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

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
1.14.13.7
-
RECOMMENDED NAME
GeneOntology No.
phenol 2-monooxygenase (NADPH)
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
phenol + NADPH + H+ + O2 = catechol + NADP+ + H2O
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Aminobenzoate degradation
-
-
chlorinated phenols degradation
-
-
Metabolic pathways
-
-
Microbial metabolism in diverse environments
-
-
phenol degradation I (aerobic)
-
-
Toluene degradation
-
-
phenol degradation
-
-
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).
CAS REGISTRY NUMBER
COMMENTARY hide
37256-84-1
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strains PHEA-2 or PHEA-12
-
-
Manually annotated by BRENDA team
strain IS-67
-
-
Manually annotated by BRENDA team
strain IS-46
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain TL3
-
-
Manually annotated by BRENDA team
strain TL3
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
strain R5
-
-
Manually annotated by BRENDA team
strain E2, formerly Alcaligenes sp.
-
-
Manually annotated by BRENDA team
strain E2, formerly Alcaligenes sp.
-
-
Manually annotated by BRENDA team
no activity in Escherichia coli
strain JM109
-
-
Manually annotated by BRENDA team
no activity in Escherichia coli JM109
strain JM109
-
-
Manually annotated by BRENDA team
no activity in Lactobacillus acidophilus
strain ATCC 4356
-
-
Manually annotated by BRENDA team
gene pheBA, single and multicomponent enzyme containing strains C PC24, F PC20, C PC31, F P69, B PC18, and F PC17
-
-
Manually annotated by BRENDA team
multicomponent enzyme containing strain PC1
-
-
Manually annotated by BRENDA team
gene pheBA, single and multicomponent enzyme containing strains B PC30, B PC16, and EST1412
-
-
Manually annotated by BRENDA team
strain CF600
-
-
Manually annotated by BRENDA team
strain KL28
-
-
Manually annotated by BRENDA team
strain OX1
-
-
Manually annotated by BRENDA team
strain 1
-
-
Manually annotated by BRENDA team
strain 1
-
-
Manually annotated by BRENDA team
strain R57
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
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
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
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
show the reaction diagram
2 ethynylbenzene + NADPH + 3 O2
2-ethynylphenol + 2-hydroxy-6-oxo-octa-2,4-dien-7-ynoic acid + NADP+ + H2O
show the reaction diagram
2,3,4-trifluorophenol + O2 + NADPH
?
show the reaction diagram
-
-
-
-
?
2,3,5,6-tetrafluorophenol + O2 + NADPH
3,4,6-trifluoro-2-benzoquinone + NADP+ + F-
show the reaction diagram
-
-
-
?
2,3,5,6-tetrafluorophenol + O2 + NADPH
?
show the reaction diagram
-
-
-
-
?
2,3,5-trifluorophenol + O2 + NADPH
?
show the reaction diagram
-
-
-
-
?
2,3,6-trifluorophenol + O2 + NADPH
?
show the reaction diagram
-
-
-
-
?
2,3-difluorophenol + O2 + NADPH
?
show the reaction diagram
-
-
-
-
?
2,4-difluorophenol + O2 + NADPH
?
show the reaction diagram
-
-
-
-
?
2,5-difluorophenol + O2 + NADPH
?
show the reaction diagram
-
-
-
-
?
2,6-difluorophenol + O2 + NADPH
?
show the reaction diagram
-
-
-
-
?
2-amino-3-methylphenol + O2 + NADPH
?
show the reaction diagram
-
-
-
-
?
2-aminophenol + O2 + NADPH
?
show the reaction diagram
2-chlorophenol + O2 + NADPH
?
show the reaction diagram
2-cresol + NADPH + O2
2-methylcatechol + 4-methylcatechol + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
2-ethylphenol + NADPH + O2
3-ethyl-benzene-1,2-diol + NADP+ + H2O
show the reaction diagram
2-fluorophenol + O2 + NADPH
?
show the reaction diagram
-
-
-
-
?
2-hydroxyphenol + NADPH + H+ + O2
?
show the reaction diagram
2-methyl-phenol + O2 + NADPH
?
show the reaction diagram
2-methylindole + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
2-nitrophenol + NADPH + H+ + O2
?
show the reaction diagram
3 toluene + 3 NADPH + 3 H+ + 3 O2
2-cresol + 3-cresol + 4-cresol + 3 NADP+ + 3 H2O
show the reaction diagram
3,4,5-trifluorophenol + O2 + NADPH
?
show the reaction diagram
-
-
-
-
?
