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
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meta-cleavage
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diiron
- cresol
- comamonas
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2-hydroxymuconic
- testosteroni
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haldane
-
coke
- radioresistens
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carboxylate-bridged
-
meta-pathway
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ortho-cleavage
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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
1.14.13.7 phenol 2-monooxygenase (NADPH)Advanced search results
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results (Natural Substrates Products
Natural Substrates Products on EC 1.14.13.7 - phenol 2-monooxygenase (NADPH)
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NATURAL SUBSTRATE 
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2 2-xylene + 2 NADPH + 2 H+ + 2 O2
2,3-dimethylphenol + 3,4-dimethylphenol + 2 NADP+ + 2 H2O
2 ethynylbenzene + NADPH + 3 O2
2-ethynylphenol + 2-hydroxy-6-oxo-octa-2,4-dien-7-ynoic acid + NADP+ + H2O
2 2-xylene + 2 NADPH + 2 H+ + 2 O2
2,3-dimethylphenol + 3,4-dimethylphenol + 2 NADP+ + 2 H2O
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?
2 2-xylene + 2 NADPH + 2 H+ + 2 O2
2,3-dimethylphenol + 3,4-dimethylphenol + 2 NADP+ + 2 H2O
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?
2 ethynylbenzene + NADPH + 3 O2
2-ethynylphenol + 2-hydroxy-6-oxo-octa-2,4-dien-7-ynoic acid + NADP+ + H2O
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substrate only for phenol-grown cells
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?
2 ethynylbenzene + NADPH + 3 O2
2-ethynylphenol + 2-hydroxy-6-oxo-octa-2,4-dien-7-ynoic acid + NADP+ + H2O
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substrate only for phenol-grown cells
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?
3 toluene + 3 NADPH + 3 H+ + 3 O2
2-cresol + 3-cresol + 4-cresol + 3 NADP+ + 3 H2O
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?
3 toluene + 3 NADPH + 3 H+ + 3 O2
2-cresol + 3-cresol + 4-cresol + 3 NADP+ + 3 H2O
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?
3 toluene + 3 NADPH + 3 H+ + 3 O2
2-cresol + 3-cresol + 4-cresol + 3 NADP+ + 3 H2O
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?
3 toluene + 3 NADPH + 3 H+ + 3 O2
2-cresol + 3-cresol + 4-cresol + 3 NADP+ + 3 H2O
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?
phenol + NADH + H+ + O2
catechol + NAD+ + H2O
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coupling between phenol hydroxylase and toluene/o-xylene monooxygenase optimizes the use of nonhydroxylated aromatic molecules by the draining effect of phenol hydroxylase on the products of oxidation catalyzed by toluene/o-xylene monooxygenase, thus avoiding phenol accumulation
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?
phenol + NADH + H+ + O2
catechol + NAD+ + H2O
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coupling between phenol hydroxylase and toluene/o-xylene monooxygenase optimizes the use of nonhydroxylated aromatic molecules by the draining effect of phenol hydroxylase on the products of oxidation catalyzed by toluene/o-xylene monooxygenase, thus avoiding phenol accumulation
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?
phenol + NADPH + H+ + O2
catechol + NADP+ + H2O
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?
phenol + NADPH + O2
catechol + NADP+ + H2O
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high phenol degradation activity in vivo in strain TL3, catabolic pathway overview
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?
phenol + NADPH + O2
catechol + NADP+ + H2O
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high phenol degradation activity in vivo in strain TL3, catabolic pathway overview
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?
phenol + NADPH + O2
catechol + NADP+ + H2O
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initial step in phenol-degrading pathway
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?
phenol + NADPH + O2
catechol + NADP+ + H2O
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initial step in phenol-degrading pathway
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?
additional information
?
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first enzyme of phenol biodegradation
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additional information
?
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only complete enzyme systems containing all three or four protein components are capable of oxidizing phenol. The electron-transfer components exert regulatory effects on substrate oxidation processes taking place at the hydroxylase actives sites, most likely through allostery. The regulatory proteins facilitate the electron-transfer step in the hydrocarbon oxidation cycle in the absence of phenol. Under these conditions, electron consumption is coupled to H2O2 formation in a hydroxylase-dependent manner
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?
additional information
?
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only complete enzyme systems containing all three or four protein components are capable of oxidizing phenol. The electron-transfer components exert regulatory effects on substrate oxidation processes taking place at the hydroxylase actives sites, most likely through allostery. The regulatory proteins facilitate the electron-transfer step in the hydrocarbon oxidation cycle in the absence of phenol. Under these conditions, electron consumption is coupled to H2O2 formation in a hydroxylase-dependent manner
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?
