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1.14.13.7: phenol 2-monooxygenase (NADPH)

This is an abbreviated version!
For detailed information about phenol 2-monooxygenase (NADPH), go to the full flat file.

Word Map on EC 1.14.13.7

Reaction

phenol
+
NADPH
+
H+
+
O2
=
catechol
+
NADP+
+
H2O

Synonyms

DmpLNO, flavin containing monooxygenase, LmPH, Mph, MphN, multi-component phenol hydroxylase, multicomponent PH, multicomponent phenol hydroxylase, multicomponent phenol hydroxylase alpha subunit, NCgl2588, oxygenase, phenol 2-mono-, PHE, phenol hydroxylase, phenol o-hydroxylase, PHH, phhY, PHIND, PHO, PHR, single-component PH, SPH

ECTree

     1 Oxidoreductases
         1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
             1.14.13 With NADH or NADPH as one donor, and incorporation of one atom of oxygen into the other donor
                1.14.13.7 phenol 2-monooxygenase (NADPH)

Crystallization

Crystallization on EC 1.14.13.7 - phenol 2-monooxygenase (NADPH)

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
complexed with FAD and phenol, hanging drop vapour diffusion method
-
the crystal structure model of phenol hydroxylase corrected for 11 sequence errors and refined against new data to 1.7 A resolution
-
computational analyses of the hydrophobic cavities in the hydroxylase alpha-subunits of phenol hydroxylase. Among the xenon-binding sites observed in phenol hydroxylase, more than 80% are localized entirely within the alpha-subunit, and 70% of those occur in the hydrophobic cavities. The hydrophobicity of a large majority of side chain residues contributing to the xenon-binding sites in the phenol hyroxylase alpha-subunit are conserved among bacterial multicomponent monooxygenases. The xenon sites delineate the path of transport of dioxygen to the diiron center during catalysis
-
native and SeMet forms of the phenol hydroxylase in complex with its regulatory protein, hanging drop vapor diffusion method, 20°C, 0.035 mM enzyme in 10 mM MES, pH 7.1, and 10% glycerol is mixed with an equal volume of crystallization buffer containing 100 mM Tris, pH 7.0, 150 mM Na2MoO4, 5% glycerol, and 17-20% PEG 8000 (w/w), X-ray diffraction structure determination and analysis at 2.3 Å resolution, molecular replacement, Single-wavelength anomalous dispersion data for the selenomethionine derivative
-