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Information on EC 1.14.13.7 - phenol 2-monooxygenase (NADPH)
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1.14.13.7 phenol 2-monooxygenase (NADPH)IUBMB Comments
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).
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Word Map
- 1.14.13.7
- catechols
-
phenol-degrading
- hydroxylases
- trichosporon
-
2,3-dioxygenase
- cutaneum
-
meta-cleavage
- comamonas
-
diiron
- cresol
- testosteroni
-
2-hydroxymuconic
-
haldane
-
coke
-
methylococcus
-
coking
-
meta-pathway
- radioresistens
-
carboxylate-bridged
- cis,cis-muconate
-
ortho-cleavage
- degradation
- industry
- synthesis
- environmental protection
The enzyme appears in viruses and cellular organisms
Synonyms
phenol hydroxylase, multicomponent phenol hydroxylase, phind, multi-component phenol hydroxylase, dmplno, multicomponent ph, ncgl2588, single-component ph, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
LmPH
Mph
multicomponent PH
multicomponent phenol hydroxylase
phenol hydroxylase
PHH
phhY
PHIND
PHO
PHR
single-component PH
SPH
LmPH
A5YUW2, A5YUW3, A5YUW6, A5YUY2, A5YUY5, A5YUY6, A5YUY7, A5YUZ3, A5YUZ5, A5YUZ6, A5YUZ7, A5YUZ8, A5YUZ9, A5YV00, A5YV01, A5YV02, A5YV03, A5YV04, A5YV05, A5YV06, A5YV08, A5YV10, A5YV11, A5YV12, A5YV13, A5YV14, A5YV15, A5YV16, A5YV18, A5YV19, A5YV20
-
phenol hydroxylase
-
multicomponent enzyme made up of three moieties: a reductase (PHR), and an oxygenase (PHO) and a regulative component
phenol hydroxylase
-
multicomponent enzyme made up of three moieties: a reductase (PHR), and an oxygenase (PHO) and a regulative component
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
phenol + NADPH + H+ + O2 = catechol + NADP+ + H2O
-
-
-
-
phenol + NADPH + H+ + O2 = catechol + NADP+ + H2O
catalytic mechanism, conformational changes upon binding of the regulatory protein comonent and effects on catalytic activity
-
phenol + NADPH + H+ + O2 = catechol + NADP+ + H2O
catalytic mechanism, conformational changes upon binding of the regulatory protein comonent and effects on catalytic activity
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
phenol,NADPH:oxygen oxidoreductase (2-hydroxylating)
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).
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CAS REGISTRY NUMBER
COMMENTARY
37256-84-1
-
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SUBSTRATE
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
1,3-dihydroxybenzene + NADPH + H+ + O2
? + NADP+ + H2O
-
50.12% activity compared to phenol
-
?
2 2-cresol + NADPH + O2
3-methylcatechol + 4-methylcatechol + NADP+ + H2O
-
-
-
?
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
2,3,5,6-tetrafluorophenol + O2 + NADPH
3,4,6-trifluoro-2-benzoquinone + NADP+ + F-
-
-
-
?
2-hydroxybenzoic acid + NADPH + H+ + O2
? + NADP+ + H2O
-
15.97% activity compared to phenol
-
?
2-naphthol + NADPH + H+ + O2
? + NADP+ + H2O
-
9.75% activity compared to phenol
-
?
3-cresol + NADPH + O2
3-methylcatechol + 4-methylcatechol + NADP+ + H2O
-
-
-
?
3-hydroxybenzoic acid + NADPH + H+ + O2
? + NADP+ + H2O
-
18.53% activity compared to phenol
-
?
3-nitrophenol + NADPH + H+ + O2
?
-
about 45% of the activity with phenol
-
?
4-chlorophenol + NADH + H+ + O2
4-chlorocatechol + NAD+ + H2O
-
27% of the activity with phenol
-
?
4-chlorophenol + NADH + H+ + O2
4-chlorochatechol + NAD+ + H2O
-
-
?
4-chlorophenol + NADPH + H+ + O2
? + NADP+ + H2O
-
28.6% activity compared to phenol
-
?
4-cresol + NADPH + O2
4-methylcatechol + NADP+ + H2O
-
best substrate
-
?
4-fluorophenol + NADH + H+ + O2
1,2-dihydroxy-4-fluorobenzene + NAD+ + H2O
-
-
-
?
4-fluorophenol + O2 + NADPH
?
-
-
-
?
4-hydroxybenzoic acid + NADPH + H+ + O2
? + NADP+ + H2O
-
14.88% activity compared to phenol
-
?
4-hydroxyphenol + NADPH + H+ + O2
?
-
about 120% of the activity with phenol
-
?
4-methylphenol + NADH + H+ + O2
1,2-dihydroxy-4-methylbenzene + NAD+ + H2O
-
-
-
?
4-nitrophenol + NADPH + H+ + O2
?
-
about 50% of the activity with phenol
-
?
dibenzofuran + NADPH + H+ + O2
1,2-dihydrobenzofuran + NADP+ + H2O
-
-
-
?
hydroquinone + NADPH + H+ + O2
? + NADP+ + H2O
-
48.25% activity compared to phenol
-
?
m-chlorophenol + NADPH + O2
4-chloro-benzene-1,2-diol + NADP+ + H2O
-
18% of the activity with phenol
-
?
m-cresol + NADPH + H+ + O2
3-methylcatechol + 4-methylcatechol + NADP+
-
-
95% 3-methylcatechol, 5% 4-methylcatechol
?
o-chlorophenol + NADPH + O2
3-chloro-benzene-1,2-diol + NADP+ + H2O
-
20% of the activity with phenol
-
?
o-cresol + NADPH + O2
3-methylcatechol + NADP+ + H2O
-
37% of the activity with phenol, measured as substrate-dependent oxygen uptake rate by derivatives of Pseudomonas aeruginosa PAO1c carrying the enzyme genes after induction with phenol
-
?
p-cresol + NADPH + O2
4-methylcatechol + NADP+ + H2O
-
114% of the activity with phenol
-
?
toluene + NADPH + H+ + O2
o-cresol + m-cresol + p-cresol + NADP+
-
-
48% o-cresol, 11% m-cresol, 41% p-cresol
?
