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1,2,3-trihydroxybenzene + O2
2-hydroxymuconate
-
-
-
-
?
1,2,4-benzenetriol + O2
?
-
52% activity compared to catechol
-
-
?
2,3-dihydroxybenzoic acid + O2
?
-
-
-
?
3,4,5,6-tetrachlorocatechol + O2
?
-
-
-
?
3,4-dihydroxybenzoic acid + O2
?
3,4-dimethylcatechol + O2
3,4-dimethyl-cis,cis-muconate
3,5-dichlorocatechol + O2
(2E,4E)-2,4-dichlorohexa-2,4-dienedioate
3,5-dichlorocatechol + O2
?
3,5-dimethylcatechol + O2
3,5-dimethyl-cis,cis-muconate
3-butylcatechol + O2
2-butylhexa-2,4-dienedioic acid
-
weak activity
-
-
?
3-chloro-5-methylcatechol + O2
2-chloro-4-methylhexa-2,4-dienedioate
3-chlorocatechol + O2
2-chloro-cis,cis-muconate
3-chlorocatechol + O2
?
-
-
-
-
?
3-chloropyrocatechol + O2
?
3-ethylcatechol + O2
2-ethyl-cis,cis-muconic acid
3-isopropylcatechol + O2
2-isopropyl-cis,cis-muconate
3-methylcatechol + O2
(2Z,4Z)-2-methylhexa-2,4-dienedioate
3-methylcatechol + O2
2-methyl-cis,cis-muconate
3-methylpyrocatechol + O2
2,3,5-trimethyl-cis-cis-muconate
3-methylthiocatechol + O2
2-methylthio-cis,cis-muconate
-
very poor substrate
-
-
?
4,5-dichlorocatechol + O2
?
4,5-difluorocatechol + O2
3,4-difluoro-cis-cis-muconate
-
-
-
-
?
4-bromocatechol + O2
3-bromo-cis-cis-muconate
4-chloro-5-fluorocatechol + O2
?
-
-
-
-
?
4-chlorocatechol + O2
(2E,4Z)-3-chlorohexa-2,4-dienedioate
4-chlorocatechol + O2
4-chloro-cis,cis-muconate
4-chlorocatechol + O2
4-chlorocis,cis-muconate
-
-
-
-
?
4-ethylcatechol + O2
4-ethyl-cis-cis-muconate
-
42% of activity with catechol
-
-
?
4-fluorocatechol + O2
3-fluoro-cis,cis-muconate
4-fluorocatechol + O2
4-fluoro-cis,cis-muconate
-
65% of activity with catechol
-
-
?
4-hydroxybenzoic acid + O2
?
4-iso-propylcatechol + O2
4-isopropyl-cis,cis-muconate
-
23% of activity with catechol
-
-
?
4-methylcatechol + O2
(2Z,4Z)-3-methylhexa-2,4-dienedioate
4-methylcatechol + O2
3-methyl-cis,cis-hexadienedioate
-
-
-
?
4-methylcatechol + O2
3-methyl-cis,cis-muconate
4-methylcatechol + O2
3-methylhexa-2,4-dienedioate
4-methylcatechol + O2
4-methyl-cis,cis-muconate
4-methylpyrocatechol + O2
2,4,5-trimethyl-cis-cis-muconate
4-n-propylcatechol + O2
4-n-propyl-cis,cis-muconate
-
17% of activity with catechol
-
-
?
4-nitrocatechol + O2
?
-
80% activity compared to catechol
-
-
?
4-tert-butylcatechol + O2
?
benzene-1,2,4-triol + O2
?
benzoate + O2
?
-
-
-
-
?
benzoic acid + O2
?
-
-
-
?
catechol + O2
cis,cis-muconate
catechol + O2
cis,cis-muconic acid
catechol + O2
cis-cis muconate
assay at pH 8.0, 30°C
-
-
?
hydroxyquinol + O2
?
i.e. 1,2,4-trihydroxy benzene
-
-
?
hydroxyquinol + O2
maleylacetic acid
protocatechuate + O2
?
i.e. 3,4-dihydroxybenzoate
-
-
?
pyrocatechol + O2
2,5-dimethyl-cis-cis-muconate
pyrogallol + O2
alpha-hydroxymuconic acid
tetrachlorocatechol + O2
cis,cis-tetrachloromuconic acid
-
-
-
-
?
additional information
?
-
3,4-dihydroxybenzoic acid + O2
?
-
-
-
?
3,4-dihydroxybenzoic acid + O2
?
-
-
-
?
3,4-dimethylcatechol + O2
3,4-dimethyl-cis,cis-muconate
-
21% of activity with catechol
-
-
?
3,4-dimethylcatechol + O2
3,4-dimethyl-cis,cis-muconate
-
21% of activity with catechol
-
-
?
3,5-dichlorocatechol + O2
(2E,4E)-2,4-dichlorohexa-2,4-dienedioate
-
reaction catalyzed by catechol 1,2-dioxygenase type II
-
-
?