3,4-difluorophenol + O2 + NADPH
?
show the reaction diagram
-
-
-
-
?
3,4-dimethylphenol + NADH + H+ + O2
1,2-dihydroxy-3,4-dimethylbenzene + NAD+ + H2O
show the reaction diagram
3,4-dimethylphenol + NADPH + O2
?
show the reaction diagram
3,5-difluorophenol + O2 + NADPH
?
show the reaction diagram
-
-
-
-
?
3-aminophenol + O2 + NADPH
?
show the reaction diagram
3-chloro-4-fluorophenol + O2 + NADPH
?
show the reaction diagram
-
-
-
-
?
3-chlorophenol + NADH + H+ + O2
4-chlorocatechol + NAD+ + H2O
show the reaction diagram
3-chlorophenol + O2 + NADPH
?
show the reaction diagram
3-cresol + NADPH + O2
3-methylcatechol + 4-methylcatechol + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
3-cyanoindole + NADPH + O2
?
show the reaction diagram
-
substrate only of strain KL28
-
-
?
3-ethylphenol + NADH + H+ + O2
4-ethylcatechol + NAD+ + H2O
show the reaction diagram
3-fluorophenol + O2 + NADPH
?
show the reaction diagram
3-hydroxyphenol + NADPH + H+ + O2
?
show the reaction diagram
3-hydroxyphenol + O2 + NADPH
?
show the reaction diagram
-
-
-
-
?
3-methylphenol + O2 + NADPH
?
show the reaction diagram
3-nitrophenol + NADPH + H+ + O2
?
show the reaction diagram
-
about 45% of the activity with phenol
-
-
?
4-aminophenol + O2 + NADPH
?
show the reaction diagram
4-chloro-3-fluorophenol + O2 + NADPH
?
show the reaction diagram
-
-
-
-
?
4-chlorocatechol + O2 + NADPH
?
show the reaction diagram
-
-
-
-
?
4-chlorophenol + NADH + H+ + O2
1,2-dihydroxy-4-methylbenzene + NAD+ + H2O
show the reaction diagram
4-chlorophenol + NADH + H+ + O2
4-chlorocatechol + NAD+ + H2O
show the reaction diagram
-
27% of the activity with phenol
-
-
?
4-chlorophenol + O2 + NADPH
?
show the reaction diagram
4-cresol + NADPH + O2
4-methylcatechol + NADP+ + H2O
show the reaction diagram
-
best substrate
-
-
?
4-ethylphenol + NADH + H+ + O2
4-ethylcatechol + NAD+ + H2O
show the reaction diagram
4-fluorophenol + NADH + H+ + O2
1,2-dihydroxy-4-fluorobenzene + NAD+ + H2O
show the reaction diagram
-
-
-
-
?
4-fluorophenol + O2 + NADPH
?
show the reaction diagram
-
-
-
-
?
4-hydroxyindole + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
4-hydroxyphenol + NADPH + H+ + O2
?
show the reaction diagram
-
about 120% of the activity with phenol
-
-
?
4-hydroxyphenol + O2 + NADPH
?
show the reaction diagram
-
-
-
-
?
4-methoxyindole + NADPH + O2
?
show the reaction diagram
-
substrate only of strain KL28
-
-
?
4-methyl-phenol + O2 + NADPH
?
show the reaction diagram
4-methylindole + NADPH + O2
?
show the reaction diagram
-
substrate only of strain KL28
-
-
?
4-methylphenol + NADH + H+ + O2
1,2-dihydroxy-4-methylbenzene + NAD+ + H2O
show the reaction diagram
-
-
-
-
?
4-nitrophenol + NADPH + H+ + O2
?
show the reaction diagram
-
about 50% of the activity with phenol
-
-
?
4-propylphenol + NADH + H+ + O2
4-propylcatechol + NAD+ + H2O
show the reaction diagram
5-aminoindole + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
5-fluoroindole + NADPH + O2
?
show the reaction diagram
-
substrate only of strain KL33
-
-
?
5-hydroxyindole + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
5-methoxyindole + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
5-methylindole + NADPH + O2
?
show the reaction diagram
-
substrate only of strain KL33
-
-
?
