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Information on EC 1.14.13.243 - toluene 2-monooxygenase
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1.14.13.243 toluene 2-monooxygenaseIUBMB Comments
The enzyme, characterized from the bacterium Burkholderia cepacia, belongs to a class of nonheme, oxygen-dependent diiron enzymes. It contains a hydroxylase component with two binuclear iron centers, an NADH-oxidoreductase component containing FAD and a [2Fe-2S] iron-sulfur cluster, and a third component involved in electron transfer between the hydroxylase and the reductase. The enzyme dihydroxylates its substrate in two sequential hydroxylations, initially forming 2-methylphenol, which is hydroxylated to 3-methylcatechol.
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Word Map
- 1.14.13.243
- cepacia
- burkholderia
- trichloroethylene
-
mendocina
-
4-monooxygenase
-
cis-dce
-
microcosms
- m-cresol
- cis-1,2-dichloroethylene
- 1-naphthol
-
tce-degrading
-
pickettii
-
aquifer
- ethenes
- degradation
- analysis
The enzyme appears in viruses and cellular organisms
Reaction Schemes
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+
+
=
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Synonyms
toluene ortho-monooxygenase, toluene 2-monooxygenase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2-methylphenol + NADH + H+ + O2 = 3-methylcatechol + NAD+ + H2O
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
toluene,NADH:oxygen oxidoreductase (2,3-dihydroxylating)
The enzyme, characterized from the bacterium Burkholderia cepacia, belongs to a class of nonheme, oxygen-dependent diiron enzymes. It contains a hydroxylase component with two binuclear iron centers, an NADH-oxidoreductase component containing FAD and a [2Fe-2S] iron-sulfur cluster, and a third component involved in electron transfer between the hydroxylase and the reductase. The enzyme dihydroxylates its substrate in two sequential hydroxylations, initially forming 2-methylphenol, which is hydroxylated to 3-methylcatechol.
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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
2-methylphenol + NADH + H+ + O2
3-methylcatechol + NAD+ + H2O
-
-
-
?
indole + NADH + H+ + O2
isoindigo + NAD+ + H2O
Q9ANX4; Q9ANX0; Q9ANX3; Q8VSV8; Q9ANX1; Q8VSV9
-
-
?
indole + NADH + H+ + O2
isoindigo + NAD+ + H2O
Q9ANX4; Q9ANX0; Q9ANX3; Q8VSV8; Q9ANX1; Q8VSV9
-
-
?
methyl p-tolyl sulfide + NADH + H+ + O2
methyl p-tolyl sulfoxide + NAD+ + H2O
Q9ANX4; Q9ANX0; Q9ANX3; Q8VSV8; Q9ANX1; Q8VSV9
-
-
?
methyl p-tolyl sulfide + NADH + H+ + O2
methyl p-tolyl sulfoxide + NAD+ + H2O
Q9ANX4; Q9ANX0; Q9ANX3; Q8VSV8; Q9ANX1; Q8VSV9
-
-
?
naphthalene + NADH + H+ + O2
1-naphthol + NAD+ + H2O
Q9ANX4; Q9ANX0; Q9ANX3; Q8VSV8; Q9ANX1; Q8VSV9
-
-
?
naphthalene + NADH + H+ + O2
1-naphthol + NAD+ + H2O
Q9ANX4; Q9ANX0; Q9ANX3; Q8VSV8; Q9ANX1; Q8VSV9
-
-
?
thioanisole + NADH + H+ + O2
methyl phenyl sulfoxide + NAD+ + H2O
Q9ANX4; Q9ANX0; Q9ANX3; Q8VSV8; Q9ANX1; Q8VSV9
-
-
?
thioanisole + NADH + H+ + O2
methyl phenyl sulfoxide + NAD+ + H2O
Q9ANX4; Q9ANX0; Q9ANX3; Q8VSV8; Q9ANX1; Q8VSV9
-
-
?
