4-aminobenzoate 1-monooxygenase
| 4-aminobenzoate 1-monooxygenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.14.13.27 | ||||||||
| CAS no. | 98668-55-4 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
4-aminobenzoate 1-monooxygenase (EC 1.14.13.27) is an enzyme that catalyzes the chemical reaction
The four substrates of this enzyme are 4-aminobenzoic acid, reduced nicotinamide adenine dinucleotide (NADH), oxygen and a proton. Its products are 4-aminophenol, oxidised NAD+, water, and carbon dioxide. Nicotinamide adenine dinucleotide phosphate can be used as an alternative cofactor.[1][2]
The enzyme is a flavin-containing monooxygenase that uses molecular oxygen as oxidant and incorporates one of its atoms into the starting material. The systematic name of this enzyme class is 4-aminobenzoate,NAD(P)H:oxygen oxidoreductase (1-hydroxylating, decarboxylating). Other names in common use include 4-aminobenzoate hydroxylase, and 4-aminobenzoate monooxygenase. It uses flavin adenine dinucleotide as a cofactor.[1]
References
- ^ a b Enzyme 1.14.13.27 at KEGG Pathway Database.
- ^ Tsuji H, Ogawa T, Bando N, Sasaoka K (1986). "Purification and properties of 4-aminobenzoate hydroxylase, a new monooxygenase from Agaricus bisporus". J. Biol. Chem. 261 (28): 13203–9. doi:10.1016/S0021-9258(18)69291-9. PMID 3489713.