2 2-xylene + 2 NADPH + 2 H+ + 2 O2
2,3-dimethylphenol + 3,4-dimethylphenol + 2 NADP+ + 2 H2O
-
-
-
?
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
-
-
product identification by GC-MS
?
2 ethynylbenzene + NADPH + 3 O2
2-ethynylphenol + 2-hydroxy-6-oxo-octa-2,4-dien-7-ynoic acid + NADP+ + H2O
-
substrate only for phenol-grown cells
-
?
2 ethynylbenzene + NADPH + 3 O2
2-ethynylphenol + 2-hydroxy-6-oxo-octa-2,4-dien-7-ynoic acid + NADP+ + H2O
-
-
product identification by GC-MS
?
2 ethynylbenzene + NADPH + 3 O2
2-ethynylphenol + 2-hydroxy-6-oxo-octa-2,4-dien-7-ynoic acid + NADP+ + H2O
-
substrate only for phenol-grown cells
-
?
2-ethylphenol + NADPH + O2
3-ethyl-benzene-1,2-diol + NADP+ + H2O
-
18% of the activity with phenol
-
?
2-ethylphenol + NADPH + O2
3-ethyl-benzene-1,2-diol + NADP+ + H2O
-
18% of the activity with phenol
-
?
2-hydroxyphenol + NADPH + H+ + O2
?
-
about 70% of the activity with phenol
-
?
2-hydroxyphenol + NADPH + H+ + O2
?
-
about 70% of the activity with phenol
-
?
2-nitrophenol + NADPH + H+ + O2
?
-
about 80% of the activity with phenol
-
?
2-nitrophenol + NADPH + H+ + O2
?
-
about 80% of the activity with phenol
-
?
3 toluene + 3 NADPH + 3 H+ + 3 O2
2-cresol + 3-cresol + 4-cresol + 3 NADP+ + 3 H2O
-
-
-
?
3 toluene + 3 NADPH + 3 H+ + 3 O2
2-cresol + 3-cresol + 4-cresol + 3 NADP+ + 3 H2O
-
-
-
?
3 toluene + 3 NADPH + 3 H+ + 3 O2
2-cresol + 3-cresol + 4-cresol + 3 NADP+ + 3 H2O
-
-
-
?
3 toluene + 3 NADPH + 3 H+ + 3 O2
2-cresol + 3-cresol + 4-cresol + 3 NADP+ + 3 H2O
-
regioselectivity, overview
-
?
3 toluene + 3 NADPH + 3 H+ + 3 O2
2-cresol + 3-cresol + 4-cresol + 3 NADP+ + 3 H2O
-
regioselectivity, overview
-
?
3 toluene + 3 NADPH + 3 H+ + 3 O2
2-cresol + 3-cresol + 4-cresol + 3 NADP+ + 3 H2O
-
-
-
?
3,4-dimethylphenol + NADH + H+ + O2
1,2-dihydroxy-3,4-dimethylbenzene + NAD+ + H2O
-
85% of the activity with phenol
-
?
3,4-dimethylphenol + NADH + H+ + O2
1,2-dihydroxy-3,4-dimethylbenzene + NAD+ + H2O
-
85% of the activity with phenol
-
?
3,4-dimethylphenol + NADPH + O2
?
-
72% of the activity with phenol
-
?
3,4-dimethylphenol + NADPH + O2
?
-
72% of the activity with phenol
-
?
3-chlorophenol + NADH + H+ + O2
4-chlorocatechol + NAD+ + H2O
-
15% of the activity with phenol
-
?
3-chlorophenol + NADH + H+ + O2
4-chlorocatechol + NAD+ + H2O
-
15% of the activity with phenol
-
?
3-fluorophenol + O2 + NADPH
?
-
below pH 6.5 3-fluorophenol is preferentially hydroxylated at the C6 ortho position, at increasing pH the C2 ortho-hydroxylation becomes more predominant
-
?
3-hydroxyphenol + NADPH + H+ + O2
?
-
about 60% of the activity with phenol
-
?
3-hydroxyphenol + NADPH + H+ + O2
?
-
about 60% of the activity with phenol
-
?
4-chlorophenol + NADH + H+ + O2
1,2-dihydroxy-4-methylbenzene + NAD+ + H2O
-
-
-
?
4-chlorophenol + NADH + H+ + O2
1,2-dihydroxy-4-methylbenzene + NAD+ + H2O
-
-
-
?
4-propylphenol + NADH + H+ + O2
4-propylcatechol + NAD+ + H2O
-
low activity
-
?
4-propylphenol + NADH + H+ + O2
4-propylcatechol + NAD+ + H2O
-
low activity
-
?
m-cresol + NADH + H+ + O2
4-methylcatechol + NAD+ + H2O
-
60% of the activity with phenol
-
?
o-cresol + NADH + H+ + O2
3-methylcatechol + NAD+ + H2O
-
60% of the activity with phenol
-
?
p-cresol + NADH + H+ + O2
4-methylcatechol + NAD+ + H2O
-
60% of the activity with phenol
-
?
phenol + NAD(P)H + H+ + O2
catechol + NAD(P)+ + H2O
can tolerate the phenol concentration up to 6 mM, degrades phenol through catechol ortho fission pathway
-
?
phenol + NAD(P)H + H+ + O2
catechol + NAD(P)+ + H2O
can tolerate the phenol concentration up to 6 mM, degrades phenol through catechol ortho fission pathway
-
?
phenol + NAD(P)H + H+ + O2
catechol + NAD(P)+ + H2O
-
-
?
phenol + NAD(P)H + H+ + O2
catechol + NAD(P)+ + H2O
can tolerate the phenol concentration up to 1 mM, harbors the both ortho and meta fission pathways simultaneously
-
?