toluene + NADH + H+ + O2
2-methylphenol + NAD+ + H2O
Q9ANX4; Q9ANX0; Q9ANX3; Q8VSV8; Q9ANX1; Q8VSV9
-
-
?
toluene + NADH + H+ + O2
2-methylphenol + NAD+ + H2O
Q9ANX4; Q9ANX0; Q9ANX3; Q8VSV8; Q9ANX1; Q8VSV9
-
-
?
toluene + NADH + H+ + O2
2-methylphenol + NAD+ + H2O
Q52570; Q52572; Q52569; Q52571; Q52573; Q52574
-
-
?
additional information
?
-
Q9ANX4; Q9ANX0; Q9ANX3; Q8VSV8; Q9ANX1; Q8VSV9
enzyme additionally oxidizes trichloroethylene, reaction of EC 1.14.13.243. All three purified toluene 2-monooxygenase protein components and NADH are required to reconstitute full trichloroethylene oxidation activity in vitro. Trichloroethylene-dependent inactivation of toluene 2-monooxygenase activity is observed
-
?
additional information
?
-
Q9ANX4; Q9ANX0; Q9ANX3; Q8VSV8; Q9ANX1; Q8VSV9
wild-type forms isoindigo via C-2 hydroxylation of the indole pyrrole. Mutant TomA3 A113G produces 4-hydroxyindole. TomA3 V106/A113 mutants with hydrophobic, polar, or charged amino acids hydroxylate indole at the C-3 and C-2 positions, forming isatin, indigo, and indirubin in a variety of distributions
-
?
additional information
?
-
Q9ANX4; Q9ANX0; Q9ANX3; Q8VSV8; Q9ANX1; Q8VSV9
wild-type forms isoindigo via C-2 hydroxylation of the indole pyrrole. Mutant TomA3 A113G produces 4-hydroxyindole. TomA3 V106/A113 mutants with hydrophobic, polar, or charged amino acids hydroxylate indole at the C-3 and C-2 positions, forming isatin, indigo, and indirubin in a variety of distributions
-
?
additional information
?
-
-
wild-type forms isoindigo via C-2 hydroxylation of the indole pyrrole. Mutant TomA3 A113G produces 4-hydroxyindole. TomA3 V106/A113 mutants with hydrophobic, polar, or charged amino acids hydroxylate indole at the C-3 and C-2 positions, forming isatin, indigo, and indirubin in a variety of distributions
-
?
additional information
?
-
Q9ANX4; Q9ANX0; Q9ANX3; Q8VSV8; Q9ANX1; Q8VSV9
enzyme additionally oxidizes trichloroethylene, reaction of EC 1.14.13.243. All three purified toluene 2-monooxygenase protein components and NADH are required to reconstitute full trichloroethylene oxidation activity in vitro. Trichloroethylene-dependent inactivation of toluene 2-monooxygenase activity is observed
-
?
additional information
?
-
-
enzyme additionally oxidizes trichloroethylene, reaction of EC 1.14.13.243. All three purified toluene 2-monooxygenase protein components and NADH are required to reconstitute full trichloroethylene oxidation activity in vitro. Trichloroethylene-dependent inactivation of toluene 2-monooxygenase activity is observed
-
?
