1.13.11.2: catechol 2,3-dioxygenase
This is an abbreviated version!
For detailed information about catechol 2,3-dioxygenase, go to the full flat file.
Word Map on EC 1.13.11.2
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1.13.11.2
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heme
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putida
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carboxylase
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hydroxylase
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rubisco
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ferredoxins
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ribulose-1,5-bisphosphate
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l-arginine
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non-heme
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rieske
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tetrahydrobiopterin
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dioxygenation
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ribulose
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toluene
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2-oxoglutarate
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naphthalene
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biphenyls
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rhodococcus
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fmn
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nnos
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bioremediation
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mixed-function
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nitric-oxide
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phenanthrene
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photorespiration
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photorespiratory
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1,5-bisphosphate
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biliverdin
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bh4
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l-citrulline
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sphingomonas
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ring-hydroxylating
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comamonas
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dihydroxylation
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carbazole
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xylene
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l-arg
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2-oxoglutarate-dependent
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heme-heme
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diiron
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ironii
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4-methylcatechol
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monooxygenation
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rubp
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testosteroni
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sphingobium
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ethylbenzene
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4.1.1.39
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degradation
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environmental protection
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fluoranthene
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rhodochrous
- 1.13.11.2
- heme
- putida
- carboxylase
- hydroxylase
- rubisco
- ferredoxins
- ribulose-1,5-bisphosphate
- l-arginine
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non-heme
-
rieske
- tetrahydrobiopterin
-
dioxygenation
- ribulose
- toluene
- 2-oxoglutarate
- naphthalene
- biphenyls
- rhodococcus
- fmn
- nnos
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bioremediation
-
mixed-function
-
nitric-oxide
- phenanthrene
-
photorespiration
-
photorespiratory
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1,5-bisphosphate
- biliverdin
- bh4
- l-citrulline
- sphingomonas
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ring-hydroxylating
- comamonas
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dihydroxylation
- carbazole
- xylene
- l-arg
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2-oxoglutarate-dependent
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heme-heme
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diiron
-
ironii
- 4-methylcatechol
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monooxygenation
- rubp
- testosteroni
- sphingobium
- ethylbenzene
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4.1.1.39
- degradation
- environmental protection
- fluoranthene
- rhodochrous
Reaction
Synonyms
2,3-dihydroxybenzenesulfonate 2,3-dioxygenase, 3-sulfocatechol-2,3-dioxygenase, 3SC23O, A23O, AtdB, BupB, C2,3O, C23D, C23o, C23O-2G, C23O1, C23O2, C23Os, CatE, catechol 2,3 dioxygenase, catechol 2,3-di-2,3-pyrocatechase, catechol 2,3-dioxygenase, catechol 2,3-oxygenase, catechol oxygenase, catechol-2,3-dioxygenase, CbzE, CD-2,3, EC 1.13.1.2, ECDO, extradiol dioxygenase MhpB, Extradiol-cleaving catecholic dioxygenase, meta-cleavage dioxygenase, metapyrocatechase, More, oxygenase, PheB, pyrocatechol 2,3-dioxygenase, Saci_2295, SSO1223, SsoC2,3O, ssol_2912, tbuE, TdnC, TodE, XylE
ECTree
1.13.11.2 catechol 2,3-dioxygenaseAdvanced search results
results (
results (Engineering
Engineering on EC 1.13.11.2 - catechol 2,3-dioxygenase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
E286K
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specific activity is 2.4fold higher than wild-type activity, in contrast with wild-type enzyme mutant enzyme shows no substrate inhibition
E286K
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specific activity is 2.4fold higher than wild-type activity, in contrast with wild-type enzyme mutant enzyme shows no substrate inhibition
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P229S
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thermostability decreases compared with that of wild-type enzyme
A23T/F212S
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random mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme
C103R/K289stop
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random mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme
F191I/C268R/Y272H/V280A/Y293D /
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random mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme
G127D/P140T
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random mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme
H24R/F168S/Q275R
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random mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme
L13R
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random mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme
M65T
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random mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme
R296Q
G127D/P140T
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random mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme
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L13R
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random mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme
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M65T
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random mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme
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R296Q
A23T/F212S
the mutant shows 40.65% activity with catechol compared to the wild type enzyme
F191I/C268R/Y272H/V280A/Y293D
the mutant shows 38.29% activity with catechol compared to the wild type enzyme
H24R/F168S/Q275R
the mutant shows 19.66% activity with catechol compared to the wild type enzyme
M65T
the mutant show increased activity compared to the wild type enzyme
R296Q
