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Information on EC 1.14.12.3 - benzene 1,2-dioxygenase
for references in articles please use BRENDA:EC1.14.12.3
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EC Tree 1 Oxidoreductases
1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
1.14.12 With NADH or NADPH as one donor, and incorporation of two atoms of oxygen into the other donor
1.14.12.3 benzene 1,2-dioxygenase
IUBMB Comments
A system, containing a reductase which is an iron-sulfur flavoprotein (FAD), an iron-sulfur oxygenase and ferredoxin. Requires Fe2+.
The enzyme appears in viruses and cellular organisms
- 1.14.12.3
- putida
- toluene
-
rieske
-
rieske-type
- dihydrodiol
-
cis-benzene
- 4-methoxybenzoate
-
iron-sulphur
-
ring-hydroxylating
- ethylbenzene
- analysis
showSynonyms
benzene dioxygenase, benzene hydroxylase, benzene 1,2-dioxygenase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
BDO
BED
benzene dioxygenase
benzene hydroxylase
oxygenase, benzene 1,2-di-
-
-
-
-
additional information
-
enzyme system consisting of three components: a flavoprotein reductase, a ferredoxin and a catalytic iron sulfur protein
BDO
-
-
-
-
benzene dioxygenase
-
-
-
-
benzene hydroxylase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
benzene + NADH + H+ + O2 = cis-cyclohexa-3,5-diene-1,2-diol + NAD+
-
-
-
-
benzene + NADH + H+ + O2 = cis-cyclohexa-3,5-diene-1,2-diol + NAD+
the catalytic iron-sulfur proteins of the enzyme consist of two dissimilar alpha and beta subunits, the alpha subunit contains a [2Fe-2S] cluster involved in electron transfer, the catalytic nonheme iron center, and is also responsible for substrate specificity
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
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redox reaction
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-
-
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reduction
-
-
-
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PATHWAY SOURCE
PATHWAYS
KEGG
MetaCyc
benzene degradation I (aerobic)
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SYSTEMATIC NAME
IUBMB Comments
benzene,NADH:oxygen oxidoreductase (1,2-hydroxylating)
A system, containing a reductase which is an iron-sulfur flavoprotein (FAD), an iron-sulfur oxygenase and ferredoxin. Requires Fe2+.
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CAS REGISTRY NUMBER
COMMENTARY
9075-66-5
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2 cyclohexene + 2 O2 + 2 NADH + 2 H+
2-cyclohexen-1-ol + cis-1,2-cyclohexanediol + 2 NAD+ + H2O
benzene + NADPH + O2
cis-cyclohexa-3,5-diene-1,2-diol + NADP+
-
Substrates: activity with NADPH is 10% of the activity with NADH
Products: -
Products: -
?
ethylbenzene + NADH + O2
cis-2,3-dihydroxy-1-ethyl-cyclohexa-4,6-diene + 1-phenethyl alcohol + NAD+
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Substrates: -
Products: -
Products: -
?
ethylbenzene + [reduced NADPH-hemoprotein reductase] + O2
cis-2,3-dihydroxy-1-ethyl-cyclohexa-4,6-diene + [oxidized NADPH-hemoprotein reductase] + H2O
-
Substrates: -
Products: -
Products: -
?
toluene + NADH + O2
cis-2,3-dihydroxy-1-methyl-cyclohexa-4,6-diene + NAD+
-
Substrates: -
Products: -
Products: -
?
2 cyclohexene + 2 O2 + 2 NADH + 2 H+
2-cyclohexen-1-ol + cis-1,2-cyclohexanediol + 2 NAD+ + H2O
-
Substrates: -
Products: -
Products: -
?