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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-methylphenol + NADH + H+ + O2
3-methylcatechol + NAD+ + H2O
-
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
-
the 40 kDa polypeptide subunit contains one FAD and a [2Fe-2S] cluster
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Iron
Iron
-
the 211 kDa alpha2beta2gamma2 component contains five to six iron atoms
Iron
-
the 40 kDa subunit contains a [2Fe2S] cluster, and the 211 kDa alpha2beta2gamma2 component contains five to six iron atoms
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1-butyne
Q9ANX4; Q9ANX0; Q9ANX3; Q8VSV8; Q9ANX1; Q8VSV9
effective inhibitor of toluene-dependent growth, presence results in the irreversible loss of toluene- and o-cresol-dependent O2 uptake activities. Presence of oxygen, supplied as H2O2, is required for inhibition by 1-butyne
1-hexyne
Q9ANX4; Q9ANX0; Q9ANX3; Q8VSV8; Q9ANX1; Q8VSV9
effective inhibitor of toluene-dependent growth, presence results in the irreversible loss of toluene- and o-cresol-dependent O2 uptake activities
2-hexyne
Q9ANX4; Q9ANX0; Q9ANX3; Q8VSV8; Q9ANX1; Q8VSV9
effective inhibitor of toluene-dependent growth, presence results in the irreversible loss of toluene- and o-cresol-dependent O2 uptake activities
3-hexyne
Q9ANX4; Q9ANX0; Q9ANX3; Q8VSV8; Q9ANX1; Q8VSV9
effective inhibitor of toluene-dependent growth, presence results in the irreversible loss of toluene- and o-cresol-dependent O2 uptake activities
Acetylene
Q9ANX4; Q9ANX0; Q9ANX3; Q8VSV8; Q9ANX1; Q8VSV9
10-50% vol/vol gas phase required for inhibition of growth on toluene
Trichloroethylene
Q9ANX4; Q9ANX0; Q9ANX3; Q8VSV8; Q9ANX1; Q8VSV9
trichloroethylene-dependent inactivation of toluene 2-monooxygenase activity
additional information
Q9ANX4; Q9ANX0; Q9ANX3; Q8VSV8; Q9ANX1; Q8VSV9
alkynes are specific, mechanism-based inactivators of toluene 2-monooxygenase, with acetylene being relatively ineffective compared to longer alkynes
-
additional information
-
alkynes are specific, mechanism-based inactivators of toluene 2-monooxygenase, with acetylene being relatively ineffective compared to longer alkynes
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.068
methyl p-tolyl sulfide
Q9ANX4; Q9ANX0; Q9ANX3; Q8VSV8; Q9ANX1; Q8VSV9
wild-type, whole cell assay, recombinant protein, pH not specified in the publication, temperature not specified in the publication
0.129
thioanisole
Q9ANX4; Q9ANX0; Q9ANX3; Q8VSV8; Q9ANX1; Q8VSV9
wild-type, whole cell assay, recombinant protein, pH not specified in the publication, temperature not specified in the publication
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Q52570 i.e. oxidase subunit TbmB, Q52572 i.e. oxidase subunit TbmD, Q52569 i.e. subunit TbmA, Q52571 i.e. subunit TbmC, Q52573 i.e. subunit TbmE, Q52574 i.e. subunit TbmF
Q52570; Q52572; Q52569; Q52571; Q52573; Q52574
UniProt
brenda
Q9ANX4 i.e. subunit tomA1, Q9ANX0 i.e. subunit tomA5, Q9ANX3 i.e. subunit TomA2, Q8VSV8 i.e. subunit TomA3, Q9ANX1 i.e. subunit TomA4, Q8VSV9 i.e. subunit TomA0
Q9ANX4; Q9ANX0; Q9ANX3; Q8VSV8; Q9ANX1; Q8VSV9
UniProt
brenda
Q9ANX4 i.e. subunit tomA1, Q9ANX0 i.e. subunit tomA5, Q9ANX3 i.e. subunit TomA2, Q8VSV8 i.e. subunit TomA3, Q9ANX1 i.e. subunit TomA4, Q8VSV9 i.e. subunit TomA0, cf. EC 1.14.13.243
Q9ANX4; Q9ANX0; Q9ANX3; Q8VSV8; Q9ANX1; Q8VSV9
UniProt
brenda