phenol + NAD(P)H + H+ + O2
catechol + NAD(P)+ + H2O
can tolerate the phenol concentration up to 6 mM, harbors the both ortho and meta fission pathways simultaneously
-
?
phenol + NAD(P)H + H+ + O2
catechol + NAD(P)+ + H2O
can tolerate the phenol concentration up to 6 mM, degrades phenol through catechol ortho fission pathway
-
?
phenol + NAD(P)H + H+ + O2
catechol + NAD(P)+ + H2O
can tolerate the phenol concentration up to 6 mM, degrades phenol through catechol ortho fission pathway
-
?
phenol + NAD(P)H + H+ + O2
catechol + NAD(P)+ + H2O
A5YUW2, A5YUW3, A5YUW6, A5YUY2, A5YUY5, A5YUY6, A5YUY7, A5YUZ3, A5YUZ5, A5YUZ6, A5YUZ7, A5YUZ8, A5YUZ9, A5YV00, A5YV01, A5YV02, A5YV03, A5YV04, A5YV05, A5YV06, A5YV08, A5YV10, A5YV11, A5YV12, A5YV13, A5YV14, A5YV15, A5YV16, A5YV18, A5YV19, A5YV20
phenol degradation in the activated sludge depends on the combined activity of a number of redundant species
-
?
phenol + NADH + H+ + O2
catechol + NAD+ + H2O
-
activity is reduced by 84% when NADPH is replaced by NADH
-
?
phenol + NADH + H+ + O2
catechol + NAD+ + H2O
-
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
-
?
phenol + NADH + H+ + O2
catechol + NAD+ + H2O
-
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
-
?
phenol + NADPH + H+ + O2
catechol + NADP+ + H2O
-
100% activity
-
?
phenol + NADPH + H+ + O2
catechol + NADP+ + H2O
-
-
-
?
phenol + NADPH + H+ + O2
catechol + NADP+ + H2O
-
the enzyme catalyzes the conversion of phenols to their 2-diol derivatives
-
?
phenol + NADPH + H+ + O2
catechol + NADP+ + H2O
-
monitoring the production of catechol in a continuous coupled assay with recombinant catechol 2,3-dioxygenase from Pseudomonas sp. OX1
-
?
phenol + NADPH + H+ + O2
catechol + NADP+ + H2O
-
monitoring the production of catechol in a continuous coupled assay with recombinant catechol 2,3-dioxygenase from Pseudomonas sp. OX1
-
?
phenol + NADPH + O2
catechol + NADP+ + H2O
-
cytochrome c, 2,6-dichlorophenolindophenol, potassium ferricyanide and nitro blue tetrazolium can act as electron acceptors in vitro
-
?
phenol + NADPH + O2
catechol + NADP+ + H2O
-
high phenol degradation activity in vivo in strain TL3, catabolic pathway overview
-
?
phenol + NADPH + O2
catechol + NADP+ + H2O
-
high phenol degradation activity in vivo in strain TL3, catabolic pathway overview
-
?
phenol + NADPH + O2
catechol + NADP+ + H2O
-
initial step in phenol-degrading pathway
-
?
phenol + NADPH + O2
catechol + NADP+ + H2O
-
initial step in phenol-degrading pathway
-
?
phenol + NADPH + O2
catechol + NADP+ + H2O
-
-
-
?
phenol + NADPH + O2
catechol + NADP+ + H2O
-
reaction mechanism
-
?
phenol + O2
?
assay at 28°C, pH 6.8-7.0, concentration of phenol diversify from 25 mg/l to 800 mg/l
-
?
phenol + O2
?
utilize phenol as sole carbon and energy source, concentration of phenol diversify from 25 mg/l to 1000 mg/l, assay at 28°C, pH 6.8-7.0
-
?
phenol + O2
?
utilize phenol as sole carbon and energy source, concentration of phenol diversify from 25 mg/l to 1000 mg/l, assay at 28°C, pH 6.8-7.0
-
?
phenol + O2
?
-
assay at 28°C, pH 6.8-7.0, concentration of phenol diversify from 25 mg/l to 800 mg/l
-
?
quinol + O2 + NADPH
1,2,4-trihydroxybenzene + NADP+ + H2O
-
-
-
?
additional information
?
-
-
no PHO activity with p-hydroxybenzoic acid, m-hydroxybenzoic acid, 2,3-dinitrophenol, 3,4-dichlorophenol, 2,4,5-trichlorophenol, 2,2'-dihydroxybiphenyl and L-Tyr
-
?
additional information
?
-
-
no PHO activity with p-hydroxybenzoic acid, m-hydroxybenzoic acid, 2,3-dinitrophenol, 3,4-dichlorophenol, 2,4,5-trichlorophenol, 2,2'-dihydroxybiphenyl and L-Tyr
-
?
additional information
?
-
-
the enzyme has broad substrate specificity against isomeric diphenols, isomeric methylphenols, halogen-substituted phenols, amino-substituted phenols, nitrophenols, hydroxybenzaldehyde and hydroxylbenzoic acid
-
?
additional information
?
-
-
not: 2,4-, 2,5- and 2,6-dimethylphenols
-
?
additional information
?
-
-
broad specificity, reaction results in the formation of the corresponding o-diols
-
?
additional information
?
-
-
overview of possible reaction products of fluorinated phenols
-
?
additional information
?
-
-
first enzyme of phenol biodegradation
-
?
additional information
?
-
-
the enzyme hydroxylates phenol and several different toxic phenol derivatives, e.g. cresols, nitrophenols and hydroxyphenols, substrate specificity, overview
-
?
additional information
?
-
-
the enzyme hydroxylates phenol and several different toxic phenol derivatives, e.g. cresols, nitrophenols and hydroxyphenols, substrate specificity, overview
-
?
additional information
?
-
-
the enzyme is a hydrocarbon-oxidizing multicomponent monooxygenase, important for activity is formation of a complex between the hydroxylase and a regulatory protein component
-
?
additional information
?