6-chloroindole + NADPH + O2
?
show the reaction diagram
-
substrate only of strain KL33
-
-
?
6-methoxyindole + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
6-methylindole + NADPH + O2
?
show the reaction diagram
-
substrate only of strain KL33
-
-
?
7-chloroindole + NADPH + O2
?
show the reaction diagram
-
substrate only of strain KL33
-
-
?
7-methylindole + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
benzene + NADPH + H+ + O2
phenol + NADP+
show the reaction diagram
benzene + NADPH + O2
?
show the reaction diagram
-
26% of the activity with phenol
-
-
?
benzene + NADPH + O2 + H+
phenol + NADP+ + H2O
show the reaction diagram
catechol + O2 + NADPH
?
show the reaction diagram
indole + NADPH + O2
7-hydroxyindole + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
m-chlorophenol + NADPH + O2
4-chloro-benzene-1,2-diol + NADP+ + H2O
show the reaction diagram
-
18% of the activity with phenol
-
-
?
m-cresol + NADH + H+ + O2
4-methylcatechol + NAD+ + H2O
show the reaction diagram
m-cresol + NADPH + H+ + O2
3-methylcatechol + 4-methylcatechol + NADP+
show the reaction diagram
m-cresol + NADPH + O2
?
show the reaction diagram
-
114% of the activity with phenol
-
-
?
metol + O2 + NADPH
?
show the reaction diagram
-
-
-
-
?
o-chlorophenol + NADPH + O2
3-chloro-benzene-1,2-diol + NADP+ + H2O
show the reaction diagram
-
20% of the activity with phenol
-
-
?
o-cresol + NADH + H+ + O2
3-methylcatechol + NAD+ + H2O
show the reaction diagram
o-cresol + NADPH + O2
3-methylcatechol + NADP+ + H2O
show the reaction diagram
-
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
-
-
?
orcinol + NADPH + O2
?
show the reaction diagram
-
46% of the activity with phenol
-
-
?
orcinol + O2 + NADPH
?
show the reaction diagram
oxindole + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
p-chlorophenol + NADPH + O2
?
show the reaction diagram
-
84% of the activity with phenol
-
-
?
p-cresol + NADH + H+ + O2
4-methylcatechol + NAD+ + H2O
show the reaction diagram
p-cresol + NADPH + O2
4-methylcatechol + NADP+ + H2O
show the reaction diagram
-
114% of the activity with phenol
-
-
?
pentafluorophenol + O2 + NADPH
?
show the reaction diagram
-
-
-
-
?
phenol + NAD(P)H + H+ + O2
catechol + NAD(P)+ + H2O
show the reaction diagram
phenol + NADH + H+ + O2
catechol + NAD+ + H2O
show the reaction diagram
phenol + NADPH + H+ + O2
catechol + NADP+
show the reaction diagram
phenol + NADPH + H+ + O2
catechol + NADP+ + H2O
show the reaction diagram
phenol + NADPH + O2
?
show the reaction diagram
-
enzyme of phenol degradation pathway
-
-
?
phenol + NADPH + O2
catechol + NADP+ + H2O
show the reaction diagram
phenol + O2
?
show the reaction diagram
phloroglucinol + O2 + NADPH
?
show the reaction diagram
quinol + NADPH + O2
?
show the reaction diagram
-
63% of the activity with phenol
-
-
?
quinol + O2 + NADPH
1,2,4-trihydroxybenzene + NADP+ + H2O
show the reaction diagram
resorcinol + NADPH + O2
?
show the reaction diagram
thiophenol + O2 + NADPH
?
show the reaction diagram
-
-
-
-
?
toluene + NADPH + H+ + O2
o-cresol + m-cresol + p-cresol + NADP+
show the reaction diagram
toluene + NADPH + O2
?
show the reaction diagram
-
28% of the activity with phenol
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
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
show the reaction diagram
2 ethynylbenzene + NADPH + 3 O2
2-ethynylphenol + 2-hydroxy-6-oxo-octa-2,4-dien-7-ynoic acid + NADP+ + H2O
show the reaction diagram
3 toluene + 3 NADPH + 3 H+ + 3 O2
2-cresol + 3-cresol + 4-cresol + 3 NADP+ + 3 H2O
show the reaction diagram
benzene + NADPH + O2 + H+
phenol + NADP+ + H2O
show the reaction diagram
phenol + NADH + H+ + O2
catechol + NAD+ + H2O
show the reaction diagram
phenol + NADPH + H+ + O2
catechol + NADP+ + H2O
show the reaction diagram
phenol + NADPH + O2
?