the mutant shows 128.47% activity with catechol compared to the wild type enzyme. The mutation also improves the activity of the enzyme against 4-chlorocatechol (582.04% activity compared to the wild type enzyme)
L226S
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increased activity with 4-ethylcatechol, reduced binding of the ferrous ion cofactor, modified the catalytic activity toward 3-methylcatechol
T253I
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increased activity with 4-ethylcatechol, reduced binding of the ferrous ion cofactor
L226S
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increased activity with 4-ethylcatechol, reduced binding of the ferrous ion cofactor, modified the catalytic activity toward 3-methylcatechol
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T253I
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increased activity with 4-ethylcatechol, reduced binding of the ferrous ion cofactor
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L226S
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increased activity with 4-ethylcatechol, reduced binding of the ferrous ion cofactor, modified the catalytic activity toward 3-methylcatechol
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T253I
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increased activity with 4-ethylcatechol, reduced binding of the ferrous ion cofactor
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environmental protection
A229C
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forming disulfide bonds, more alkalescency stable, improvement of thermostability, widened optimum temperature from 40-50°C
H294C
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forming disulfide bonds, more alkalescency stable, improvement of thermostability, widened optimum temperature from 40-50°C
A229C
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forming disulfide bonds, more alkalescency stable, improvement of thermostability, widened optimum temperature from 40-50°C
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H294C
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forming disulfide bonds, more alkalescency stable, improvement of thermostability, widened optimum temperature from 40-50°C
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H199N
strongly reduced activity, significant changes in pH profile
H246A
strongly reduced activity, significant changes in pH profile
H246N
strongly reduced activity, significant changes in pH profile
T254A
catalytic activity of the mutant enzyme hardly changes. It shows a broader substrate specificity than the wild-type enzyme. The activities of the mutant enzyme on 3-methylcatechol and 4-methylcatechol increases 3.7fold and 2.5folds, respectively, as compared to catechol
additional information
R296Q
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random mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme
R296Q
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random mutagenesis, the mutant shows significant tolerance to acidic pH with an optimum at pH 5.0, as well as a over 1.5fold increased activity, altered substrate inhibition, and 2.5fold lower KM compared to the wild-type enzyme
R296Q
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random mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme
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R296Q
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random mutagenesis, the mutant shows significant tolerance to acidic pH with an optimum at pH 5.0, as well as a over 1.5fold increased activity, altered substrate inhibition, and 2.5fold lower KM compared to the wild-type enzyme
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environmental protection
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integration and expression of catechol-2,3-dioxygenase gene in pyrene degrading bacteria genome. The engineering bacteria taking polycyclic aromatic hydrocarbons degrading dominant strain as acceptor can effectively remove polycyclic aromatic hydrocarbonss from petroleum-contaminated soil
environmental protection
Pseudomonas songnenensis wp3-1
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integration and expression of catechol-2,3-dioxygenase gene in pyrene degrading bacteria genome. The engineering bacteria taking polycyclic aromatic hydrocarbons degrading dominant strain as acceptor can effectively remove polycyclic aromatic hydrocarbonss from petroleum-contaminated soil
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additional information
construction of hybrid enzymes by exchange of parts of protein domain 2 with that of enzyme from Pseudomonas putida strain GJ31. Results indicate that the 43 C-terminal amino acids probably determine the substrate specificities
additional information
construction of hybrid enzymes by exchange of parts of protein domain 2 with that of enzyme from Pseudomonas putida strain GJ31. Results indicate that the 43 C-terminal amino acids probably determine the substrate specificities
additional information
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construction of hybrid enzymes by exchange of parts of protein domain 2 with that of enzyme from Pseudomonas putida strain GJ31. Results indicate that the 43 C-terminal amino acids probably determine the substrate specificities
additional information
construction of hybrid enzymes by exchange of parts of protein domain 2 with that of enzyme from Pseudomonas putida strain UCC2. Results indicate that the 43 C-terminal amino acids probably determine the substrate specificities
additional information
construction of hybrid enzymes by exchange of parts of protein domain 2 with that of enzyme from Pseudomonas putida strain UCC2. Results indicate that the 43 C-terminal amino acids probably determine the substrate specificities
additional information
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construction of hybrid enzymes by exchange of parts of protein domain 2 with that of enzyme from Pseudomonas putida strain UCC2. Results indicate that the 43 C-terminal amino acids probably determine the substrate specificities
additional information
used for identifying potential sites of introducing disulfide bond of C23O from Pseudomonas sp.
additional information
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construction of hybrid enzymes by exchange of parts of protein domain 2 with that of enzyme from Pseudomonas putida strain GJ31. Results indicate that the 43 C-terminal amino acids probably determine the substrate specificities
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additional information
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construction of different hybrid enzymes containing different parts of type I.2.A and I.2.B enzyme, only one of the constructed enzymes is found to be active
additional information
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construction of different hybrid enzymes containing different parts of type I.2.A and I.2.B enzyme, only one of the constructed enzymes is found to be active
additional information
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immobilization of catechol 2,3-dioxygenase from KB2 strain using calcium alginate, the iimmobilized enzyme shows relatively higher activity against 3-methylcatechol, 4-methylcatechol, 4,5-dichlorocatechol, 3,5-dichlorocatechol, hydroquinone and tetrachlorohydroquinone than soluble enzyme, immobilization protects the enzyme from the inhibition and enhanced its resistance to inactivation during catalysis
additional information
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immobilization of catechol 2,3-dioxygenase from KB2 strain using calcium alginate, the iimmobilized enzyme shows relatively higher activity against 3-methylcatechol, 4-methylcatechol, 4,5-dichlorocatechol, 3,5-dichlorocatechol, hydroquinone and tetrachlorohydroquinone than soluble enzyme, immobilization protects the enzyme from the inhibition and enhanced its resistance to inactivation during catalysis
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