3,5-dichlorocatechol + O2
(2E,4E)-2,4-dichlorohexa-2,4-dienedioate
-
reaction catalyzed by catechol 1,2-dioxygenase type II
-
-
?
3,5-dichlorocatechol + O2
?
-
-
-
?
3,5-dichlorocatechol + O2
?
99.35% compared to the activity with catechol
-
-
?
3,5-dichlorocatechol + O2
?
99.35% compared to the activity with catechol
-
-
?
3,5-dimethylcatechol + O2
3,5-dimethyl-cis,cis-muconate
-
36% of activity with catechol
-
-
?
3,5-dimethylcatechol + O2
3,5-dimethyl-cis,cis-muconate
-
36% of activity with catechol
-
-
?
3-chloro-5-methylcatechol + O2
2-chloro-4-methylhexa-2,4-dienedioate
-
reaction catalyzed by catechol 1,2-dioxygenase type II
-
-
?
3-chloro-5-methylcatechol + O2
2-chloro-4-methylhexa-2,4-dienedioate
-
reaction catalyzed by catechol 1,2-dioxygenase type II
-
-
?
3-chlorocatechol + O2
2-chloro-cis,cis-muconate
CatA1: 4.4% of the activity with catechol
-
-
?
3-chlorocatechol + O2
2-chloro-cis,cis-muconate
CatA1: 4.4% of the activity with catechol
-
-
?
3-chlorocatechol + O2
2-chloro-cis,cis-muconate
-
-
-
-
?
3-chlorocatechol + O2
2-chloro-cis,cis-muconate
-
-
-
-
?
3-chlorocatechol + O2
2-chloro-cis,cis-muconate
-
pyrocatechase II, in 3-chlorobenzoate-grown cells
-
-
?
3-chlorocatechol + O2
2-chloro-cis,cis-muconate
-
pyrocatechase II, in 3-chlorobenzoate-grown cells
-
-
?
3-chlorocatechol + O2
2-chloro-cis,cis-muconate
1.7% activity compared to catechol
-
-
?
3-chlorocatechol + O2
2-chloro-cis,cis-muconate
1.7% activity compared to catechol
-
-
?
3-chloropyrocatechol + O2
?
-
weak activity
-
-
?
3-chloropyrocatechol + O2
?
-
-
-
-
?
3-chloropyrocatechol + O2
?
-
-
-
-
?
3-chloropyrocatechol + O2
?
-
-
-
-
?
3-chloropyrocatechol + O2
?
-
-
-
-
?
3-ethylcatechol + O2
2-ethyl-cis,cis-muconic acid
-
-
-
-
?
3-ethylcatechol + O2
2-ethyl-cis,cis-muconic acid
-
poor substrate
-
?
3-isopropylcatechol + O2
2-isopropyl-cis,cis-muconate
-
-
-
-
?
3-isopropylcatechol + O2
2-isopropyl-cis,cis-muconate
-
-
-
-
?
3-methylcatechol + O2
(2Z,4Z)-2-methylhexa-2,4-dienedioate
-
-
-
-
?
3-methylcatechol + O2
(2Z,4Z)-2-methylhexa-2,4-dienedioate
-
-
-
-
?
3-methylcatechol + O2
(2Z,4Z)-2-methylhexa-2,4-dienedioate
-
-
-
-
?
3-methylcatechol + O2
(2Z,4Z)-2-methylhexa-2,4-dienedioate
the enzyme preferentially recognizes 4-substituted over 3-substituted catechols
-
-
?
3-methylcatechol + O2
(2Z,4Z)-2-methylhexa-2,4-dienedioate
the enzyme preferentially recognizes 4-substituted over 3-substituted catechols
-
-
?
3-methylcatechol + O2
(2Z,4Z)-2-methylhexa-2,4-dienedioate
-
-
-
-
?
3-methylcatechol + O2
(2Z,4Z)-2-methylhexa-2,4-dienedioate
-
-
-
-
?
3-methylcatechol + O2
(2Z,4Z)-2-methylhexa-2,4-dienedioate
-
-
-
?
3-methylcatechol + O2
(2Z,4Z)-2-methylhexa-2,4-dienedioate
-
-
-
-
?
3-methylcatechol + O2
(2Z,4Z)-2-methylhexa-2,4-dienedioate
-
poor substrate
-
?
3-methylcatechol + O2
(2Z,4Z)-2-methylhexa-2,4-dienedioate
-
poor substrate
-
?
3-methylcatechol + O2
(2Z,4Z)-2-methylhexa-2,4-dienedioate
-
poor substrate
-
-
?
3-methylcatechol + O2
(2Z,4Z)-2-methylhexa-2,4-dienedioate
-
poor substrate
-
-
?
3-methylcatechol + O2
(2Z,4Z)-2-methylhexa-2,4-dienedioate
-
-
-
-
?
3-methylcatechol + O2
(2Z,4Z)-2-methylhexa-2,4-dienedioate
-
poor substrate
-
-
?