Q9ANX4 i.e. subunit tomA1, Q9ANX0 i.e. subunit tomA5, Q9ANX3 i.e. subunit TomA2, Q8VSV8 i.e. subunit TomA3, Q9ANX1 i.e. subunit TomA4, Q8VSV9 i.e. subunit TomA0
Q9ANX4; Q9ANX0; Q9ANX3; Q8VSV8; Q9ANX1; Q8VSV9
UniProt
brenda
Q9ANX4 i.e. subunit tomA1, Q9ANX0 i.e. subunit tomA5, Q9ANX3 i.e. subunit TomA2, Q8VSV8 i.e. subunit TomA3, Q9ANX1 i.e. subunit TomA4, Q8VSV9 i.e. subunit TomA0, cf. EC 1.14.13.243
Q9ANX4; Q9ANX0; Q9ANX3; Q8VSV8; Q9ANX1; Q8VSV9
UniProt
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
-
enzyme consists of a 40 kDa polypeptide containing one FAD and a [2Fe-2S] cluster, a 10.4 kDa polypeptide that contains no identifiable metals or organic cofactors, and a 211 kDa alpha2beta2gamma2 component containing five to six iron atoms. The 40 kDa flavo-iron-sulfur protein oxidizes NADH and transfers electrons to cytochrome c, dyes, and the alpha2beta2gamma2 component, which contains the site for toluene binding and hydroxylation
physiological function
-
three-component enzyme system, consisting of a 40 kDa polypeptide containing one FAD and a [2Fe2S] cluster, a 10.4 kDa polypeptide that contains no identifiable metals or organic cofactors, and a 211 kDa alpha2beta2gamma2 component containing five to six iron atoms. The 40 kDa flavo-iron-sulfur protein oxidizes NADH and transfers electrons to cytochrome c, dyes, and the alpha2beta2gamma2 component. The 10.4 kDa component, added to the other two components and NADH, increases toluene oxidation rates 40 kDa polypeptide containing one FAD and a [2Fe2S] cluster, a 10.4 kDa polypeptide that contains no identifiable metals or organic cofactors, and a 211 kDa alpha2beta2gamma2 component containing five to six iron atoms10fold. The alpha2beta2gamma2 component contains the site for toluene binding and hydroxylation
physiological function
-
enzyme consists of a 40 kDa polypeptide containing one FAD and a [2Fe-2S] cluster, a 10.4 kDa polypeptide that contains no identifiable metals or organic cofactors, and a 211 kDa alpha2beta2gamma2 component containing five to six iron atoms. The 40 kDa flavo-iron-sulfur protein oxidizes NADH and transfers electrons to cytochrome c, dyes, and the alpha2beta2gamma2 component, which contains the site for toluene binding and hydroxylation
physiological function
-
three-component enzyme system, consisting of a 40 kDa polypeptide containing one FAD and a [2Fe2S] cluster, a 10.4 kDa polypeptide that contains no identifiable metals or organic cofactors, and a 211 kDa alpha2beta2gamma2 component containing five to six iron atoms. The 40 kDa flavo-iron-sulfur protein oxidizes NADH and transfers electrons to cytochrome c, dyes, and the alpha2beta2gamma2 component. The 10.4 kDa component, added to the other two components and NADH, increases toluene oxidation rates 40 kDa polypeptide containing one FAD and a [2Fe2S] cluster, a 10.4 kDa polypeptide that contains no identifiable metals or organic cofactors, and a 211 kDa alpha2beta2gamma2 component containing five to six iron atoms10fold. The alpha2beta2gamma2 component contains the site for toluene binding and hydroxylation
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
three-component enzyme system, consisting of a 40 kDa polypeptide, a 10.4 kDa polypeptide, and a 211 kDa alpha2beta2gamma2 component, SDS-PAGE
additional information
-