-
-
the enzyme is a multicomponent phenol hydroxylase, production of dyes from indole derivatives by recombinant enzymes expressed in Escherichia coli, substrate specificities of the enzyme from strain KL28 and KL33, the products formed by the enzyme from the two strain are different, detailed overview
-
?
additional information
?
-
-
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
-
?
additional information
?
-
-
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
-
?
additional information
?
-
-
the enzyme is a hydrocarbon-oxidizing multicomponent monooxygenase, important for activity is formation of a complex between the hydroxylase and a regulatory protein component
-
?
additional information
?
-
-
the enzyme hydroxylates benzenes to catechols via the intermediate production of phenols
-
?
additional information
?
-
-
the enzyme hydroxylates benzenes to catechols via the intermediate production of phenols
-
?
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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
-
-
-
-
?
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
-
substrate only for phenol-grown cells
-
-
?
2 ethynylbenzene + NADPH + 3 O2
2-ethynylphenol + 2-hydroxy-6-oxo-octa-2,4-dien-7-ynoic acid + NADP+ + H2O
-
substrate only for phenol-grown cells
-
-
?
3 toluene + 3 NADPH + 3 H+ + 3 O2
2-cresol + 3-cresol + 4-cresol + 3 NADP+ + 3 H2O
-
-
-
-
?
3 toluene + 3 NADPH + 3 H+ + 3 O2
2-cresol + 3-cresol + 4-cresol + 3 NADP+ + 3 H2O
-
-
-
-
?
3 toluene + 3 NADPH + 3 H+ + 3 O2
2-cresol + 3-cresol + 4-cresol + 3 NADP+ + 3 H2O
-
-
-
-
?
3 toluene + 3 NADPH + 3 H+ + 3 O2
2-cresol + 3-cresol + 4-cresol + 3 NADP+ + 3 H2O
-
-
-
-
?
phenol + NADH + H+ + O2
catechol + NAD+ + H2O
-
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
-
-
?
phenol + NADH + H+ + O2
catechol + NAD+ + H2O
-
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
-
-
?
phenol + NADPH + H+ + O2
catechol + NADP+ + H2O
-
-
-
-
?
phenol + NADPH + O2
catechol + NADP+ + H2O
-
high phenol degradation activity in vivo in strain TL3, catabolic pathway overview
-
-
?
phenol + NADPH + O2
catechol + NADP+ + H2O
-
high phenol degradation activity in vivo in strain TL3, catabolic pathway overview
-
-
?
phenol + NADPH + O2
catechol + NADP+ + H2O
-
initial step in phenol-degrading pathway
-
-
?
phenol + NADPH + O2
catechol + NADP+ + H2O
-
initial step in phenol-degrading pathway
-
-
?
additional information
?
-
-
first enzyme of phenol biodegradation
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
[2Fe-2S]-center
-
under ideal conditions, the hydroxylated product yield is about 50% of the diiron centers, suggesting that the enzyme operates by half-sites reactivity mechanisms
FAD
-
2 FAD per dimer and 3 FAD per tetramer after removing FAD and reconstituting the apoenzyme with the cofactor
NADH
-
the phenol hydrolxylase component P reduces several artificial electron acceptors such as horse heart cytochrome c, 2,6-dichlorophenolindophenol, and potassium ferricyanide, with either NADH or NADPH as electron donor. NADH is preferentially used
NADPH
-
-
438777, 438779, 438780, 438781, 438782, 438783, 438784, 438785, 438786, 438789, 438791, 690215, 690216
NADPH
-
the phenol hydrolxylase component P reduces several artificial electron acceptors such as horse heart cytochrome c, 2,6-dichlorophenolindophenol, and potassium ferricyanide, with either NADH or NADPH as electron donor. NADH is preferentially used
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
Iron
-
the reductase component PHR contains one iron-sulfur cluster, whose function is electron transfer from NADH to the dinuclear iron centre of the oxygenase
additional information
-
does not contain heme, non-heme iron or copper
Fe2+
-
the enzyme contains dinuclear iron active site, structure with a Fe(II)Fe(III) oxidation state, helix E comprises part of the iron-coordinating four-helix bundle
Fe2+
-
PHK, the accessory component of the phenol hydroxylase, may be responsible for enhancing iron incorporation into the active site of the apo-hydroxylase
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
accessory component PHK of phenol hydroxylase
-
the accessory component of the phenol hydroxylase mediates inhibition of phenol hydroxylase activity, overview
-
dithiothreitol
-
dithiothreitol acts as H2O2 generator and inhibits the oxygenase component of the enzyme, catalase protects the loss of activity
ethynylbenzene
-
reversible, competitive inhibition at concentrations above 1 mM
p-chloromercuribenzoate
-
inhibition is reversed by dithiothreitol
pyridoxal 5'-phosphate
-
reversible, 50% loss of activity in 2 min at 0.5 mM
additional information
-
benzoate causes transcriptional repression of phenol utilization by transcriptional inhibition of the mph operon. MphR encoding the transcriptional activator and mphN encoding the largest subunit of multi-component phenol hydroxylase in the benA mutant are significantly downregulated (about 7- and 70fold) on the basis of mRNA levels when benzoate is added to the medium
-
additional information
-
strain IS-67 could not grow in medium supplemented with 1000 mg/l of phenol
-
additional information
strain IS-67 could not grow in medium supplemented with 1000 mg/l of phenol
-
additional information
strain IS-67 could not grow in medium supplemented with 1000 mg/l of phenol
-
additional information
strain IS-67 could not grow in medium supplemented with 1000 mg/l of phenol
-
additional information
strain IS-67 could not grow in medium supplemented with 1000 mg/l of phenol
-
additional information
strain IS-67 could not grow in medium supplemented with 1000 mg/l of phenol
-
additional information
strain IS-67 could not grow in medium supplemented with 1000 mg/l of phenol
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
following injection, dissolved oxygen increases, whereas benzene, toluene, ethylbenzene, and xylene concentrations decrease, and copies of PHE and and ring-hydroxylating toluene monooxygenase (RMO) increase indicating growth of benzene, toluene, ethylbenzene, and xylene-utilizing bacteria harboring the RMO/PHE pathway
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
Km value is 6-20times higher when phenol derivative is added before NADPH
-
additional information
additional information
-
Km values with various electron acceptors
-
additional information
additional information
-
kinetics and regioselectivity, overview
-
additional information
additional information
-
kinetic analysis of the enzyme from different strains, overview
-
additional information
additional information
-
kinetic analysis of the enzyme from different strains, overview
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
various phenolic substrates
-
additional information