3-methylcatechol + O2
(2Z,4Z)-2-methylhexa-2,4-dienedioate
-
poor substrate
-
-
?
3-methylcatechol + O2
(2Z,4Z)-2-methylhexa-2,4-dienedioate
-
-
-
?
3-methylcatechol + O2
(2Z,4Z)-2-methylhexa-2,4-dienedioate
-
-
-
-
?
3-methylcatechol + O2
(2Z,4Z)-2-methylhexa-2,4-dienedioate
-
-
-
-
?
3-methylcatechol + O2
(2Z,4Z)-2-methylhexa-2,4-dienedioate
-
-
-
-
?
3-methylcatechol + O2
(2Z,4Z)-2-methylhexa-2,4-dienedioate
-
-
-
-
?
3-methylcatechol + O2
(2Z,4Z)-2-methylhexa-2,4-dienedioate
104% activity compared to catechol
-
-
?
3-methylcatechol + O2
(2Z,4Z)-2-methylhexa-2,4-dienedioate
104% activity compared to catechol
-
-
?
3-methylcatechol + O2
(2Z,4Z)-2-methylhexa-2,4-dienedioate
-
-
-
-
?
3-methylcatechol + O2
(2Z,4Z)-2-methylhexa-2,4-dienedioate
-
-
-
-
?
3-methylcatechol + O2
(2Z,4Z)-2-methylhexa-2,4-dienedioate
117.4% compared to the activity with catechol
-
-
?
3-methylcatechol + O2
(2Z,4Z)-2-methylhexa-2,4-dienedioate
9.9% compared to the activity with catechol
-
-
?
3-methylcatechol + O2
(2Z,4Z)-2-methylhexa-2,4-dienedioate
9.9% compared to the activity with catechol
-
-
?
3-methylcatechol + O2
(2Z,4Z)-2-methylhexa-2,4-dienedioate
117.4% compared to the activity with catechol
-
-
?
3-methylcatechol + O2
2-methyl-cis,cis-muconate
-
-
-
-
?
3-methylcatechol + O2
2-methyl-cis,cis-muconate
-
10% of the activity with catechol
-
-
?
3-methylcatechol + O2
2-methyl-cis,cis-muconate
-
10% of the activity with catechol
-
-
?
3-methylcatechol + O2
2-methyl-cis,cis-muconate
-
64% of activity with catechol
-
-
?
3-methylcatechol + O2
2-methyl-cis,cis-muconate
-
64% of activity with catechol
-
-
?
3-methylcatechol + O2
2-methyl-cis,cis-muconate
-
enzyme from aniline-grown cells: 74% of the activity with catechol, enzyme from L-malate-grown cells: 71% of the activity with catechol
-
-
?
3-methylcatechol + O2
2-methyl-cis,cis-muconate
11.6% of the activity with catechol
-
-
?
3-methylcatechol + O2
2-methyl-cis,cis-muconate
11.6% of the activity with catechol
-
-
?
3-methylcatechol + O2
?
-
-
-
-
?
3-methylcatechol + O2
?
assay at pH 8.0, 30°C
-
-
?
3-methylcatechol + O2
?
-
-
-
-
?
3-methylcatechol + O2
?
assay at pH 8.0, 30°C
-
-
?
3-methylcatechol + O2
?
-
2% activity compared to catechol
-
-
?
3-methylcatechol + O2
?
-
assay at 60°C, pH 7.0
-
-
?
3-methylcatechol + O2
?
-
assay at 60°C, pH 7.0
-
-
?
3-methylcatechol + O2
?
-
-
-
-
?
3-methylcatechol + O2
?
-
-
-
-
?
3-methylpyrocatechol + O2
2,3,5-trimethyl-cis-cis-muconate
-
-
-
-
?
3-methylpyrocatechol + O2
2,3,5-trimethyl-cis-cis-muconate
-
-
-
-
?
3-methylpyrocatechol + O2
2,3,5-trimethyl-cis-cis-muconate
-
-
-
-
?
3-methylpyrocatechol + O2
2,3,5-trimethyl-cis-cis-muconate
-
-
-
-
?
3-methylpyrocatechol + O2
2,3,5-trimethyl-cis-cis-muconate
-
-
-
-
?
4,5-dichlorocatechol + O2
?
assay at pH 8.0, 30°C
-
-
?
4,5-dichlorocatechol + O2
?
the enzyme possesses only a quite rare capability to process 4,5-dichlorocatechol
-
-
?
4,5-dichlorocatechol + O2
?
the enzyme possesses only a quite rare capability to process 4,5-dichlorocatechol
-
-
?
4,5-dichlorocatechol + O2
?
assay at pH 8.0, 30°C
-
-
?
4,5-dichlorocatechol + O2
?
-
-
-
?
4-bromocatechol + O2
3-bromo-cis-cis-muconate
-
-
-
-
?
4-bromocatechol + O2
3-bromo-cis-cis-muconate
-
-
-
-
?