2 cyclohexene + 2 O2 + 2 NADH + 2 H+
2-cyclohexen-1-ol + cis-1,2-cyclohexanediol + 2 NAD+ + H2O
-
Substrates: -
Products: failure of transformed bacteria to grow on cyclohexene is attributed to the toxicity of metabolic intermediates accumulating from the 2-cyclohexen-1-ol metabolism, cyclohexene metabolism pathways, overview
Products: failure of transformed bacteria to grow on cyclohexene is attributed to the toxicity of metabolic intermediates accumulating from the 2-cyclohexen-1-ol metabolism, cyclohexene metabolism pathways, overview
?
benzene + NADH + H+ + O2
cis-cyclohexa-3,5-diene-1,2-diol + NAD+
-
Substrates: -
Products: -
Products: -
?
benzene + NADH + H+ + O2
cis-cyclohexa-3,5-diene-1,2-diol + NAD+
-
Substrates: -
Products: -
Products: -
?
benzene + NADH + O2
(1R,2S)-cis-cyclohexa-3,5-diene-1,2-diol + NAD+
-
Substrates: -
Products: -
Products: -
?
benzene + NADH + O2
(1R,2S)-cis-cyclohexa-3,5-diene-1,2-diol + NAD+
-
Substrates: bioremediation of aromatic environmental pollutants, initial step of benzene degradation
Products: -
Products: -
?
benzene + NADH + O2
?
-
Substrates: reaction in benzene catabolism
Products: -
Products: -
?
benzene + NADH + O2
?
-
Substrates: reaction in benzene catabolism
Products: -
Products: -
?
benzene + NADH + O2
?
-
Substrates: reaction in benzene catabolism
Products: -
Products: -
?
benzene + NADH + O2
cis-cyclohexa-3,5-diene-1,2-diol + NAD+
-
Substrates: -
Products: -
Products: -
?
benzene + NADH + O2
cis-cyclohexa-3,5-diene-1,2-diol + NAD+
-
Substrates: -
Products: the enzyme oxidizes cyclohexene to a mixture of two products, a monohydroxylated 2-cyclohexen-1-ol product and a dihydroxylated cis-1,2-cyclohexanediol
Products: the enzyme oxidizes cyclohexene to a mixture of two products, a monohydroxylated 2-cyclohexen-1-ol product and a dihydroxylated cis-1,2-cyclohexanediol
?
benzene + NADH + O2
cis-cyclohexa-3,5-diene-1,2-diol + NAD+
-
Substrates: -
Products: -
Products: -
?
benzene + NADH + O2
cis-cyclohexa-3,5-diene-1,2-diol + NAD+
-
Substrates: -
Products: the enzyme oxidizes cyclohexene to a mixture of two products, a monohydroxylated 2-cyclohexen-1-ol product and a dihydroxylated cis-1,2-cyclohexanediol
Products: the enzyme oxidizes cyclohexene to a mixture of two products, a monohydroxylated 2-cyclohexen-1-ol product and a dihydroxylated cis-1,2-cyclohexanediol
?
benzene + NADH + O2
cis-cyclohexa-3,5-diene-1,2-diol + NAD+
-
Substrates: -
Products: -
Products: -
?
benzene + NADH + O2
cis-cyclohexa-3,5-diene-1,2-diol + NAD+
Substrates: -
Products: -
Products: -
?
benzene + O2 + NADH
cis-cyclohexa-3,5-diene-1,2-diol + NAD+
-
Substrates: -
Products: -
Products: -
?
benzene + O2 + NADH
cis-cyclohexa-3,5-diene-1,2-diol + NAD+
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Substrates: best substrate
Products: -
Products: -
?
benzene + O2 + NADH
cis-cyclohexa-3,5-diene-1,2-diol + NAD+
-
Substrates: -
Products: -
Products: -
?
benzene + O2 + NADH
cis-cyclohexa-3,5-diene-1,2-diol + NAD+
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Substrates: best substrate
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2 cyclohexene + 2 O2 + 2 NADH + 2 H+
2-cyclohexen-1-ol + cis-1,2-cyclohexanediol + 2 NAD+ + H2O
-
Substrates: -
Products: failure of transformed bacteria to grow on cyclohexene is attributed to the toxicity of metabolic intermediates accumulating from the 2-cyclohexen-1-ol metabolism, cyclohexene metabolism pathways, overview
Products: failure of transformed bacteria to grow on cyclohexene is attributed to the toxicity of metabolic intermediates accumulating from the 2-cyclohexen-1-ol metabolism, cyclohexene metabolism pathways, overview
?
benzene + NADH + O2
(1R,2S)-cis-cyclohexa-3,5-diene-1,2-diol + NAD+
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Substrates: bioremediation of aromatic environmental pollutants, initial step of benzene degradation
Products: -
Products: -
?
benzene + NADH + H+ + O2
cis-cyclohexa-3,5-diene-1,2-diol + NAD+
-
Substrates: -
Products: -
Products: -
?
benzene + NADH + H+ + O2
cis-cyclohexa-3,5-diene-1,2-diol + NAD+
-
Substrates: -
Products: -
Products: -
?
benzene + NADH + O2
?
