Biology:Orcinol 2-monooxygenase
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Short description: Class of enzymes
| orcinol 2-monooxygenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 1.14.13.6 | ||||||||
| CAS number | 37217-34-8 | ||||||||
| 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 | ||||||||
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Orcinol 2-monooxygenase (EC 1.14.13.6) is an enzyme that catalyzes the chemical reaction
- REDIRECT Template:Chemical reaction
The four substrates of this enzyme are orcinol, reduced nicotinamide adenine dinucleotide (NADH), oxygen, and a proton. Its products are 2,3,5-trihydroxytoluene, oxidised NAD+, and water.[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 orcinol,NADH:oxygen oxidoreductase (2-hydroxylating). It is also called orcinol hydroxylase. It uses flavin adenine dinucleotide as a cofactor.[1][3]
References
- ↑ 1.0 1.1 Enzyme 1.14.13.6 at KEGG Pathway Database.
- ↑ "Crystallization of orcinol hydroxylase from Pseudomonas putida". FEBS Lett. 11 (3): 189–192. 1970. doi:10.1016/0014-5793(70)80525-7. PMID 11945483. Bibcode: 1970FEBSL..11..189O.
- ↑ Montersino, Stefania; Tischler, Dirk; Gassner, George T.; Van Berkel, Willem J. H. (2011). "Catalytic and Structural Features of Flavoprotein Hydroxylases and Epoxidases". Advanced Synthesis & Catalysis 353 (13): 2301–2319. doi:10.1002/adsc.201100384.
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