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
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phenol-degrading
- hydroxylases
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2,3-dioxygenase
- trichosporon
- cutaneum
-
meta-cleavage
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diiron
- cresol
- comamonas
-
2-hydroxymuconic
- testosteroni
-
haldane
-
coke
- radioresistens
-
carboxylate-bridged
-
meta-pathway
-
ortho-cleavage
-
methylococcus
- cis,cis-muconate
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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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Subunits
Subunits on EC 1.14.13.7 - phenol 2-monooxygenase (NADPH)
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dimer
hexamer
homotetramer
tetramer
additional information
dimer
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SDS-PAGE shows three polypeptides with molecular masses of 13000, 39000 and 60000, gel filtration experiments are consistent with the existence of a dimer
dimer
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SDS-PAGE shows three polypeptides with molecular masses of 13000, 39000 and 60000, gel filtration experiments are consistent with the existence of a dimer
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(alphabetagamma)2, 2 * 54000 + 2 * 37800 + 2 * 11600, oxygenase component PHO, SDS-PAGE
hexamer
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(alphabetagamma)2, 2 * 54000 + 2 * 37800 + 2 * 11600, oxygenase component PHO, SDS-PAGE
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tetramer
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4 * 76000, non-denaturing PAGE, after expression in Escherichia coli
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the whole enzyme phenol hydroxylase comprises an oxygenase component (PHO), a reductase component (PHR) and a regulatory component (PHI). PHI is required for catalysis of the conversion of phenol to catechol in vitro, but is not required for PHR activity towards alternative electron acceptors such as cytochrome c and Nitro Blue Tetrazolium. The molecular mass of PHI is determined to be 10000 Da by SDS-PAGE, 8800 Da by MALDI-TOF spectrometry and 18000 Da by gel filtration. PHI is in the native state a homodimer. In the reconstituted system, optimal rate is achieved when the stoichiometry of the components is 2 reductase monomers:1 PHI dimer: 1 PHO (alphabetagamma)2
additional information
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the whole enzyme phenol hydroxylase comprises an oxygenase component (PHO), a reductase component (PHR) and a regulatory component (PHI). PHI is required for catalysis of the conversion of phenol to catechol in vitro, but is not required for PHR activity towards alternative electron acceptors such as cytochrome c and Nitro Blue Tetrazolium. The molecular mass of PHI is determined to be 10000 Da by SDS-PAGE, 8800 Da by MALDI-TOF spectrometry and 18000 Da by gel filtration. PHI is in the native state a homodimer. In the reconstituted system, optimal rate is achieved when the stoichiometry of the components is 2 reductase monomers:1 PHI dimer: 1 PHO (alphabetagamma)2
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additional information
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peptide mass fingerprinting and MALDI-TOF analysis of the 25 kD enzyme
additional information
Auxenochlorella pyrenoidosa NCIM 2738
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peptide mass fingerprinting and MALDI-TOF analysis of the 25 kD enzyme
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additional information
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the regulatory protein component binds in a canyon on one side of the (alpha,beta)2 enzyme dimer, contacting alpha-subunit helices A, E, and F about 12 A above the diiron core
additional information
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the phenol hydroxylase complex possesses the PHL, PHN, PHO, PHM, and PHK subunits
additional information
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the regulatory protein component binds in a canyon on one side of the (alpha,beta)2 enzyme dimer, contacting alpha-subunit helices A, E, and F about 12 A above the diiron core
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additional information
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the phenol hydroxylase complex possesses the PHL, PHN, PHO, PHM, and PHK subunits
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