1.13.11.1: catechol 1,2-dioxygenase This is an abbreviated version! For detailed information about catechol 1,2-dioxygenase, go to the full flat file .
Reaction
catechol +
O2 =
cis,cis-muconate
Synonyms (chloro-)catechol 1,2-dioxygenase, 1,2 CTD, 1,2-CTD, 1,2-pyrocatechase, 3-chlorocatechol 1,2-dioxygenase, BC-C23O, C1,2-DO, C1,2O, C12, C12D, C12DO, C12O, cat12, CatA, catechase, catechol 1,2 dioxygenase, catechol 1,2-dioxygenase, catechol 1,2-dioxygenase type I, catechol 1,2-dioxygenase type II, catechol 1,2-oxygenase, catechol dioxygenase, catechol oxygenase, catechol-oxygen 1,2-oxidoreductase, catechol:oxygen 1,2-oxidoreductase, CD I, CD II, CD-I, CD-II, CD-III-1, CD-III-2, CDI1, CDI2, chlorocatechol 1,2-dioxygenase, clCA, extradiol dioxygenase MhpB, IsoB, putative catechol 2,3-dioxygenase, pyrocatechase, pyrocatechol 1,2-dioxygenase, TfdC
ECTree
Engineering
Engineering on EC 1.13.11.1 - catechol 1,2-dioxygenase
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A72P
-
site-directed mutagenesis, the mutant shows altered thermal stability values, pH and temperature dependence
A72G
-
the mutant shows decreased activity with catechol and no activity with 3-methylcatechol compared to the wild type enzyme
-
L69A
-
the mutant shows decreased activity with catechol and increased activity for 4-chlorocatechol compared to the wild type enzyme
-
A72D
-
site-directed mutagenesis, the mutant shows a low level of iron incorporation compared to the wild-type enzyme and altered thermal stability values, pH and temperature dependence
-
R215W
-
site-directed mutagenesis
A72D
enhanced substrate specificity towards chlorinated substrates
A72D
-
site-directed mutagenesis, the mutant shows a low level of iron incorporation compared to the wild-type enzyme and altered thermal stability values, pH and temperature dependence
A72G
enhanced substrate specificity towards chlorinated substrates
A72G
the mutant shows decreased activity with catechol and no activity with 3-methylcatechol compared to the wild type enzyme
A72G
-
site-directed mutagenesis, the mutant shows altered thermal stability values, pH and temperature dependence
A72N
enhanced substrate specificity towards chlorinated substrates
A72N
-
site-directed mutagenesis, the mutant shows a disturbed iron binding and altered thermal stability values, pH and temperature dependence
A72S
enhanced substrate specificity towards chlorinated substrates
A72S
-
site-directed mutagenesis, the mutant shows altered thermal stability values, pH and temperature dependence
L69A
specificity preference towards 4-chlorocatechol
L69A
the mutant shows decreased activity with catechol and increased activity for 4-chlorocatechol compared to the wild type enzyme
L69A
-
site-directed mutagenesis, the mutant shows altered thermal stability values, pH and temperature dependence
L69G/A72G
heavily destabilised
L69G/A72G
-
site-directed mutagenesis, the mutant shows altered thermal stability values, pH and temperature dependence
A72G
-
site-directed mutagenesis, the mutant shows altered thermal stability values, pH and temperature dependence
-
A72G
-
enhanced substrate specificity towards chlorinated substrates
-
A72S
-
site-directed mutagenesis, the mutant shows altered thermal stability values, pH and temperature dependence
-
A72S
-
enhanced substrate specificity towards chlorinated substrates
-
L69A
-
site-directed mutagenesis, the mutant shows altered thermal stability values, pH and temperature dependence
-
L69A
-
specificity preference towards 4-chlorocatechol
-
L69G/A72G
-
site-directed mutagenesis, the mutant shows altered thermal stability values, pH and temperature dependence
-
L69G/A72G
-
heavily destabilised
-
additional information
used as a template for catechol 1,2-dioxygenase from Acinetobacter radioresistens strain S13
additional information
catechol 1,2-dioxygenase from Acinetobacter ADP1 is used as a template
additional information
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immobilized enzyme on nanosponges
additional information
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immobilized enzyme on nanosponges
-
additional information
-
catechol 1,2-dioxygenase from Acinetobacter ADP1 is used as a template
-
additional information
-
immobilization of the enzyme from extract on sodium alginate. The catechol 1,2-dioxygenase of Mycobacterium fortuitum in the immobilized extract has greater stability to the variations of pH, temperature and reaction time, and show higher activity in presence of ions, comparing to the cell free extract, overview
additional information
-
construction of an inactive catR mutant strain 1290R, which is no longer able to grow on indole-3-acetic acid and shows completely abolished inhibitory effect of exogenous indole-3-acetic acid on the elongation of radish roots, phylogeny and phenotype, overview