1.14.12.3: benzene 1,2-dioxygenase
This is an abbreviated version!
For detailed information about benzene 1,2-dioxygenase, go to the full flat file.
Word Map on EC 1.14.12.3
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1.14.12.3
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putida
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toluene
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rieske
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rieske-type
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dihydrodiol
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cis-benzene
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4-methoxybenzoate
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iron-sulphur
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ring-hydroxylating
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ethylbenzene
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analysis
- 1.14.12.3
- putida
- toluene
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rieske
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rieske-type
- dihydrodiol
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cis-benzene
- 4-methoxybenzoate
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iron-sulphur
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ring-hydroxylating
- ethylbenzene
- analysis
Reaction
Synonyms
BDO, BED, benzene dioxygenase, benzene hydroxylase, More, oxygenase, benzene 1,2-di-
ECTree
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Engineering
Engineering on EC 1.14.12.3 - benzene 1,2-dioxygenase
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H119C
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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the mutant alpha-subunit of the terminal dioxygenase is unable to coordinate an EPR-detectable Rieske [2Fe-2S] cluster with the characteristic g factors
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H222M
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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
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H98C
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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
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Y118S
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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
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Y221A
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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
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additional information
I301V/T305S/I307L/L309V
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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
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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
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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
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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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