4-chlorocatechol + O2
(2E,4Z)-3-chlorohexa-2,4-dienedioate
the enzyme preferentially recognizes 4-substituted over 3-substituted catechols
-
-
?
4-chlorocatechol + O2
(2E,4Z)-3-chlorohexa-2,4-dienedioate
the enzyme preferentially recognizes 4-substituted over 3-substituted catechols
-
-
?
4-chlorocatechol + O2
(2E,4Z)-3-chlorohexa-2,4-dienedioate
CatA1: 18.1% of the activity with catechol
-
-
?
4-chlorocatechol + O2
(2E,4Z)-3-chlorohexa-2,4-dienedioate
CatA2: 2.5% of the activity with catechol
-
-
?
4-chlorocatechol + O2
(2E,4Z)-3-chlorohexa-2,4-dienedioate
CatA1: 18.1% of the activity with catechol
-
-
?
4-chlorocatechol + O2
(2E,4Z)-3-chlorohexa-2,4-dienedioate
CatA2: 2.5% of the activity with catechol
-
-
?
4-chlorocatechol + O2
(2E,4Z)-3-chlorohexa-2,4-dienedioate
-
-
-
-
?
4-chlorocatechol + O2
(2E,4Z)-3-chlorohexa-2,4-dienedioate
-
-
-
-
?
4-chlorocatechol + O2
(2E,4Z)-3-chlorohexa-2,4-dienedioate
-
-
-
?
4-chlorocatechol + O2
(2E,4Z)-3-chlorohexa-2,4-dienedioate
-
11% of the activity with catechol
-
-
?
4-chlorocatechol + O2
(2E,4Z)-3-chlorohexa-2,4-dienedioate
-
11% of the activity with catechol
-
-
?
4-chlorocatechol + O2
(2E,4Z)-3-chlorohexa-2,4-dienedioate
-
-
-
-
?
4-chlorocatechol + O2
(2E,4Z)-3-chlorohexa-2,4-dienedioate
-
poor substrate
-
-
?
4-chlorocatechol + O2
(2E,4Z)-3-chlorohexa-2,4-dienedioate
-
-
-
-
?
4-chlorocatechol + O2
(2E,4Z)-3-chlorohexa-2,4-dienedioate
-
-
-
?
4-chlorocatechol + O2
(2E,4Z)-3-chlorohexa-2,4-dienedioate
-
pyrocatechase II, in 3-chlorobenzoate-grown cells
-
-
?
4-chlorocatechol + O2
(2E,4Z)-3-chlorohexa-2,4-dienedioate
-
pyrocatechase II, in 3-chlorobenzoate-grown cells
-
-
?
4-chlorocatechol + O2
(2E,4Z)-3-chlorohexa-2,4-dienedioate
2.7% activity compared to catechol
-
-
?
4-chlorocatechol + O2
(2E,4Z)-3-chlorohexa-2,4-dienedioate
2.7% activity compared to catechol
-
-
?
4-chlorocatechol + O2
(2E,4Z)-3-chlorohexa-2,4-dienedioate
3.3% compared to the activity with catechol
-
-
?
4-chlorocatechol + O2
(2E,4Z)-3-chlorohexa-2,4-dienedioate
70% compared to the activity with catechol
-
-
?
4-chlorocatechol + O2
(2E,4Z)-3-chlorohexa-2,4-dienedioate
3.3% compared to the activity with catechol
-
-
?
4-chlorocatechol + O2
(2E,4Z)-3-chlorohexa-2,4-dienedioate
70% compared to the activity with catechol
-
-
?
4-chlorocatechol + O2
4-chloro-cis,cis-muconate
28.05% of the activity compared to catechol
-
-
?
4-chlorocatechol + O2
4-chloro-cis,cis-muconate
28.05% of the activity compared to catechol
-
-
?
4-chlorocatechol + O2
4-chloro-cis,cis-muconate
-
-
-
-
?
4-chlorocatechol + O2
?
-
-
-
-
?
4-chlorocatechol + O2
?
assay at pH 8.0, 30°C
-
-
?
4-chlorocatechol + O2
?
-
-
-
-
?
4-chlorocatechol + O2
?
assay at pH 8.0, 30°C
-
-
?
4-chlorocatechol + O2
?
-
-
-
-
?
4-chlorocatechol + O2
?
-
-
-
-
?
4-fluorocatechol + O2
3-fluoro-cis,cis-muconate
-
-
-
-
?
4-fluorocatechol + O2
3-fluoro-cis,cis-muconate
-
-
-
-
?
4-fluorocatechol + O2
3-fluoro-cis,cis-muconate
-
-
-
-
?
4-hydroxybenzoic acid + O2
?
-
-
-
?
4-hydroxybenzoic acid + O2
?
-
-
-
?
4-methylcatechol + O2
(2Z,4Z)-3-methylhexa-2,4-dienedioate
-
-
-
-
?
4-methylcatechol + O2
(2Z,4Z)-3-methylhexa-2,4-dienedioate
-
-
-
-
?