three-component enzyme system, consisting of a 40 kDa polypeptide, a 10.4 kDa polypeptide, and a 211 kDa alpha2beta2gamma2 component, SDS-PAGE
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
homology modeling of subunit structure
Q9ANX4; Q9ANX0; Q9ANX3; Q8VSV8; Q9ANX1; Q8VSV9
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A106E
Q9ANX4; Q9ANX0; Q9ANX3; Q8VSV8; Q9ANX1; Q8VSV9
mutation in hydroxylase alpha-subunit TomA3, variant degrades its natural substrate toluene 63% faster than wild-type, with 50% 2-methylphenol, 25% 3-methylphenol, and 25% 4-methylphenol being formed. Whole cells expressing the A106E variant have two times better naphthalene-to-1-naphthol activity than the wild-type, and the regiospecificity of the A106E variant is unchanged, with 98% 1-naphthol formed
A113H
Q9ANX4; Q9ANX0; Q9ANX3; Q8VSV8; Q9ANX1; Q8VSV9
mutation in subunit TomA3. Mutant enzyme produces primarily isatin from indole
A113I
Q9ANX4; Q9ANX0; Q9ANX3; Q8VSV8; Q9ANX1; Q8VSV9
mutation in subunit TomA3. Mutant enzyme produces primarily indirubin from indole
A113V
Q9ANX4; Q9ANX0; Q9ANX3; Q8VSV8; Q9ANX1; Q8VSV9
mutation in subunit TomA3, colony turns blue. Mutant enzyme produces primarily indigo from indole
V106A
Q9ANX4; Q9ANX0; Q9ANX3; Q8VSV8; Q9ANX1; Q8VSV9
mutation in subunit TomA3, colony turns green. Mutant degrades trichloroethylene, 1,1-dichloroethylene, and trans-dichloroethylene more rapidly than wild-type. Whole cells expressing the mutant synthesize 1-naphthol six times faster than wild-type enzyme
V106A/A113G
Q9ANX4; Q9ANX0; Q9ANX3; Q8VSV8; Q9ANX1; Q8VSV9
mutation in subunit TomA3. Mutant enzyme produces primarily isatin from indole
V106M
Q9ANX4; Q9ANX0; Q9ANX3; Q8VSV8; Q9ANX1; Q8VSV9
mutation of the alpha-hydroxylase subunit TomA3, improves both rate and enantioselectivity. Mutant oxidizes methyl phenyl sulfide to the corresponding sulfoxide at a rate of 3.0 nmol/min/mg protein compared with 1.6 for the wild-type enzyme, and the enantiomeric excess (pro-S) increases from 51% for the wild type to 88% for the mutant
A106E
-
mutation in hydroxylase alpha-subunit TomA3, variant degrades its natural substrate toluene 63% faster than wild-type, with 50% 2-methylphenol, 25% 3-methylphenol, and 25% 4-methylphenol being formed. Whole cells expressing the A106E variant have two times better naphthalene-to-1-naphthol activity than the wild-type, and the regiospecificity of the A106E variant is unchanged, with 98% 1-naphthol formed
A113H
-
mutation in subunit TomA3. Mutant enzyme produces primarily isatin from indole
A113I
-
mutation in subunit TomA3. Mutant enzyme produces primarily indirubin from indole
A113V
-
mutation in subunit TomA3, colony turns blue. Mutant enzyme produces primarily indigo from indole
V106A
-
mutation in subunit TomA3, colony turns green. Mutant degrades trichloroethylene, 1,1-dichloroethylene, and trans-dichloroethylene more rapidly than wild-type. Whole cells expressing the mutant synthesize 1-naphthol six times faster than wild-type enzyme
V106A/A113G
-
mutation in subunit TomA3. Mutant enzyme produces primarily isatin from indole
V106M
-
mutation of the alpha-hydroxylase subunit TomA3, improves both rate and enantioselectivity. Mutant oxidizes methyl phenyl sulfide to the corresponding sulfoxide at a rate of 3.0 nmol/min/mg protein compared with 1.6 for the wild-type enzyme, and the enantiomeric excess (pro-S) increases from 51% for the wild type to 88% for the mutant
