes the chemical reaction
The four substrates of this enzyme are phthalic acid, nicotinamide adenine dinucleotide (NADH), oxygen, and a proton. Its products are cis-4,5-dihydroxycyclohexa-2,6-diene-1,2-dicarboxylic acid and NAD+.[1][2]
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with molecular oxygen as oxidant and incorporation or reduction of oxygen. The systematic name of its class is phthalate,NADH:oxygen oxidoreductase (4,5-hydroxylating). Other names in common use include PDO, and phthalate dioxygenase. The enzyme participates in 2,4-dichlorobenzoate degradation. It is an Iron-sulfur protein which uses flavin mononucleotide as a cofactor.[1]
References
- 1 2 Enzyme 1.14.12.7 at KEGG Pathway Database.
- ↑ Batie CJ, LaHaie E, Ballou DP (1987). "Purification and characterization of phthalate oxygenase and phthalate oxygenase reductase from Pseudomonas cepacia". J. Biol. Chem. 262 (4): 1510–8. doi:10.1016/S0021-9258(19)75664-6. PMID 3805038.