KEGG   ENZYME: 1.14.13.7Help
Entry
EC 1.14.13.7                Enzyme                                 

Name
phenol 2-monooxygenase (NADPH);
phenol hydroxylase;
phenol o-hydroxylase
Class
Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
With NADH or NADPH as one donor, and incorporation of one atom of oxygen into the other donor
BRITE hierarchy
Sysname
phenol,NADPH:oxygen oxidoreductase (2-hydroxylating)
Reaction(IUBMB)
phenol + NADPH + H+ + O2 = catechol + NADP+ + H2O [RN:R00815]
Reaction(KEGG)
R00815;
(other) R03566 R03568
Show
Substrate
phenol [CPD:C00146];
NADPH [CPD:C00005];
H+ [CPD:C00080];
O2 [CPD:C00007]
Product
catechol [CPD:C00090];
NADP+ [CPD:C00006];
H2O [CPD:C00001]
Comment
A flavoprotein (FAD). The enzyme from the fungus Trichosporon cutaneum has a broad substrate specificity, and has been reported to catalyse the hydroxylation of a variety of substituted phenols, such as fluoro-, chloro-, amino- and methyl-phenols and also dihydroxybenzenes. cf. EC 1.14.14.20, phenol 2-monooxygenase (FADH2).
History
EC 1.14.13.7 created 1972, modified 2011, modified 2016
Pathway
ec00623  Toluene degradation
ec00627  Aminobenzoate degradation
ec01100  Metabolic pathways
ec01120  Microbial metabolism in diverse environments
Orthology
K03380  phenol 2-monooxygenase
Genes
PXB: 103942874
DHA: DEHA2C14784g
PIC: PICST_57166(PHH2)
SPAA: SPAPADRAFT_59206
LEL: LELG_04072
CAL: CAALFM_CR07820WA(CaO19.3711) CAALFM_CR07940WA(CaO19.604)
CTP: CTRG_00423 CTRG_03102
COT: CORT_0D06110
CDU: CD36_33480 CD36_33600
SLB: AWJ20_109 AWJ20_385
NTE: NEUTE1DRAFT121791(NEUTE1DRAFT_121791) NEUTE1DRAFT61928(NEUTE1DRAFT_61928) NEUTE1DRAFT78296(NEUTE1DRAFT_78296)
MGR: MGG_04639
MBE: MBM_07857
ANG: ANI_1_2070074(An08g06720) ANI_1_2320104(An12g10250) ANI_1_3124014(An01g11800)
ABP: AGABI1DRAFT118718(AGABI1DRAFT_118718) AGABI1DRAFT129336(AGABI1DRAFT_129336)
ABV: AGABI2DRAFT180260(AGABI2DRAFT_180260) AGABI2DRAFT185850(AGABI2DRAFT_185850)
HAM: HALO0393
ADI: B5T_03289
AXE: P40_15405
BPH: Bphy_6383
LIM: L103DPR2_02688(pcpB)
HYB: Q5W_00715
ARA: Arad_7218
RHT: NT26_0615
BJA: blr4222
BRA: BRADO5224
BBT: BBta_5688
BRS: S23_40400
AOL: S58_24710
BRAD: BF49_0830
MET: M446_6872
PHL: KKY_2081
PDE: Pden_3488
SPSE: SULPSESMR1_02017(mobA)
MAGX: XM1_0851
MAGN: WV31_12590
CGL: NCgl0050(Cgl0050) NCgl2588(Cgl2681)
CGT: cgR_2584
CGM: cgp_2966
CSP: WM42_1475
CPHO: CPHO_12190
CAQU: CAQU_01280
NFA: NFA_27810
NFR: ERS450000_01314(pcpB_3)
RHS: A3Q41_02968(mobA)
GPO: GPOL_c33240(mphP2)
MTS: MTES_0649
ART: Arth_3519
ARM: ART_3167
ACH: Achl_3607
AAI: AARI_11920 AARI_30840(1.14.13.-)
KRH: KRH_22060
CFI: Celf_2070
SERJ: SGUI_0719
DCO: SAMEA4475696_1574(pcpB)
PSEH: XF36_28815
RXY: Rxyl_0473
 » show all
Taxonomy
Reference
1  [PMID:14478080]
  Authors
NAKAGAWA H, TAKEDA Y.
  Title
Phenol hydroxylase.
  Journal
Biochim. Biophys. Acta. 62 (1962) 423-6.
Reference
2  [PMID:4146224]
  Authors
Neujahr HY, Gaal A.
  Title
Phenol hydroxylase from yeast. Purification and properties of the enzyme from Trichosporon cutaneum.
  Journal
Eur. J. Biochem. 35 (1973) 386-400.
  Sequence
Reference
3  [PMID:810352]
  Authors
Neujahr HY, Gaal A.
  Title
Phenol hydroxylase from yeast. Sulfhydryl groups in phenol hydroxylase from Trichosporon cutaneum.
  Journal
Eur. J. Biochem. 58 (1975) 351-7.
Other DBs
ExplorEnz - The Enzyme Database: 1.14.13.7
IUBMB Enzyme Nomenclature: 1.14.13.7
ExPASy - ENZYME nomenclature database: 1.14.13.7
UM-BBD (Biocatalysis/Biodegradation Database): 1.14.13.7
BRENDA, the Enzyme Database: 1.14.13.7
CAS: 37256-84-1

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