1.14.12.24: 2,4-dinitrotoluene dioxygenase
This is an abbreviated version!
For detailed information about 2,4-dinitrotoluene dioxygenase, go to the full flat file.
Word Map on EC 1.14.12.24
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1.14.12.24
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burkholderia
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4-methyl-5-nitrocatechol
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cepacia
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monooxygenase
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naphthalene
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2-nitrotoluene
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fission
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dinitrotoluenes
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sphingomonas
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nitroaromatic
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extradiol
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nahac
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vitreoscilla
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regiospecificity
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enantiomeric
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priority
- 1.14.12.24
- burkholderia
- 4-methyl-5-nitrocatechol
- cepacia
- monooxygenase
- naphthalene
- 2-nitrotoluene
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fission
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dinitrotoluenes
- sphingomonas
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nitroaromatic
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extradiol
- nahac
- vitreoscilla
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regiospecificity
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enantiomeric
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priority
Reaction
Synonyms
2,4-dinitrotoluene dioxygenase, 2,4-DNT dioxygenase, 2,4-DNTDO, DDO, DNT dioxygenase, dntA, DntAc, DNTDO
ECTree
1.14.12.24 2,4-dinitrotoluene dioxygenaseAdvanced search results
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results (Engineering
Engineering on EC 1.14.12.24 - 2,4-dinitrotoluene dioxygenase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
V350F
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the mutant of the alpha subunit is inactive with 2,4-dinitrotoluene but shows significantly increased activity towards 2-nitrophenol (47times), 3-nitrophenol (34times), and 2-methoxyphenol (174times) as well as an expanded substrate range that now includes 3-methoxyphenol, o-cresol, and m-cresol (wild type enzyme has no detectable activity for these substrates). The mutant also exhibits 10fold enhanced activity towards naphthalene forming (1R,2S)-cis-1,2-dihydro-1,2-dihydroxynaphthalene
V350M
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the mutant is inactive with 2,4-dinitrotoluene but displays increased activity towards 2-nitrophenol (20times) and 2-methoxyphenol (162times) as well as novel activity towards 2-cresol compared to the wild type enzyme. The mutant also exhibits 10fold enhanced activity towards naphthalene forming (1R,2S)-cis-1,2-dihydro-1,2-dihydroxynaphthalene
V350F
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the mutant of the alpha subunit is inactive with 2,4-dinitrotoluene but shows significantly increased activity towards 2-nitrophenol (47times), 3-nitrophenol (34times), and 2-methoxyphenol (174times) as well as an expanded substrate range that now includes 3-methoxyphenol, o-cresol, and m-cresol (wild type enzyme has no detectable activity for these substrates). The mutant also exhibits 10fold enhanced activity towards naphthalene forming (1R,2S)-cis-1,2-dihydro-1,2-dihydroxynaphthalene
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V350M
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the mutant is inactive with 2,4-dinitrotoluene but displays increased activity towards 2-nitrophenol (20times) and 2-methoxyphenol (162times) as well as novel activity towards 2-cresol compared to the wild type enzyme. The mutant also exhibits 10fold enhanced activity towards naphthalene forming (1R,2S)-cis-1,2-dihydro-1,2-dihydroxynaphthalene
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I204L
the mutant transforms both 2,6-dinitrotoluene and 2,4-dinitrotoluene 2fold faster than the wild type enzyme and exhibits activity with 2,5- and 2,3-dinitrotoluene
I204Y
V350F
mutant displays significantly increased activity towards o-nitrophenol (47 times), m-nitrophenol (34 times), and o-methoxyphenol (174 times) as well as an expanded substrate range that now includes m-methoxyphenol, o-cresol, and m-cresol
V350M
mutant displays increased activity towards o-nitrophenol (20 times) and o-methoxyphenol (162 times) as well as novel activity towards o-cresol
I204L
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the mutant transforms both 2,6-dinitrotoluene and 2,4-dinitrotoluene 2fold faster than the wild type enzyme and exhibits activity with 2,5- and 2,3-dinitrotoluene