4-methylcatechol + O2
(2Z,4Z)-3-methylhexa-2,4-dienedioate
-
-
-
-
?
4-methylcatechol + O2
(2Z,4Z)-3-methylhexa-2,4-dienedioate
-
-
-
-
?
4-methylcatechol + O2
(2Z,4Z)-3-methylhexa-2,4-dienedioate
-
-
-
-
?
4-methylcatechol + O2
(2Z,4Z)-3-methylhexa-2,4-dienedioate
-
-
-
-
?
4-methylcatechol + O2
(2Z,4Z)-3-methylhexa-2,4-dienedioate
-
-
-
?
4-methylcatechol + O2
(2Z,4Z)-3-methylhexa-2,4-dienedioate
-
-
-
-
?
4-methylcatechol + O2
(2Z,4Z)-3-methylhexa-2,4-dienedioate
-
-
-
-
?
4-methylcatechol + O2
(2Z,4Z)-3-methylhexa-2,4-dienedioate
-
-
-
-
?
4-methylcatechol + O2
(2Z,4Z)-3-methylhexa-2,4-dienedioate
-
better substrate than catechol
-
?
4-methylcatechol + O2
(2Z,4Z)-3-methylhexa-2,4-dienedioate
-
better substrate than catechol
-
?
4-methylcatechol + O2
(2Z,4Z)-3-methylhexa-2,4-dienedioate
-
poor substrate
-
-
?
4-methylcatechol + O2
(2Z,4Z)-3-methylhexa-2,4-dienedioate
-
poor substrate
-
-
?
4-methylcatechol + O2
(2Z,4Z)-3-methylhexa-2,4-dienedioate
-
free enzyme shows 1.5times the activity of immobilized enzyme
-
-
?
4-methylcatechol + O2
(2Z,4Z)-3-methylhexa-2,4-dienedioate
-
-
-
-
?
4-methylcatechol + O2
(2Z,4Z)-3-methylhexa-2,4-dienedioate
-
-
-
-
?
4-methylcatechol + O2
(2Z,4Z)-3-methylhexa-2,4-dienedioate
-
-
-
-
?
4-methylcatechol + O2
(2Z,4Z)-3-methylhexa-2,4-dienedioate
-
-
-
?
4-methylcatechol + O2
(2Z,4Z)-3-methylhexa-2,4-dienedioate
preferred substrate
-
-
?
4-methylcatechol + O2
(2Z,4Z)-3-methylhexa-2,4-dienedioate
-
-
-
-
?
4-methylcatechol + O2
(2Z,4Z)-3-methylhexa-2,4-dienedioate
-
-
-
-
?
4-methylcatechol + O2
(2Z,4Z)-3-methylhexa-2,4-dienedioate
-
-
-
-
?
4-methylcatechol + O2
(2Z,4Z)-3-methylhexa-2,4-dienedioate
-
-
-
-
?
4-methylcatechol + O2
(2Z,4Z)-3-methylhexa-2,4-dienedioate
-
-
-
-
?
4-methylcatechol + O2
(2Z,4Z)-3-methylhexa-2,4-dienedioate
-
-
-
-
?
4-methylcatechol + O2
(2Z,4Z)-3-methylhexa-2,4-dienedioate
-
-
-
-
?
4-methylcatechol + O2
(2Z,4Z)-3-methylhexa-2,4-dienedioate
-
-
-
-
?
4-methylcatechol + O2
(2Z,4Z)-3-methylhexa-2,4-dienedioate
136.4% compared to the activity with catechol
-
-
?
4-methylcatechol + O2
(2Z,4Z)-3-methylhexa-2,4-dienedioate
18.2% compared to the activity with catechol
-
-
?
4-methylcatechol + O2
(2Z,4Z)-3-methylhexa-2,4-dienedioate
18.2% compared to the activity with catechol
-
-
?
4-methylcatechol + O2
(2Z,4Z)-3-methylhexa-2,4-dienedioate
136.4% compared to the activity with catechol
-
-
?
4-methylcatechol + O2
3-methyl-cis,cis-muconate
CatA1: 39.5% of the activity with catechol
-
-
?
4-methylcatechol + O2
3-methyl-cis,cis-muconate
CatA2: 13.1% of the activity with catechol
-
-
?
4-methylcatechol + O2
3-methyl-cis,cis-muconate
CatA1: 39.5% of the activity with catechol
-
-
?
4-methylcatechol + O2
3-methyl-cis,cis-muconate
CatA2: 13.1% of the activity with catechol
-
-
?
4-methylcatechol + O2
3-methyl-cis,cis-muconate
-
-
-
-
?
4-methylcatechol + O2
3-methyl-cis,cis-muconate
-
-
-
-
?
4-methylcatechol + O2
3-methyl-cis,cis-muconate
-
-
-
-
?
4-methylcatechol + O2
3-methyl-cis,cis-muconate
-
43% of the activity with catechol
-
-
?
