1.14.12.11: toluene dioxygenase
This is an abbreviated version!
For detailed information about toluene dioxygenase, go to the full flat file.
Word Map on EC 1.14.12.11
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1.14.12.11
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putida
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naphthalene
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trichloroethylene
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ethylbenzene
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chlorobenzene
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cis-dihydrodiols
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dihydrodiols
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cis-dihydroxylation
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dot-t1e
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ring-hydroxylating
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cis-toluene
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indene
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cis-diols
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pseudoalcaligenes
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1-indanone
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toluene-grown
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3-methylcatechol
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synthesis
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analysis
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degradation
- 1.14.12.11
- putida
- naphthalene
- trichloroethylene
- ethylbenzene
- chlorobenzene
- cis-dihydrodiols
- dihydrodiols
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cis-dihydroxylation
- dot-t1e
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ring-hydroxylating
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cis-toluene
- indene
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cis-diols
- pseudoalcaligenes
- 1-indanone
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toluene-grown
- 3-methylcatechol
- synthesis
- analysis
- degradation
Reaction
Synonyms
ISPTOD, ISPTOL, More, oxygenase, toluene 2,3-di-, oxygenaseTOL, TDO, Tod, todC1C2BA, toluene 2,3-dioxygenase
ECTree
1.14.12.11 toluene dioxygenaseAdvanced search results
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results (Engineering
Engineering on EC 1.14.12.11 - toluene dioxygenase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
D219A
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mutation at alpha-subunit of oxygenase component completely abolishes toluene dioxygenase activity, mutation completely eliminates formation of cis-toluene dihydrodiol
E214A
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mutation at alpha-subunit of oxygenase component completely abolishes toluene dioxygenase activity, mutation completely eliminates formation of cis-toluene dihydrodiol
F366
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the mutant shows strongly reduced activity compared to the wild type enzyme
H222A
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mutation at alpha-subunit of oxygenase component completely abolishes toluene dioxygenase activity, mutation completely eliminates formation of cis-toluene dihydrodiol
H228A
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mutation at alpha-subunit of oxygenase component completely abolishes toluene dioxygenase activity, mutation completely eliminates formation of cis-toluene dihydrodiol
I324F
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the mutant shows reduced activity compared to the wild type enzyme
T365N
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the mutant shows slightly reduced activity compared to the wild type enzyme
Y221A
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mutation at alpha-subunit of oxygenase component, 42% of the activity of the wild-type enzyme, formation of cis-toluene dihydrodiol is reduced
Y266A
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mutation at alpha-subunit of oxygenase component, 12% of the activity of the wild-type enzyme, formation of cis-toluene dihydrodiol is reduced
additional information
additional information
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Escherichia coli expressed mutant enzyme TDO 2-B38, in which the wild-type stop codon is replaced with a codon encoding threonine, exhibits 5.6times higher activity towards 4-picoline and about 20% more activity towards toluene than the wild-type enzyme
additional information
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mutants SP6-1A, SP6-1G, and SP14-4H (created by error-prone PCR mutagenesis) show decreased 1-indenol production in comparison to the wild type enzyme
additional information
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mutations in the different TodT boxes affect TodT binding to the mutant promoters, overview
additional information
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introduction of a plasmid containing the entire tod operon todC1C2BADE to Pseudomonas putida T57 to enhance its ability to degrade 4-chloroaniline. The resulting strain shows 250-fold higher 4-chloroaniline degradation activity the parental strain. The recobinant strain degrades 2-chloroaniline, 3-chloroaniline, and 3,4-dichloroaniline as well as 3-chloroaniline, but not 3,5-dichloroaniline
additional information
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introduction of a plasmid containing the entire tod operon todC1C2BADE to Pseudomonas putida T57 to enhance its ability to degrade 4-chloroaniline. The resulting strain shows 250-fold higher 4-chloroaniline degradation activity the parental strain. The recobinant strain degrades 2-chloroaniline, 3-chloroaniline, and 3,4-dichloroaniline as well as 3-chloroaniline, but not 3,5-dichloroaniline
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