Phenol 2-monooxygenase

Phenol 2-monooxygenase
Identifiers
EC no.1.14.13.7
CAS no.37256-84-1
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
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
 
 
 
 

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 1FOH, 1HQI, and 1PN0.

References

  1. ^ a b 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.