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I204Y
V350F
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mutant displays significantly increased activity towards o-nitrophenol (47 times), m-nitrophenol (34 times), and o-methoxyphenol (174 times) as well as an expanded substrate range that now includes m-methoxyphenol, o-cresol, and m-cresol
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V350M
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mutant displays increased activity towards o-nitrophenol (20 times) and o-methoxyphenol (162 times) as well as novel activity towards o-cresol
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additional information
I204Y
mutation in alpha subunit DntAc, results in two- to fourfold faster oxidization of the aminonitrotoluenes
I204Y
the mutant transforms both 2,6-dinitrotoluene 2,5fold faster than the wild type enzyme and exhibits activity with 2,5- and 2,3-dinitrotoluene
I204Y
the mutation results in 2-4fold faster oxidization of the aminonitrotoluenes compared to the wild type enzyme
I204Y
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the mutation results in 2-4fold faster oxidization of the aminonitrotoluenes compared to the wild type enzyme
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I204Y
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mutation in alpha subunit DntAc, results in two- to fourfold faster oxidization of the aminonitrotoluenes
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I204Y
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the mutant transforms both 2,6-dinitrotoluene 2,5fold faster than the wild type enzyme and exhibits activity with 2,5- and 2,3-dinitrotoluene
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additional information
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construction of hybrid dioxygenases with the genes encoding 2-nitrotoluene 2,3-dioxygenase from Pseudomonas sp. strain JS42 and 2,4-dinitrotoluene dioxygenase from Burkholderia sp. strain DNT. The C-terminal region of the large subunit of the oxygenase component is responsible for the enzyme specificity differences observed between 2-nitrotoluene 2,3-dioxygenase and 2,4-dinitrotoluene dioxygenase
additional information
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engineering of hybrid dioxygenase enzymes coexpressing genes from naphthalene and 2,4-dinitrotoluene dioxygenases in Escherichia coli. In the active hybrids, replacement of small subunits affects the rate of product formation but has no effect on the substrate range, regiospecificity, or enantiomeric purity of oxidation products with the substrates tested. The small subunit of the oxygenase is essential for activity but does not play a major role in determining the specificity of these enzymes. Introduction of the small subunit of 2-nitrotolene synthase from Pseudomonas sp. strain JS42 leads to 30% reduction in product formation from naphthalene and dinitrotoluene
additional information
engineering of hybrid dioxygenase enzymes coexpressing genes from naphthalene and 2,4-dinitrotoluene dioxygenases in Escherichia coli. In the active hybrids, replacement of small subunits affects the rate of product formation but has no effect on the substrate range, regiospecificity, or enantiomeric purity of oxidation products with the substrates tested. The small subunit of the oxygenase is essential for activity but does not play a major role in determining the specificity of these enzymes. Introduction of the small subunit of 2-nitrotolene synthase from Pseudomonas sp. strain JS42 leads to 30% reduction in product formation from naphthalene and dinitrotoluene
additional information
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construction of hybrid dioxygenases with the genes encoding 2-nitrotoluene 2,3-dioxygenase from Pseudomonas sp. strain JS42 and 2,4-dinitrotoluene dioxygenase from Burkholderia sp. strain DNT. The C-terminal region of the large subunit of the oxygenase component is responsible for the enzyme specificity differences observed between 2-nitrotoluene 2,3-dioxygenase and 2,4-dinitrotoluene dioxygenase
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additional information
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engineering of hybrid dioxygenase enzymes coexpressing genes from naphthalene and 2,4-dinitrotoluene dioxygenases in Escherichia coli. In the active hybrids, replacement of small subunits affects the rate of product formation but has no effect on the substrate range, regiospecificity, or enantiomeric purity of oxidation products with the substrates tested. The small subunit of the oxygenase is essential for activity but does not play a major role in determining the specificity of these enzymes. Introduction of the small subunit of 2-nitrotolene synthase from Pseudomonas sp. strain JS42 leads to 30% reduction in product formation from naphthalene and dinitrotoluene
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