additional information
-
with various electron acceptors
-
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
7.6
additional information
-
effect of pH on oxidative half-reaction
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 8.5
-
pH 6.5: about 45% of maximal activity, pH 8.5: about 30% of maximal activity, oxygenase component PHO
6.8 - 7
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
28
30
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 37
-
20°C: about 70% of maximal activity, 24°C: maximal activity, 30°C: about 40% of maximal activity, 32°C: about 65% of maximal activity, 37°C: about 30% of maximal activity, oxygenase component PHO
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
isoelectric point of the regulatory component PHI is 4.1
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene pheBA, single and multicomponent enzyme containing strains C PC24, F PC20, C PC31, F P69, B PC18, and F PC17
-
-
brenda
gene pheBA, single and multicomponent enzyme containing strains B PC30, B PC16, and EST1412
-
-
brenda
-
438779, 438781, 438782, 438784, 438785, 438789, 438791, 438793, 438794, 438796, 438798, 438799, 438800, 438801, 657449, 690215
-
-
brenda
R57, mutants able to degrade higher phenol concentration exhibits elevated specific activity
-
-
brenda
strain NBIMCC 2414, strain ATCC 46490, and strain ATCC 58094, isolated from different waste waters, gene phyA
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
high levels of specific activity when phenol is used as major carbon and energy source
brenda
additional information
-
isolated from Alcaligenes faecalis strains from activated sludge of an industrial coking wastewater treatment plant
brenda
additional information
isolated from Alcaligenes faecalis strains from activated sludge of an industrial coking wastewater treatment plant
brenda
additional information
isolated from Alcaligenes faecalis strains from activated sludge of an industrial coking wastewater treatment plant
brenda
additional information
isolated from Alcaligenes faecalis strains from activated sludge of an industrial coking wastewater treatment plant
brenda
additional information
isolated from Alcaligenes faecalis strains from activated sludge of an industrial coking wastewater treatment plant
brenda
additional information
isolated from Alcaligenes faecalis strains from activated sludge of an industrial coking wastewater treatment plant
brenda
additional information
isolated from Alcaligenes faecalis strains from activated sludge of an industrial coking wastewater treatment plant
brenda
additional information
-
isolated from Alcaligenes faecalis strains from activated sludge of an industrial coking wastewater treatment plant
brenda
additional information
isolated from Alcaligenes faecalis strains from activated sludge of an industrial coking wastewater treatment plant
brenda
additional information
-
strain KL28 is a strain that can grow on n-alkylphenols as a carbon and energy source
brenda
additional information
from bacterial communities from laboratory-scale activated sludge
brenda
additional information
from bacterial communities from laboratory-scale activated sludge
brenda
additional information
from bacterial communities from laboratory-scale activated sludge
brenda
additional information
from bacterial communities from laboratory-scale activated sludge
brenda
additional information
from bacterial communities from laboratory-scale activated sludge
brenda
additional information
from bacterial communities from laboratory-scale activated sludge
brenda
additional information
from bacterial communities from laboratory-scale activated sludge
brenda
additional information
from bacterial communities from laboratory-scale activated sludge
brenda
additional information
from bacterial communities from laboratory-scale activated sludge
brenda
additional information
from bacterial communities from laboratory-scale activated sludge
brenda
additional information
from bacterial communities from laboratory-scale activated sludge
brenda
additional information
from bacterial communities from laboratory-scale activated sludge
brenda
additional information
from bacterial communities from laboratory-scale activated sludge
brenda
additional information
from bacterial communities from laboratory-scale activated sludge
brenda
additional information
from bacterial communities from laboratory-scale activated sludge
brenda
additional information
from bacterial communities from laboratory-scale activated sludge
brenda
additional information
from bacterial communities from laboratory-scale activated sludge
brenda
additional information
from bacterial communities from laboratory-scale activated sludge
brenda
additional information
from bacterial communities from laboratory-scale activated sludge
brenda
additional information
from bacterial communities from laboratory-scale activated sludge
brenda
additional information
from bacterial communities from laboratory-scale activated sludge
brenda
additional information
from bacterial communities from laboratory-scale activated sludge
brenda
additional information
from bacterial communities from laboratory-scale activated sludge
brenda
additional information
from bacterial communities from laboratory-scale activated sludge
brenda
additional information
from bacterial communities from laboratory-scale activated sludge
brenda
additional information
from bacterial communities from laboratory-scale activated sludge
brenda
additional information
from bacterial communities from laboratory-scale activated sludge
brenda
additional information
from bacterial communities from laboratory-scale activated sludge
brenda
additional information
from bacterial communities from laboratory-scale activated sludge
brenda
additional information
from bacterial communities from laboratory-scale activated sludge
brenda
additional information
from bacterial communities from laboratory-scale activated sludge
brenda
additional information
-
microorganisms from impacted wells from an operating gasoline station with dissolved benzene, toluene, ethylbenzene, and xylene concentrations ranging from 3128 to less than 5 microg/l
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
-
the enzyme is an indicator of aerobic benzene, toluene, ethylbenzene, and xylenes biodegradation potential
physiological function
-
the enzyme is a component of the operon encoding the meta-pathway genes, it catalyzes the first step of the phenol degradative meta-pathway
additional information
additional information
-
PHK, the accessory component of the phenol hydroxylase, is neither involved in the catalytic activity of the phenol hydroxylase complex nor required for the assembly of apo-hydroxylase, but may be responsible for enhancing iron incorporation into the active site of the apo-hydroxylase
