Phenol 2-monooxygenase

Phenol 2-monooxygenase
Identifiers
EC no.1.14.13.7
CAS no.37256-84-1
Databases
BRENDAenzyme data
ExPASyNiceZyme view
KEGGenzyme entry
MetaCycmetabolic pathway
Rheareactions
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

Phenol 2-monooxygenase (EC 1.14.13.7) is an enzyme that catalyzes the chemical reaction

+ NADPH + H+
 
 
O2
H2O
Rightward reaction arrow with minor substrate(s) from top left and minor product(s) to top right
 
 
 
 

The four substrates of this enzyme are phenol, reduced nicotinamide adenine dinucleotide phosphate (NADPH), oxygen and a proton. Its products are catechol, oxidised NADP+, and water.[1][2][3]

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 phenol,NADPH:oxygen oxidoreductase (2-hydroxylating). Other names in common use include phenol hydroxylase, and phenol o-hydroxylase. It uses flavin adenine dinucleotide as a cofactor.[4] The enzyme from Trichosporon cutaneum can hydroxylate a range of phenols.[1][5]

Structural studies

As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes PDB: 1FOH​, PDB: 1HQI​, and PDB: 1PN0​.

References

  1. 1 2 Enzyme 1.14.13.7 at KEGG Pathway Database.
  2. ↑ Nakagawa H, Takeda Y (1962). "Phenol hydroxylase". Biochim. Biophys. Acta. 62 (2): 423–6. doi:10.1016/0006-3002(62)90275-5. PMID 14478080.
  3. ↑ Neujahr HY, Gaal A (1973). "Phenol hydroxylase from yeast. Purification and properties of the enzyme from Trichosporon cutaneum". Eur. J. Biochem. 35 (2): 386–400. doi:10.1111/j.1432-1033.1973.tb02851.x. PMID 4146224.
  4. ↑ 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.
  5. ↑ Neujahr HY, Gaal A (1975). "Phenol hydroxylase from yeast. Sulfhydryl groups in phenol hydroxylase from Trichosporon cutaneum". Eur. J. Biochem. 58 (2): 351–7. doi:10.1111/j.1432-1033.1975.tb02381.x. PMID 810352.