show the reaction diagram
-
enzyme of phenol degradation pathway
-
-
?
phenol + NADPH + O2
catechol + NADP+ + H2O
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cytochrome P450
-
essential component of the enzyme system
-
NADPH
[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
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Anions
-
effect of anions on attachment of flavin
Cu2+
-
participation of Cu2+ in reaction
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
Monovalent anions
-
effect on mechanism
additional information
-
does not contain heme, non-heme iron or copper
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
-
slight inhibition at 0.0005 to 0.001 mM
2-Fluorophenol
-
substrate inhibition
3-chlorophenol
-
substrate inhibition
3-Fluorophenol
-
substrate inhibition
4-Chlorophenol
-
substrate inhibition
4-Fluorophenol
-
substrate inhibition
5,5'-dithiobis(2-nitrobenzoate)
-
-
acetate
-
50% inhibition at 0.123 M
AgNO3
-
0.01 mM
ammonium sulfate
-
-
ascorbate
-
52% inhibition at 50 mM
Br-
-
50% inhibition at 0.072 M
catechol
-
substrate inhibition
CN-
-
50% inhibition at 0.004 M
Copper-chelating agents
-
CuSO4
-
0.01 mM
dithiothreitol
-
dithiothreitol acts as H2O2 generator and inhibits the oxygenase component of the enzyme, catalase protects the loss of activity
ethylene glycol
-
-
ethynylbenzene
-
reversible, competitive inhibition at concentrations above 1 mM
F-
-
50% inhibition at 0.01 M
FeSO4
-
0.1 mM
formaldehyde
-
-
Glutardialdehyde
-
-
glutathione
-
-
Guanidinium chloride
-
70-80% inhibition at 0.1 M
H2O2
-
71% inhibition at 0.1 M
HgCl2
-
0.01 mM
I-
-
50% inhibition at 0.05 M
NO3-
-
50% inhibition at 0.035 M
p-chloromercuribenzoate
-
inhibition is reversed by dithiothreitol
p-hydroxymercuribenzoate
-
-
Peroxidase
-
-
-
phenol
PHK
-
the accessory component of the phenol hydroxylase mediates inhibition of phenol hydroxylase activity, overview
-
phosphate
-
60-70% inhibition at 5 mM
potassium ethylxanthate
-
1 mM
pyridoxal 5'-phosphate
-
reversible, 50% loss of activity in 2 min at 0.5 mM
pyridoxamine phosphate
-
slight
resorcinol
-
substrate inhibition
Sodium borohydride
-
-
Sodium diethyldithiocarbamate
-
1 mM
Sodium dithionite
-
-
trichloroacetate
-
complete inhibition at 0.1 M
Triton X-100
-
-
Urea
-
70-80% inhibition at 2 M
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
dithiothreitol
-
20% increase of activity at 1 mM
PEG 400
-
slight increase
Thiophenol
-
binds to the enzyme and stimulates NADPH oxidation
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
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0031
2-Cresol
-
25C, recombinant enzyme
0.005
2-Fluorophenol
-
-
0.0325
2-xylene
-
25C, recombinant enzyme
0.055
3-chlorophenol
-
-
0.0018
3-cresol
-
25C, recombinant enzyme
0.008
3-Fluorophenol
-
-
0.039
4-Chlorophenol
-
-
0.0006
4-Cresol
-
25C, recombinant enzyme
0.017
4-Fluorophenol
-
-
0.025
Benzene
-
25C, recombinant enzyme
0.012
catechol
-
-
0.03779
NADH
-
phenol hydrolxylase component P
0.03 - 1.7
NADPH
0.0006 - 1.7
phenol
0.0015 - 0.032
resorcinol
0.022
Toluene
-
25C, recombinant enzyme
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.95
2-Cresol
Pseudomonas stutzeri
-
25C, recombinant enzyme
0.125
2-xylene
Pseudomonas stutzeri
-
25C, recombinant enzyme
0.61
3-cresol
Pseudomonas stutzeri
-
25C, recombinant enzyme
0.77
4-Cresol
Pseudomonas stutzeri
-
25C, recombinant enzyme
0.1
Benzene
Pseudomonas stutzeri
-
25C, recombinant enzyme
1980
NADH
Acinetobacter radioresistens
-
oxygenase component PHO
2.08 - 11.5
NADPH
Trichosporon cutaneum
-
value depends on phenolic substrate
0.286 - 1980
phenol
0.15
Toluene
Pseudomonas stutzeri
-
25C, recombinant enzyme
4.5 - 13.2
various phenolic substrates
Trichosporon cutaneum
-
-
-
additional information
additional information
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
30.8
2-Fluorophenol
-
-
2.3
3-chlorophenol
-
-
6.3
3-Fluorophenol
-
-
2.6
4-Chlorophenol
-
-
2.3
4-Fluorophenol
-
-
12.5
catechol
-
-
0.17 - 9.41
phenol
1.8
resorcinol
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.083
-
cells grown at 30C on phenol as sole carbon source
0.087
-
cells grown at 25C on phenol as sole carbon source
0.78 - 1.4
-
-
0.84
-