additional information
-
PHK, the accessory component of the phenol hydroxylase, is neither involved in the catalytic activity of the phenol hydroxylase complex nor required for the assembly of apo-hydroxylase, but may be responsible for enhancing iron incorporation into the active site of the apo-hydroxylase
Show AA Sequence and Transmembrane Helices (1223 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
11600
-
(alphabetagamma)2, 2 * 54000 + 2 * 37800 + 2 * 11600, oxygenase component PHO, SDS-PAGE
37800
-
(alphabetagamma)2, 2 * 54000 + 2 * 37800 + 2 * 11600, oxygenase component PHO, SDS-PAGE
54000
-
(alphabetagamma)2, 2 * 54000 + 2 * 37800 + 2 * 11600, oxygenase component PHO, SDS-PAGE
76000
76000
-
4 * 76000, non-denaturing PAGE, after expression in Escherichia coli
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
hexamer
homotetramer
tetramer
additional information
dimer
-
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
-
SDS-PAGE shows three polypeptides with molecular masses of 13000, 39000 and 60000, gel filtration experiments are consistent with the existence of a dimer
hexamer
-
(alphabetagamma)2, 2 * 54000 + 2 * 37800 + 2 * 11600, oxygenase component PHO, SDS-PAGE
hexamer
-
(alphabetagamma)2, 2 * 54000 + 2 * 37800 + 2 * 11600, oxygenase component PHO, SDS-PAGE
tetramer
-
4 * 76000, non-denaturing PAGE, after expression in Escherichia coli
additional information
-
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
-
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
-
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
-
the phenol hydroxylase complex possesses the PHL, PHN, PHO, PHM, and PHK subunits
additional information
-
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
-
the phenol hydroxylase complex possesses the PHL, PHN, PHO, PHM, and PHK subunits
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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
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C349S
-
the mutant shows 30% activity compared to the wild type enzyme
C476S
-
the mutant shows 45% activity compared to the wild type enzyme
D75N
-
the mutant shows 288% activity compared to the wild type enzyme
P261S
-
the mutant shows 15% activity compared to the wild type enzyme
R262S
-
the mutant shows 427% activity compared to the wild type enzyme
R269L
-
the mutant shows 232% activity compared to the wild type enzyme
D54N
-
slower reaction than wild type enzyme, higher dissociation constant for binding of phenol than wild type enzyme
P364S
-
only 13% of the FAD is utilized to hydroxylate the substrate phenol, when resorcinol is used as substrate, the reaction is not significantly different from the reaction of the wild type enzyme
R281M
-
slower reaction than wild type enzyme, binds the FAD cofactor more weakly than wild type enzyme
additional information
additional information
-
production ToMO mutants with modified regioselectivity compared with the regioselectivity of the wild-type protein in order to alter the ability of the recombinant upper pathway to produce methylcatechol isomers from toluene and to produce 3,4-dimethylcatechol from o-xylene, the combination of ToMO mutant E103G and phenol oxidase increases the production of 4-methylcatechol from toluene and the formation of 3,4-dimethylcatechol from o-xylene, overview
additional information
-
production ToMO mutants with modified regioselectivity compared with the regioselectivity of the wild-type protein in order to alter the ability of the recombinant upper pathway to produce methylcatechol isomers from toluene and to produce 3,4-dimethylcatechol from o-xylene, the combination of ToMO mutant E103G and phenol oxidase increases the production of 4-methylcatechol from toluene and the formation of 3,4-dimethylcatechol from o-xylene, overview
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
dilution causes considerable loss of activity and cannot be prevented by addition of proteins such as egg or serum albumin or substances of high molecular weight such as Carbowax-4000 or polyvinylpyrrolidone
-
partially purified enzyme loses considerable activity upon dialysis or aging, addition of boiled extract prepared from crude extract fully restores activity
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
anion exchanger-immobilized enzyme is stable for several months at 4°C in 0.01 M buffers at pH 7.6
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant PHK, the accessory component of the phenol hydroxylase, from Escherichia coli
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
a 7.6 kb SalI fragment of pZC1115 containing LmPH gene subcloned to pUC19 vector, resulting in recombinant plasmid pME08. Expressed in Escherichia coli DH5alpha
co-expression of phenol hydroxylase with the regulatory protein in Escherichia coli JM109, expression of selenomethionine-enzyme in Escherichia coli strain BL21(DE3)
-
co-expression with wild-type or E103 mutant toluene o-xylene monooxygenases in Escherichia coli strain JM109
-
DNA and amino acid sequence determination and analysis of diverse strains and their genes encoding the enzyme, phylogenetic analysis, sequence comparisons, overview
-
DNA and amino acid sequence determination and analysis, expression analysis
-
expressed in Escherichia coli BL21(DE3) cells
expression in Escherichia coli LE392
expression of the phenol hydroxylase gene cluster in Escherichia coli strain JM109 in the absence or presence of the phk gene
-
gene pheBA, DNA and amino acid sequence determination and analysis, expression analysis
gene phyA, DNA and amino acid sequence determinations from different strains and analysis, expression analysis, expression of the enzymes from strains R57 and ATCC 46490 in Saccharomyces cerevisiae
-
the enzyme is encoded in the ph operon, expression in Escherichia coli strain JM109
-
a 7.6 kb SalI fragment of pZC1115 containing LmPH gene subcloned to pUC19 vector, resulting in recombinant plasmid pME08. Expressed in Escherichia coli DH5alpha
a 7.6 kb SalI fragment of pZC1115 containing LmPH gene subcloned to pUC19 vector, resulting in recombinant plasmid pME08. Expressed in Escherichia coli DH5alpha
gene pheBA, DNA and amino acid sequence determination and analysis, expression analysis
-
gene pheBA, DNA and amino acid sequence determination and analysis, expression analysis
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression of mphN encoding the largest subunit of multi-component phenol hydroxylase is reduced 70fold in the presence of both phenol and benzoate. Repression of mphN transcription is specifically released in the presence of benzoate
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