-
Substrates: reaction in benzene catabolism
Products: -
Products: -
?
benzene + NADH + O2
?
-
Substrates: reaction in benzene catabolism
Products: -
Products: -
?
benzene + NADH + O2
?
-
Substrates: reaction in benzene catabolism
Products: -
Products: -
?
benzene + O2 + NADH
cis-cyclohexa-3,5-diene-1,2-diol + NAD+
-
Substrates: -
Products: -
Products: -
?
benzene + O2 + NADH
cis-cyclohexa-3,5-diene-1,2-diol + NAD+
-
Substrates: -
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ferredoxin
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the benzene dioxygenase comprises three components: 1. flavoprotein, NADH:ferredoxin oxidoreductase, 2. an intermediate electron-transfer protein, or ferredoxin and 3. a terminal dioxygenase
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
Iron
Fe2+
-
the benzene dioxygenase comprises three components: 1. flavoprotein, NADH:ferredoxin oxidoreductase, 2. an intermediate electron-transfer protein, or ferredoxin with a [2Fe-2S] cluster and 3. a terminal dioxygenase, containing two [2Fe-2S]iron-sulfur clusters which require two additional Fe2+ atoms/molecules for oxygenase activity
Fe2+
-
the terminal dioxygenase component contains two Fe2+ ions per molecule in addition to two [2Fe-2S] iron-sulfur clusters
Fe2+
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the alpha subunit of the enzyme contains a catalytic [2Fe-2S] cluster involved in electron transfer, the catalytic nonheme iron center is also responsible for substrate specificity, overview
Iron
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the terminal dioxygenase component contains two Fe2+ ions per molecule in addition to two [2Fe-2S] iron-sulfur clusters. The ferredoxin component contains one [2Fe-2S] cluster
Iron
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Rieske-type [2Fe-2S] centres are coordinated by two histidines and two cysteines
Iron
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the sequence of the ferredoxin component of the benzene dioxygenase contains five Cys residues, four of which are required to coordinate the iron-sulfur cluster
Iron
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the intermediate electron-carrying protein possesses on [2Fe-2S] cluster, the terminal dioxygenase possesses 2 [2Fe-2S] clusters
Iron
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the terminal dioxygenase protein [2Fe-2S] centres, in the oxidized form the two iron atoms within the centre are high-spin ferric
Iron
-
the benzene dioxygenase comprises three components: 1. flavoprotein, NADH:ferredoxin oxidoreductase, 2. an intermediate electron-transfer protein, or ferredoxin with a [2Fe-2S] cluster and 3. a terminal dioxygenase, containing two [2Fe-2S]iron-sulfur clusters which require two additional Fe2+ atoms/molecules for oxygenase activity
Iron
-
the terminal dioxygenase component contains 2 atoms of iron and 3 atoms of inorganic sulfur
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0049
-
recombinant enzyme expressed in Escherichia coli, substrate cyclohexene
0.0077
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recombinant enzyme expressed in Escherichia coli, substrate 1-methylcyclohexene
0.0086
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recombinant enzyme expressed in Escherichia coli, substrate 3-methylcyclohexene
0.0172
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recombinant enzyme expressed in Escherichia coli, substrate toluene
0.0236
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recombinant enzyme expressed in Escherichia coli, substrate benzene
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line Links Show AA Sequence and Transmembrane Helices (171 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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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
11860
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ferredoxin component of the benzene dioxygenase, fast atom bombardment mass spectrometry
23500
42000
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alpha2, beta2, 2 * 54500 + 2 * 23500, terminal dioxygenase component. 2 * 42000, reductase component. The ferredoxin component has a MW of 12300 Da
54500
55000
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55000 Da is the MW of the alpha-subunit of the terminal dioxygenase
23500
-
alpha2, beta2, 2 * 54500 + 2 * 23500, terminal dioxygenase component. 2 * 42000, reductase component. The ferredoxin component has a MW of 12300 Da
54500
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alpha2, beta2, 2 * 54500 + 2 * 23500, terminal dioxygenase component. 2 * 42000, reductase component. The ferredoxin component has a MW of 12300 Da
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
tetramer
additional information
?