4-methylcatechol + O2
3-methyl-cis,cis-muconate
-
43% of the activity with catechol
-
-
?
4-methylcatechol + O2
3-methyl-cis,cis-muconate
-
76% of activity with catechol
-
-
?
4-methylcatechol + O2
3-methyl-cis,cis-muconate
-
76% of activity with catechol
-
-
?
4-methylcatechol + O2
3-methyl-cis,cis-muconate
-
enzyme from aniline-grown cells: 86% of the activity with catechol, enzyme from L-malate-grown cells: 87% of the activity with catechol
-
-
?
4-methylcatechol + O2
3-methylhexa-2,4-dienedioate
-
reaction catalyzed by catechol 1,2-dioxygenase type I and type II
-
-
?
4-methylcatechol + O2
3-methylhexa-2,4-dienedioate
-
reaction catalyzed by catechol 1,2-dioxygenase type I and type II
-
-
?
4-methylcatechol + O2
4-methyl-cis,cis-muconate
the enzyme preferentially recognizes 4-substituted over 3-substituted catechols
-
-
?
4-methylcatechol + O2
4-methyl-cis,cis-muconate
the enzyme preferentially recognizes 4-substituted over 3-substituted catechols
-
-
?
4-methylcatechol + O2
4-methyl-cis,cis-muconate
90.12% of the activity compared to catechol
-
-
?
4-methylcatechol + O2
4-methyl-cis,cis-muconate
90.12% of the activity compared to catechol
-
-
?
4-methylcatechol + O2
4-methyl-cis,cis-muconate
71.5% activity compared to catechol
-
-
?
4-methylcatechol + O2
4-methyl-cis,cis-muconate
23.0% of the activity with catechol
-
-
?
4-methylcatechol + O2
4-methyl-cis,cis-muconate
23.0% of the activity with catechol
-
-
?
4-methylcatechol + O2
?
-
-
-
-
?
4-methylcatechol + O2
?
assay at pH 8.0, 30°C
-
-
?
4-methylcatechol + O2
?
-
-
-
-
?
4-methylcatechol + O2
?
assay at pH 8.0, 30°C
-
-
?
4-methylcatechol + O2
?
-
61% activity compared to catechol
-
-
?
4-methylcatechol + O2
?
-
assay at 60°C, pH 7.0
-
-
?
4-methylcatechol + O2
?
-
assay at 60°C, pH 7.0
-
-
?
4-methylcatechol + O2
?
-
-
-
-
?
4-methylcatechol + O2
?
-
-
-
-
?
4-methylpyrocatechol + O2
2,4,5-trimethyl-cis-cis-muconate
-
-
-
-
?
4-methylpyrocatechol + O2
2,4,5-trimethyl-cis-cis-muconate
-
-
-
-
?
4-methylpyrocatechol + O2
2,4,5-trimethyl-cis-cis-muconate
-
-
-
-
?
4-methylpyrocatechol + O2
2,4,5-trimethyl-cis-cis-muconate
-
-
-
-
?
4-methylpyrocatechol + O2
2,4,5-trimethyl-cis-cis-muconate
-
-
-
-
?
4-tert-butylcatechol + O2
?
assay at pH 8.0, 30°C
-
-
?
4-tert-butylcatechol + O2
?
assay at pH 8.0, 30°C
-
-
?
benzene-1,2,4-triol + O2
?
-
16% of the activity with catechol
-
-
?
benzene-1,2,4-triol + O2
?
-
16% of the activity with catechol
-
-
?
catechol + ?
?
-
-
-
-
?
catechol + O2
cis,cis-muconate
-
-
-
-
?
catechol + O2
cis,cis-muconate
-
-
-
-
?
catechol + O2
cis,cis-muconate
-
-
-
-
?
catechol + O2
cis,cis-muconate
best substrate
-
-
?
catechol + O2
cis,cis-muconate
best substrate
-
-
?
catechol + O2
cis,cis-muconate
-
-
-
-
?
catechol + O2
cis,cis-muconate
-
-
-
-
?
catechol + O2
cis,cis-muconate
-
best substrate
-
-
?
catechol + O2
cis,cis-muconate
catechol binds to the Fe(III) as a dianion. Protonation of an endogenous tyrosinate ligand after it dissociates from the ferric center upon substrate binding
-
-
?
catechol + O2
cis,cis-muconate
-
-
-
-
?
catechol + O2
cis,cis-muconate
-
best substrate
-
-
?
catechol + O2
cis,cis-muconate
-
100% activity
-
-
?
catechol + O2
cis,cis-muconate
-
-
-
ir
catechol + O2
cis,cis-muconate
-
-
-
-
?
catechol + O2
cis,cis-muconate
-
-
-
-
?
catechol + O2
cis,cis-muconate
-
-
-
-
?
catechol + O2
cis,cis-muconate
-
-
-
-
?
catechol + O2
cis,cis-muconate
-
-
-
?
catechol + O2
cis,cis-muconate
-
-
-
?