degradation
environmental protection
industry
synthesis
-
the multicomponent phenol hydroxylases can be used as biocatalysts for producing dyes, e.g. indigo, and hydroxyindoles such as 7-hydroxyindole from indole and its derivatives, overview, multicomponent phenol hydroxylases may serve as potential agents for organic syntheses as well as bioremediation
additional information
degradation
-
phenol degradation, among kinetic parameters of growth, the maximum specific growth rate significantly affects the rate of contaminant degradation and is therefore an important parameter to characterise microbes in biological reatment systems
degradation
-
phenol degradation, among kinetic parameters of growth, the maximum specific growth rate significantly affects the rate of contaminant degradation and is therefore an important parameter to characterise microbes in biological reatment systems
degradation
-
phenol degradation, among kinetic parameters of growth, the maximum specific growth rate significantly affects the rate of contaminant degradation and is therefore an important parameter to characterise microbes in biological reatment systems
environmental protection
-
the enzyme is useful in degradation of industrial pollutants
environmental protection
-
the enzyme is useful in degradation of industrial pollutants
additional information
potential application of LmPH as a molecular marker for the phylogenetic analysis of phenol-degrading strains
additional information
potential application of LmPH as a molecular marker for the phylogenetic analysis of phenol-degrading strains
additional information
potential application of LmPH as a molecular marker for the phylogenetic analysis of phenol-degrading strains
additional information
potential application of LmPH as a molecular marker for the phylogenetic analysis of phenol-degrading strains
additional information
potential application of LmPH as a molecular marker for the phylogenetic analysis of phenol-degrading strains
additional information
potential application of LmPH as a molecular marker for the phylogenetic analysis of phenol-degrading strains
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Krug, M.; Straube, G.
Degradation of phenolic compounds by the yeast Candida tropicalis HP 15. II. Some properties of the first two enzymes of the degradation pathway
J. Basic Microbiol.
26
271-281
1986
Candida tropicalis
brenda
Neujahr, H.Y.; Gaal, A.
Phenol hydroxylase from yeast. Purification and properties of the enzyme from Trichosporon cutaneum
Eur. J. Biochem.
35
386-400
1973
Cutaneotrichosporon cutaneum
brenda
Nakagawa, H.; Takeda, Y.
Phenol hydroxylase
Biochim. Biophys. Acta
62
423-426
1962
Brevibacterium fuscum
brenda
Neujahr, H.Y.; Gaal, A.
Phenol hydroxylase from yeast. Sulfhydryl groups in phenol hydroxylase from Trichosporon cutaneum
Eur. J. Biochem.
58
351-357
1975
Cutaneotrichosporon cutaneum
brenda
Kjellen, K.G.; Neujahr, H.Y.
Immobilization of phenol hydroxylase
Biotechnol. Bioeng.
21
715-719
1979
Cutaneotrichosporon cutaneum
brenda
Detmer, K.; Massey, V.
Effect of monovalent anions on the mechanism of phenol hydroxylase
J. Biol. Chem.
259
11265-11272
1984
Cutaneotrichosporon cutaneum
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Effect of substrate and pH on the oxidative half-reaction of phenol hydroxylase
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Cutaneotrichosporon cutaneum
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Cutaneotrichosporon cutaneum
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Effect of anions, chaotropes, and phenol on the attachment of flavin adenine dinucleotide to phenol hydroxylase
Biochemistry
22
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1983
Cutaneotrichosporon cutaneum
brenda
Neujahr, H.Y.; Kjellen, K.G.
Phenol hydroxylase from yeast: a lysyl residue essential for binding of reduced nicotinamide adenine dinucleotide phosphate
Biochemistry
19
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Cutaneotrichosporon cutaneum
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Selitz, T.; Neujahr, H.Y.
Phenol hydroxylase from yeast. A model for phenol binding and an improved purification procedure
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Cutaneotrichosporon cutaneum
brenda
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In situ and in vitro kinetics of phenol hydroxylase
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Cutaneotrichosporon cutaneum
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Pseudomonas sp., Pseudomonas sp. CF 600
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The crystal structure of phenol hydroxylase in complex with FAD and phenol provides evidence for a concerted conformational change in the enzyme and its cofactor during catalysis
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1998
Cutaneotrichosporon cutaneum
brenda
Hino, S.; Watanabe, K.; Takahashi, N.
Phenol hydroxylase cloned from Ralstonia eutropha strain E2 exhibits novel kinetic properties
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Cupriavidus necator, Cupriavidus necator E2
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Cutaneotrichosporon cutaneum
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On the reaction mechanism of phenol hydroxylase. New information obtained by correlation of fluorescence and absorbance stopped flow studies
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268
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Cutaneotrichosporon cutaneum
brenda
Peelen, S.; Rietjens, I.M.C.M.; Boersma, M.G.; Vervoort, J.
Conversion of phenol derivatives to hydroxylated products by phenol hydroxylase from Trichosporon cutaneum. A comparison of regioselectivity and rate of conversion with calculated molecular orbital substrate characteristics
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227
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1995
Cutaneotrichosporon cutaneum
brenda
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Fluorine-19 NMR study on the pH-dependent regioselectivity and rate of the ortho-hydroxylation of 3-fluorophenol by phenol hydroxylase from Trichosporon cutaneum. Implications for the reaction mechanism
Eur. J. Biochem.
218
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1993
Cutaneotrichosporon cutaneum
brenda
Pessione, E.; Divari, S.; Griva, E.; Cavaletto, M.; Rossi, G.L.; Gilardi, G.; Giunta, C.
Phenol hydroxylase from Acinetobacter radioresistens is a multicomponent enzyme. Purification and characterization of the reductase moiety
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265
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1999
Acinetobacter radioresistens
brenda
Waters, S.; Neujahr, H.Y.