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alpha2, beta2, 2 * 54500 + 2 * 23500, terminal dioxygenase component. 2 * 42000, reductase component. The ferredoxin component has a MW of 12300 Da
?
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alpha2, beta2, 2 * 54500 + 2 * 23500, terminal dioxygenase component. 2 * 42000, reductase component. The ferredoxin component has a MW of 12300 Da
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dimer
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the enzyme consist of two dissimilar alpha and beta subunits, alpha subunit structure modeling
additional information
-
the benzene dioxygenase comprises three components: 1. flavoprotein, NADH:ferredoxin oxidoreductase, 2. an intermediate electron-transfer protein, or ferredoxin and 3. a terminal dioxygenase
additional information
-
the benzene dioxygenase comprises three components: 1. flavoprotein, NADH:ferredoxin oxidoreductase, 2. an intermediate electron-transfer protein, or ferredoxin and 3. a terminal dioxygenase
additional information
-
55000 Da is the MW of the alpha-subunit of the terminal dioxygenase
additional information
-
the benzene dioxygenase comprises three components: 1. flavoprotein, NADH:ferredoxin oxidoreductase, 2. an intermediate electron-transfer protein, or ferredoxin and 3. a terminal dioxygenase
-
additional information
-
55000 Da is the MW of the alpha-subunit of the terminal dioxygenase
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H119C
-
the mutant alpha-subunit of the terminal dioxygenase is unable to coordinate an EPR-detectable Rieske [2Fe-2S] cluster with the characteristic g factors
H222M
-
in the reconstitution assay with the reductase component, the ferredoxin component and the beta-subunit of terminal dioxygenase the mutant alpha-subunit is unable to reconstitute dioxygenase activity
H228C
-
in the reconstitution assay with the reductase component, the ferredoxin component and the beta-subunit of terminal dioxygenase the mutant alpha-subunit is unable to reconstitute dioxygenase activity
H98C
-
the mutant alpha-subunit of the terminal dioxygenase is unable to coordinate an EPR-detectable Rieske [2Fe-2S] cluster with the characteristic g factors, detection of a novel EPR spectrum, the intensity of the spectrum is approximately 8% from the wild-type
I301V
-
the mutation in the C-terminal part of subunit alpha enhances the substrate specificity for ethylbenzene, the mutant shows altered patterns of products formed from toluene and ethylbenzene, including monohydroxylated side chains
I301V/T305S/I307L/L309V
I307L
-
the mutation in the C-terminal part of subunit alpha enhances the substrate specificity for ethylbenzene, the mutant shows altered patterns of products formed from toluene and ethylbenzene, including monohydroxylated side chains
L309V
-
the mutation in the C-terminal part of subunit alpha enhances the substrate specificity for ethylbenzene, the mutant shows altered patterns of products formed from toluene and ethylbenzene, including monohydroxylated side chains
T305S
-
the mutation in the C-terminal part of subunit alpha enhances the substrate specificity for ethylbenzene, the mutant shows altered patterns of products formed from toluene and ethylbenzene, including monohydroxylated side chains
Y118S
-
the mutant alpha-subunit of the terminal dioxygenase shows an EPR spectrum of half the intensity of that of the wild-type. In the reconstitution assay with the reductase component, the ferredoxin component and the beta-subunit of terminal dioxygenase it shows significantly reduced activities
Y221A
-
in the reconstitution assay with the reductase component, the ferredoxin component and the beta-subunit of terminal dioxygenase the mutant alpha-subunit shows significantly reduced activity
H119C
-
the mutant alpha-subunit of the terminal dioxygenase is unable to coordinate an EPR-detectable Rieske [2Fe-2S] cluster with the characteristic g factors
-
H222M
-
in the reconstitution assay with the reductase component, the ferredoxin component and the beta-subunit of terminal dioxygenase the mutant alpha-subunit is unable to reconstitute dioxygenase activity
-
H98C
-
the mutant alpha-subunit of the terminal dioxygenase is unable to coordinate an EPR-detectable Rieske [2Fe-2S] cluster with the characteristic g factors, detection of a novel EPR spectrum, the intensity of the spectrum is approximately 8% from the wild-type
