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
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1.14.13.7
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catechols
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phenol-degrading
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hydroxylases
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2,3-dioxygenase
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trichosporon
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cutaneum
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meta-cleavage
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diiron
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cresol
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comamonas
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2-hydroxymuconic
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testosteroni
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haldane
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coke
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radioresistens
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carboxylate-bridged
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meta-pathway
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ortho-cleavage
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methylococcus
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cis,cis-muconate
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coking
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environmental protection
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industry
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synthesis
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degradation
- 1.14.13.7
- catechols
-
phenol-degrading
- hydroxylases
-
2,3-dioxygenase
- trichosporon
- cutaneum
-
meta-cleavage
-
diiron
- cresol
- comamonas
-
2-hydroxymuconic
- testosteroni
-
haldane
-
coke
- radioresistens
-
carboxylate-bridged
-
meta-pathway
-
ortho-cleavage
-
methylococcus
- cis,cis-muconate
-
coking
- environmental protection
- industry
- synthesis
- degradation
Reaction
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
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Crystallization
Crystallization on EC 1.14.13.7 - phenol 2-monooxygenase (NADPH)
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complexed with FAD and phenol, hanging drop vapour diffusion method
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the crystal structure model of phenol hydroxylase corrected for 11 sequence errors and refined against new data to 1.7 A resolution
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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
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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
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