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
Q9ANX4; Q9ANX0; Q9ANX3; Q8VSV8; Q9ANX1; Q8VSV9
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
degradation
analysis
-
enzymativc biosensor for in situ measurement of toluene using toluene ortho-monooxygenase, while an optical fiber with an oxygen-sensitive ruthenium-based phosphorescent dye serves as the transducer. The biosensor has a limit of detection of 3 microM, a linear signal range up to 100 microM, and a response time of 1 h
analysis
-
enzymativc biosensor for in situ measurement of toluene using toluene ortho-monooxygenase, while an optical fiber with an oxygen-sensitive ruthenium-based phosphorescent dye serves as the transducer. The biosensor has a limit of detection of 3 microM, a linear signal range up to 100 microM, and a response time of 1 h
degradation
Q9ANX4; Q9ANX0; Q9ANX3; Q8VSV8; Q9ANX1; Q8VSV9
coexpression of subunit TomA3 mutant V106A and an engineered epoxide hydrolase EchA from Agrobacterium radiobacter AD1, enhances the degradation of cis-dichloroethylene
degradation
Q9ANX4; Q9ANX0; Q9ANX3; Q8VSV8; Q9ANX1; Q8VSV9
expression in Pseudomonas fluorescens for removal of trichloroethylene from soils. Closed microcosms containing the constitutive monooxygenase-expressing microorganism, soil, and wheat degrade an average of 63% of the initial trichloroethylene in 4 days (20.6 nmol of trichloroethylene/day and plant), compared to 9% of the initial trichloroethylene removed by microcosms containing wild-type Pseudomonas fluorescens 2-79 inoculated wheat, uninoculated wheat, or sterile soil
degradation
-
coexpression of subunit TomA3 mutant V106A and an engineered epoxide hydrolase EchA from Agrobacterium radiobacter AD1, enhances the degradation of cis-dichloroethylene
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Johnson, G.R.; Olsen, R.H.
Nucleotide sequence analysis of genes encoding a toluene/benzene-2-monooxygenase from Pseudomonas sp. strain JS150
Appl. Environ. Microbiol.
61
3336-3346
1995
Pseudomonas sp. (Q52570 and Q52572 and Q52569 and Q52571 and Q52573 and Q52574)
brenda
Yee, D.C.; Maynard, J.A.; Wood, T.K.
Rhizoremediation of trichloroethylene by a recombinant, root-colonizing Pseudomonas fluorescens strain expressing toluene ortho-monooxygenase constitutively
Appl. Environ. Microbiol.
64
112-118
1998
Burkholderia cepacia (Q9ANX4 and Q9ANX0 and Q9ANX3 and Q8VSV8 and Q9ANX1 and Q8VSV9), Burkholderia cepacia
brenda
Yeager, C.M.; Bottomley, P.J.; Arp, D.J.; Hyman, M.R.
Inactivation of toluene 2-monooxygenase in Burkholderia cepacia G4 by alkynes
Appl. Environ. Microbiol.
65
632-639
1999
Burkholderia cepacia (Q9ANX4 and Q9ANX0 and Q9ANX3 and Q8VSV8 and Q9ANX1 and Q8VSV9), Burkholderia cepacia, Burkholderia cepacia G4 (Q9ANX4 and Q9ANX0 and Q9ANX3 and Q8VSV8 and Q9ANX1 and Q8VSV9), Burkholderia cepacia G4
brenda
Rui, L.; Kwon, Y.M.; Fishman, A.; Reardon, K.F.; Wood, T.K.
Saturation mutagenesis of toluene ortho-monooxygenase of Burkholderia cepacia G4 for enhanced 1-naphthol synthesis and chloroform degradation
Appl. Environ. Microbiol.
70
3246-3252
2004
Burkholderia cepacia (Q9ANX4 and Q9ANX0 and Q9ANX3 and Q8VSV8 and Q9ANX1 and Q8VSV9), Burkholderia cepacia G4 (Q9ANX4 and Q9ANX0 and Q9ANX3 and Q8VSV8 and Q9ANX1 and Q8VSV9), Burkholderia cepacia G4
brenda
Feingersch, R.; Shainsky, J.; Wood, T.K.; Fishman, A.