tetrameric form
1.5
-
reconstituted tetrameric form
2.3
-
dimeric form
2.6
-
reconstituted dimeric form
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5
-
complete utilization of 0.5 g/l phenol in 6 days
7
-
assay at
7.2 - 7.6
-
in phosphate buffer
7.4
-
assay at
7.6
-
assay at
8.2
-
in Tris-Cl buffer
additional information
-
effect of pH on oxidative half-reaction
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 8.5
-
pH 6.5: about 45% of maximal activity, pH 8.5: about 30% of maximal activity, oxygenase component PHO
7 - 8.7
-
about 50% of activity maximum at pH 7.0 and 8.7
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
-
assay at room temperature
24
-
and a second smaller peak at 32C
40
-
enzyme from phenol-induced cells
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 37
-
20C: about 70% of maximal activity, 24C: maximal activity, 30C: about 40% of maximal activity, 32C: about 65% of maximal activity, 37C: about 30% of maximal activity, oxygenase component PHO
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.7
-
oxygenase component PHO
additional information
-
isoelectric point of the regulatory component PHI is 4.1
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
low activity
Manually annotated by BRENDA team
-
16fold higher activity than in cytosol
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
11600
-
(alphabetagamma)2, 2 * 54000 + 2 * 37800 + 2 * 11600, oxygenase component PHO, SDS-PAGE
25500
-
PHK accessory protein
37800
-
(alphabetagamma)2, 2 * 54000 + 2 * 37800 + 2 * 11600, oxygenase component PHO, SDS-PAGE
38800
-
gel filtration
54000
-
(alphabetagamma)2, 2 * 54000 + 2 * 37800 + 2 * 11600, oxygenase component PHO, SDS-PAGE
60000
-
4 * 60000, SDS-PAGE
67000
-
SDS-PAGE
148000
-
gel filtration
207000
-
oxygenase component PHO, gel filtration
240000
-
gel filtration
302000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexamer
tetramer
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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, 20C, 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 resolution, molecular replacement, Single-wavelength anomalous dispersion data for the selenomethionine derivative
-
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
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5
-
stable for at least 7 days
438777
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4
-
stable for some hours
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
chloride destabilizes
-
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
-
longer exposure to ultrasound drastically reduces enzyme activity
-
partially purified enzyme loses considerable activity upon dialysis or aging, addition of boiled extract prepared from crude extract fully restores activity
-
phosphate stabilizes
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 4-6 weeks stable
-
-70C, 6 months stable
-
anion exchanger-immobilized enzyme is stable for several months at 4C in 0.01 M buffers at pH 7.6
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
oxygenase component PHO
-
purification of the oxygenase component
-
recombinant PHK, the accessory component of the phenol hydroxylase, from Escherichia coli
-
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
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; expression in Escherichia coli LE392; expression in Escherichia coli LE392; expression in Escherichia coli LE392; expression in Escherichia coli LE392; expression in Escherichia coli LE392; expression in Escherichia coli LE392
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
-
expression in Pseudomonas aeruginosa PAO1c
-
expression of enzyme from strain KL33 and KL28 in Escherichia coli
-
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
-
oxygenase component PHO
-
the enzyme is encoded in the ph operon, expression in Escherichia coli strain JM109
-
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
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
Y298F
-
binds phenol more weakly than wild type enzyme
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
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
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