-
Y118S
-
the mutant alpha-subunit of the terminal dioxygenase shows an EPR spectrum of half the intensity of that of the wild-type. In the reconstitution assay with the reductase component, the ferredoxin component and the beta-subunit of terminal dioxygenase it shows significantly reduced activities
-
Y221A
-
in the reconstitution assay with the reductase component, the ferredoxin component and the beta-subunit of terminal dioxygenase the mutant alpha-subunit shows significantly reduced activity
-
additional information
I301V/T305S/I307L/L309V
-
the mutations in the C-terminal part of subunit alpha enhance the substrate specificity for ethylbenzene, the quadruple mutant also shows a high uncoupled rate of electron transfer without product formation
additional information
-
construction of chimeric proteins and mutants of the benzene dioxygenase alpha subunit, the chimera are formed by benzene and toluene dioxygenases, the amino acid sequences of the alpha subunits of both enzymes differ at only 33 of 450 amino acids, these residues are primarily responsible for the change in specificity, the chimeric protein containing toluene dioxygenase C-terminal region residues 281 to 363 shows greater substrate preference for alkyl benzenes, identification of four amino acid substitutions in this region, I301V, T305S, I307L, and L309V, that particularly enhance the preference for ethylbenzene, structure modeling, overview
additional information
-
establishing of a detection system to monitor environmental benzene contamination by co-expression of benzene dioxygenase with benzene dihydrodiol dehydrogenase in Escherichia coli. The procedures involving whole-cell bioassays determine the concentration of benzene through benzene dioxygenase activity, which allows for direct correlation of oxygen consumption, and through the benzene dihydrodiol dehydrogenase that causes catechol accumulation and restores NADH necessary for the activity of the first enzyme
additional information
-
establishing of a detection system to monitor environmental benzene contamination by co-expression of benzene dioxygenase with benzene dihydrodiol dehydrogenase in Escherichia coli. The procedures involving whole-cell bioassays determine the concentration of benzene through benzene dioxygenase activity, which allows for direct correlation of oxygen consumption, and through the benzene dihydrodiol dehydrogenase that causes catechol accumulation and restores NADH necessary for the activity of the first enzyme
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
iron-sulfur proteins of the benzene dioxygenase system: 1.intermediate electron-carrying protein and terminal dioxygenase
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli strain DH5alpha and JM109, co-expression with benzene dihydrodiol dehydrogenase under the control of the Ptac promoter or without any induction. The recombinant strains expressing the BED and the BDDH enzymes transform benzene into dihydrodiol with corresponding consumption of oxygen and regenerate NADH by converting dihydrodiol to catechol
-
expression of the alpha-subunit and the beta-subunit of terminal dioxygenase in Escherichia coli
-
expression of wild-type and mutant enzymes in Escherichia coli strains JM109 and CJ236
-
genes bedC1 and bedC2 encoding the terminal oxygenase alpha-subunit and beta-subunit, expression in Escherichia coli
-
genes bedC1C2BA, under the control of the tac promoter, subcloned into pLAFR5, successfully conjugated into seven of the Gram-negative cis-1,2-cyclohexanediol-degrading isolates and stably maintained and expressed in three of them, strain CHD1CHD3, the strains grow on cis-1,2-cyclohexanediol as sole carbon source, express an active BDO and oxidise cyclohexene, but none of the three strains is able to grow on cyclohexene as sole carbon source, overview, expression in Escherichia coli strain JM109
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
analysis
-
the enzyme is used in a whole-cell assay as biosensor for benzene concentration and vapopur, overview
analysis
-
the enzyme is used in a whole-cell assay as biosensor for benzene concentration and vapopur, overview
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Crutcher, S.E.; Geary, P.J.