A fermentor culture for production of recombinant phenol hydroxylase
Protein Expr. Purif.
5
534-540
1994
Cutaneotrichosporon cutaneum
brenda
Waters, S.; Neujahr, H.Y.
Sources and nature of heterogeneity in recombinant phenol hydroxylase derived from the basidiomycetous soil yeast Trichosporon cutaneum
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1997
Cutaneotrichosporon cutaneum
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brenda
Xu, D.; Ballou, D.P.; Massey, V.
Studies of the mechanism of phenol hydroxylase: mutants Tyr289Phe, Asp54Asn, and Arg281Met
Biochemistry
40
12369-12378
2001
Cutaneotrichosporon cutaneum
brenda
Xu, D.; Enroth, C.; Lindqvist, Y.; Ballou, D.P.; Massey, V.
Studies of the mechanism of phenol hydroxylase: Effect of mutation of proline 364 to serine
Biochemistry
41
13627-13636
2002
Cutaneotrichosporon cutaneum
brenda
Enroth, C.
High-resolution structure of phenol hydroxylase and correction of sequence errors
Acta Crystallogr. Sect. D
59
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2003
Cutaneotrichosporon cutaneum
brenda
Cafaro, V.; Izzo, V.; Scognamiglio, R.; Notomista, E.; Capasso, P.; Casbarra, A.; Pucci, P.; Di Donato, A.
Phenol hydroxylase and toluene/o-xylene monooxygenase from Pseudomonas stutzeri OX1: interplay between two enzymes
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70
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Pseudomonas stutzeri, Pseudomonas stutzeri OX1
brenda
Alexievaa, Z.; Gerginova, M.; Zlateva, P.; Peneva, N.
Comparison of growth kinetics and phenol metabolizing enzymes of Trichosporon cutaneum R57 and mutants with modified degradation abilities
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Cutaneotrichosporon cutaneum
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brenda
Griva, E.; Pessione, E.; Divari, S.; Valetti, F.; Cavaletto, M.; Rossi, G.L.; Giunta, C.
Phenol hydroxylase from Acinetobacter radioresistens S13. Isolation and characterization of the regulatory component
Eur. J. Biochem.
270
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2003
Acinetobacter radioresistens, Acinetobacter radioresistens S13
brenda
Divari, S.; Valetti, F.; Caposio, P.; Pessione, E.; Cavaletto, M.; Griva, E.; Gribaudo, G.; Gilardi, G.; Giunta, C.
The oxygenase component of phenol hydroxylase from Acinetobacter radioresistens S13
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270
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2003
Acinetobacter radioresistens, Acinetobacter radioresistens S13
brenda
Stiborova, M.; Sucha, V.; Miksanova, M.; Paca, J.Jr.; Paca, J.
Hydroxylation of phenol to catechol by Candida tropicalis: involvement of cytochrome P450
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22
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2003
Candida tropicalis
brenda
Jeong, J.J.; Kim, J.H.; Kim, C.K.; Hwang, I.; Lee, K.
3- and 4-alkylphenol degradation pathway in Pseudomonas sp. strain KL28: genetic organization of the lap gene cluster and substrate specificities of phenol hydroxylase and catechol 2,3-dioxygenase
Microbiology
149
3265-3277
2003
Pseudomonas sp., Pseudomonas sp. KL28
brenda
Ahuatzi-Chacon, D.; Ordorica-Morales, G.; Ruiz-Ordaz, N.; Cristiani-Urbina, E.; Juarez-Ramirez, C.; Galindez-Mayer, J.
Kinetic study of phenol hydroxylase and catechol 1,2-dioxygenase dioxygenase biosynthesis by Candida tropicalis cells grown on different phenolic substrates.
World J. Microbiol. Biotechnol.
20
695-702
2004
Candida tropicalis
brenda
Teramoto, M.; Futamata, H.; Harayama, S.; Watanabe, K.
Characterization of a high-affinity phenol hydroxylase from Comamonas testosteroni R5 by gene cloning, and expression in Pseudomonas aeruginosa PAO1c
Mol. Gen. Genet.
262
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1999
Comamonas testosteroni, Comamonas testosteroni R5
brenda
Cafaro, V.; Notomista, E.; Capasso, P.; Di Donato, A.
Regiospecificity of two multicomponent monooxygenases from Pseudomonas stutzeri OX1: molecular basis for catabolic adaptation of this microorganism to methylated aromatic compounds
Appl. Environ. Microbiol.
71
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2005
Pseudomonas stutzeri, Pseudomonas stutzeri OX1
brenda
Cafaro, V.; Notomista, E.; Capasso, P.; Di Donato, A.
Mutation of glutamic acid 103 of toluene o-xylene monooxygenase as a means to control the catabolic efficiency of a recombinant upper pathway for degradation of methylated aromatic compounds
Appl. Environ. Microbiol.
71
4744-4750
2005
Pseudomonas stutzeri, Pseudomonas stutzeri OX1
brenda
Kagle, J.; Hay, A.G.
Phenylacetylene reversibly inhibits the phenol hydroxylase of Pseudomonas sp. CF600 at high concentrations but is oxidized at lower concentrations
Appl. Microbiol. Biotechnol.
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306-315
2006
Pseudomonas sp., Pseudomonas sp. CF 600
brenda
Merimaa, M.; Heinaru, E.; Liivak, M.; Vedler, E.; Heinaru, A.
Grouping of phenol hydroxylase and catechol 2,3-dioxygenase genes among phenol- and p-cresol-degrading Pseudomonas species and biotypes
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287-296
2006
Pseudomonas sp.
brenda
Sazinsky, M.H.; Dunten, P.W.; McCormick, M.S.; Didonato, A.; Lippard, S.J.
X-ray structure of a hydroxylase-regulatory protein complex from a hydrocarbon-oxidizing multicomponent monooxygenase, Pseudomonas sp. OX1 phenol hydroxylase
Biochemistry
45
15392-15404
2006
Pseudomonas sp., Pseudomonas sp. OX1
brenda