catechol + O2
cis,cis-muconate
-
-
-
?
catechol + O2
cis,cis-muconate
-
-
-
?
catechol + O2
cis,cis-muconate
-
-
-
?
catechol + O2
cis,cis-muconate
both catechol dioxygenases, CatA1 and CatA2 are produced in benzoate-grown cells, CatA1 is undetectable when strain TH2 is grown on 2-chlorobenzoate or cis,cis-muconate. Production of CatA1 during growth on 2-chlorobenzoate or cis,cis-muconate is observed when cat2 genes are disrupted. The inducer of Cat1 is benzoate. cis,cis-Muconate or its metabolite acts as an inducer for CatA2. Genes are not indispensable for growth of strain TH2 on 2-chlorobenzoate, they are advantageous
-
-
?
catechol + O2
cis,cis-muconate
-
-
-
?
catechol + O2
cis,cis-muconate
both catechol dioxygenases, CatA1 and CatA2 are produced in benzoate-grown cells, CatA1 is undetectable when strain TH2 is grown on 2-chlorobenzoate or cis,cis-muconate. Production of CatA1 during growth on 2-chlorobenzoate or cis,cis-muconate is observed when cat2 genes are disrupted. The inducer of Cat1 is benzoate. cis,cis-Muconate or its metabolite acts as an inducer for CatA2. Genes are not indispensable for growth of strain TH2 on 2-chlorobenzoate, they are advantageous
-
-
?
catechol + O2
cis,cis-muconate
-
-
-
-
?
catechol + O2
cis,cis-muconate
-
-
-
-
?
catechol + O2
cis,cis-muconate
-
-
-
?
catechol + O2
cis,cis-muconate
-
-
-
-
?
catechol + O2
cis,cis-muconate
-
-
-
-
?
catechol + O2
cis,cis-muconate
-
-
-
-
?
catechol + O2
cis,cis-muconate
-
-
-
-
?
catechol + O2
cis,cis-muconate
-
-
-
-
?
catechol + O2
cis,cis-muconate
-
-
-
-
?
catechol + O2
cis,cis-muconate
-
-
-
?
catechol + O2
cis,cis-muconate
-
-
-
?
catechol + O2
cis,cis-muconate
-
-
-
?
catechol + O2
cis,cis-muconate
-
reaction catalyzed by catechol 1,2-dioxygenase type I
-
-
?
catechol + O2
cis,cis-muconate
-
reaction catalyzed by catechol 1,2-dioxygenase type I
-
-
?
catechol + O2
cis,cis-muconate
-
-
-
?
catechol + O2
cis,cis-muconate
-
-
-
?
catechol + O2
cis,cis-muconate
-
intradiol dioxygenase reaction
-
-
?
catechol + O2
cis,cis-muconate
-
-
-
-
?
catechol + O2
cis,cis-muconate
-
-
-
-
?
catechol + O2
cis,cis-muconate
-
catechol 1,2-dioxygenase activity is induced eightfold in cultures grown on salicylate compared to cultures grown on glucose
-
-
?
catechol + O2
cis,cis-muconate
-
catechol 1,2-dioxygenase activity is induced eightfold in cultures grown on salicylate compared to cultures grown on glucose
-
-
?
catechol + O2
cis,cis-muconate
-
intradiol, assay at 60°C, pH 7.0
-
-
?
catechol + O2
cis,cis-muconate
-
intradiol, assay at 60°C, pH 7.0
-
-
?
catechol + O2
cis,cis-muconate
-
-
-
-
?
catechol + O2
cis,cis-muconate
-
-
-
-
?
catechol + O2
cis,cis-muconate
-
the enzyme is involved in the catabolic pathway of L-tryptophan degradation, overview
-
-
?
catechol + O2
cis,cis-muconate
-
-
-
-
?
catechol + O2
cis,cis-muconate
-
-
i.e. cis,cis-hexadienedioate or (2Z,4Z)-hexa-2,4-dienedioate
-
?
catechol + O2
cis,cis-muconate
-
-
-
-
?
catechol + O2
cis,cis-muconate
-
-
-
?
catechol + O2
cis,cis-muconate
-
-
-
?
catechol + O2
cis,cis-muconate
-
-
-
-
?
catechol + O2
cis,cis-muconate
-
-
-
-
?
catechol + O2
cis,cis-muconate
-
-
-
-
?
catechol + O2
cis,cis-muconate
-
-
-
?
catechol + O2
cis,cis-muconate
-
catechol is an intermediate of the indole-3-acetic acid catabolic pathway, overview
-
-
?
catechol + O2
cis,cis-muconate
-
isozyme1 is able to function as lyophilized enzyme in a non-aqueous environment catalyzing the oxidation of catechol in n-hexane, overview
-
-
?
catechol + O2
cis,cis-muconate
-
benzoate degadation pathway
-
-
?
catechol + O2
cis,cis-muconate
-
-
-
-
?
catechol + O2
cis,cis-muconate
-
-
-
?