Properties of the iron--sulphur proteins of the benzene dioxygenase system from Pseudomonas putida
Biochem. J.
177
393-400
1979
Pseudomonas putida
brenda
Zamanian, M.; Mason, J.R.
Benzene dioxygenase in Pseudomonas putida. Subunit composition and immuno-cross-reactivity with other aromatic dioxygenases
Biochem. J.
244
611-616
1987
Pseudomonas putida, Pseudomonas putida ML2
brenda
Geary, P.J.; Dickson, D.P.
Moessbauer spectroscopic studies of the terminal dioxygenase protein of benzene dioxygenase from Pseudomonas putida
Biochem. J.
195
199-203
1981
Pseudomonas putida
brenda
Geary, P.J.; Saboowalla, F.; Patil, D.; Cammack, R.
An investigation of the iron-sulphur proteins of benzene dioxygenase from Pseudomonas putida by electron-spin-resonance spectroscopy
Biochem. J.
217
667-673
1984
Pseudomonas putida
brenda
Axcell, B.C.; Geary, P.J.
Purification and some properties of a soluble benzene-oxidizing system from a strain of Pseudomonas
Biochem. J.
146
173-183
1975
Pseudomonas sp.
brenda
Morrice, N.; Geary, P.J.; Cammack, R.; Harris, A.; Beg, F.; Aitken, A.
Primary structure of protein B from Pseudomonas putida, member of a new class of 2Fe-2S ferredoxins
FEBS Lett.
231
336-340
1988
Pseudomonas putida, Pseudomonas putida ML2
brenda
Wackett, L.P.
Benzene dioxygenase from Pseudomonas putida, ML2 (NCIB 12190)
Methods Enzymol.
188
52-60
1990
Pseudomonas putida, Pseudomonas putida ML2
brenda
Mason, J.R.; Butler, C.S.; Cammack, R.; Shergill, J.K.
Structural studies on the catalytic component of benzene dioxygenase from Pseudomonas putida
Biochem. Soc. Trans.
25
90-95
1997
Pseudomonas putida, Pseudomonas putida ML2
brenda
Shergill, J.K.; Butler, C.S.; White, A.C.; Cammack, R.; Mason, J.R.
EPR, ENDOR and ESEEM studies on recombinant benzene dioxygenase
Biochem. Soc. Trans.
22
288S
1994
Pseudomonas putida, Pseudomonas putida ML2
brenda
Swift, R.J.; Carter, S.F.; Widdowson, D.A.; Mason, J.R.; Leak, D.J.
Expression of benzene dioxygenase from Pseudomonas putida ML2 in cis-1,2-cyclohexanediol-degrading pseudomonads
Appl. Microbiol. Biotechnol.
55
721-726
2001
Pseudomonas putida, Pseudomonas putida ML2
brenda
Bagneris, C.; Cammack, R.; Mason, J.R.
Subtle difference between benzene and toluene dioxygenases of Pseudomonas putida
Appl. Environ. Microbiol.
71
1570-1580
2005
Pseudomonas putida
brenda
Na, K.S.; Kuroda, A.; Takiguchi, N.; Ikeda, T.; Ohtake, H.; Kato, J.
Isolation and characterization of benzene-tolerant Rhodococcus opacus strains
J. Biosci. Bioeng.
99
378-382
2005
Rhodococcus opacus (Q588I8), Rhodococcus opacus (Q588I9), Rhodococcus opacus
brenda
Di Gennaro, P.; Bruzzese, N.; Anderlini, D.; Aiossa, M.; Papacchini, M.; Campanella, L.; Bestetti, G.
Development of microbial engineered whole-cell systems for environmental benzene determination
Ecotoxicol. Environ. Saf.
74
542-549
2010
Pseudomonas putida, Pseudomonas putida MST
brenda
EXTERNAL LINKS (specific for EC-Number 1.14.12.3)
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Release 2023.1 (January 2023)
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