Protein engineering of toluene monooxygenases for synthesis of chiral sulfoxides
Appl. Environ. Microbiol.
74
1555-1566
2008
Burkholderia cepacia (Q9ANX4 and Q9ANX0 and Q9ANX3 and Q8VSV8 and Q9ANX1 and Q8VSV9), Burkholderia cepacia G4 (Q9ANX4 and Q9ANX0 and Q9ANX3 and Q8VSV8 and Q9ANX1 and Q8VSV9), Burkholderia cepacia G4
brenda
Rui, L.; Reardon, K.F.; Wood, T.K.
Protein engineering of toluene ortho-monooxygenase of Burkholderia cepacia G4 for regiospecific hydroxylation of indole to form various indigoid compounds
Appl. Microbiol. Biotechnol.
66
422-429
2005
Burkholderia cepacia (Q9ANX4 and Q9ANX0 and Q9ANX3 and Q8VSV8 and Q9ANX1 and Q8VSV9), Burkholderia cepacia G4 (Q9ANX4 and Q9ANX0 and Q9ANX3 and Q8VSV8 and Q9ANX1 and Q8VSV9), Burkholderia cepacia G4
brenda
Newman, L.M.; Wackett, L.P.
Purification and characterization of toluene 2-monooxygenase from Burkholderia cepacia G4
Biochemistry
34
14066-14076
1995
Burkholderia cepacia, Burkholderia cepacia G4
brenda
Zhong, Z.; Fritzsche, M.; Pieper, S.B.; Wood, T.K.; Lear, K.L.; Dandy, D.S.; Reardon, K.F.
Fiber optic monooxygenase biosensor for toluene concentration measurement in aqueous samples
Biosens. Bioelectron.
26
2407-2412
2011
Burkholderia cepacia, Burkholderia cepacia G4
brenda
Newman, L.M.; Wackett, L.P.
Trichloroethylene oxidation by purified toluene 2-monooxygenase products, kinetics, and turnover-dependent inactivation
J. Bacteriol.
179
90-96
1997
Burkholderia cepacia (Q9ANX4 and Q9ANX0 and Q9ANX3 and Q8VSV8 and Q9ANX1 and Q8VSV9), Burkholderia cepacia G4 (Q9ANX4 and Q9ANX0 and Q9ANX3 and Q8VSV8 and Q9ANX1 and Q8VSV9), Burkholderia cepacia G4
brenda
Canada, K.A.; Iwashita, S.; Shim, H.; Wood, T.K.
Directed evolution of toluene ortho-monooxygenase for enhanced 1-naphthol synthesis and chlorinated ethene degradation
J. Bacteriol.
184
344-349
2002
Burkholderia cepacia (Q9ANX4 and Q9ANX0 and Q9ANX3 and Q8VSV8 and Q9ANX1 and Q8VSV9), Burkholderia cepacia G4 (Q9ANX4 and Q9ANX0 and Q9ANX3 and Q8VSV8 and Q9ANX1 and Q8VSV9), Burkholderia cepacia G4
brenda
Rui, L.; Cao, L.; Chen, W.; Reardon, K.F.; Wood, T.K.
Active site engineering of the epoxide hydrolase from Agrobacterium radiobacter AD1 to enhance aerobic mineralization of cis-1,2-dichloroethylene in cells expressing an evolved toluene ortho-monooxygenase
J. Biol. Chem.
279
46810-46817
2004
Burkholderia cepacia (Q9ANX4 and Q9ANX0 and Q9ANX3 and Q8VSV8 and Q9ANX1 and Q8VSV9), Burkholderia cepacia G4 (Q9ANX4 and Q9ANX0 and Q9ANX3 and Q8VSV8 and Q9ANX1 and Q8VSV9)
brenda
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