catechol + O2
cis,cis-muconate
-
-
-
?
catechol + O2
cis,cis-muconate
-
-
-
-
?
catechol + O2
cis,cis-muconate
-
-
-
-
?
catechol + O2
cis,cis-muconate
-
-
-
-
?
catechol + O2
cis,cis-muconate
-
-
-
-
?
catechol + O2
cis,cis-muconate
-
-
-
-
?
catechol + O2
cis,cis-muconate
-
-
-
-
?
catechol + O2
cis,cis-muconate
-
-
-
-
?
catechol + O2
cis,cis-muconate
-
-
-
-
?
catechol + O2
cis,cis-muconate
-
-
-
-
?
catechol + O2
cis,cis-muconate
100% activity
-
-
?
catechol + O2
cis,cis-muconate
-
-
-
-
?
catechol + O2
cis,cis-muconate
100% activity
-
-
?
catechol + O2
cis,cis-muconate
-
the enzyme is involved in the biodegradation of benzothiazole
-
-
?
catechol + O2
cis,cis-muconate
-
the enzyme is involved in the biodegradation of benzothiazole
-
-
?
catechol + O2
cis,cis-muconate
-
-
-
-
?
catechol + O2
cis,cis-muconate
-
-
-
-
?
catechol + O2
cis,cis-muconate
-
-
-
-
?
catechol + O2
cis,cis-muconate
-
-
-
-
?
catechol + O2
cis,cis-muconate
-
-
-
-
?
catechol + O2
cis,cis-muconate
-
-
-
-
?
catechol + O2
cis,cis-muconate
-
-
-
?
catechol + O2
cis,cis-muconate
-
-
-
?
catechol + O2
cis,cis-muconate
-
-
-
-
?
catechol + O2
cis,cis-muconate
-
-
-
?
catechol + O2
cis,cis-muconate
best substrate
-
-
?
catechol + O2
cis,cis-muconate
-
-
-
-
?
catechol + O2
cis,cis-muconate
-
-
-
?
catechol + O2
cis,cis-muconate
best substrate
-
-
?
catechol + O2
cis,cis-muconate
Stutzerimonas stutzeri
-
-
-
?
catechol + O2
cis,cis-muconate
Stutzerimonas stutzeri GOM2
-
-
-
?
catechol + O2
cis,cis-muconic acid
-
-
-
-
?
catechol + O2
cis,cis-muconic acid
-
-
-
?
catechol + O2
cis,cis-muconic acid
-
-
-
?
hydroxyquinol + O2
maleylacetic acid
-
-
-
-
?
hydroxyquinol + O2
maleylacetic acid
-
-
-
-
?
hydroxyquinol + O2
maleylacetic acid
-
better substrate than catechol
-
?
hydroxyquinol + O2
maleylacetic acid
-
better substrate than catechol
-
?
phenol + O2
?
best substrate
-
-
?
phenol + O2
?
best substrate
-
-
?
pyrocatechol + O2
2,5-dimethyl-cis-cis-muconate
-
-
-
-
?
pyrocatechol + O2
2,5-dimethyl-cis-cis-muconate
-
-
-
-
?
pyrocatechol + O2
2,5-dimethyl-cis-cis-muconate
-
-
-
-
?
pyrocatechol + O2
2,5-dimethyl-cis-cis-muconate
-
-
-
-
?
pyrocatechol + O2
2,5-dimethyl-cis-cis-muconate
-
-
-
-
?
pyrogallol + O2
?
-
-
-
-
?
pyrogallol + O2
?
-
-
-
-
?
pyrogallol + O2
alpha-hydroxymuconic acid
-
-
-
?
pyrogallol + O2
alpha-hydroxymuconic acid
-
poor substrate
-
?
pyrogallol + O2
alpha-hydroxymuconic acid
-
poor substrate
-
?
pyrogallol + O2
alpha-hydroxymuconic acid
-
180% of the activity with catechol
-
-
?
pyrogallol + O2
alpha-hydroxymuconic acid
-
180% of the activity with catechol
-
-
?
pyrogallol + O2
alpha-hydroxymuconic acid
-
-
-
-
?
pyrogallol + O2
alpha-hydroxymuconic acid
-
-
-
-
?
pyrogallol + O2
alpha-hydroxymuconic acid
i.e.benzene-1,2,3-triol
-
-
?
pyrogallol + O2
alpha-hydroxymuconic acid
i.e.benzene-1,2,3-triol
-
-
?
pyrogallol + O2
alpha-hydroxymuconic acid
-
-
-
-
?
additional information
?
-
-
no substrates: 4-nitrocatechol, alpha-chloro-3,4-dihydroxyacetophenone, 3,4-dihydroxyphenylacetic acid, 3,4-dihydroxycinnamic acid, protocatechuic acid, protoacatechualdehyde, pyrogallol
-
-
?
additional information
?
-
-
no substrates: 4-nitrocatechol, alpha-chloro-3,4-dihydroxyacetophenone, 3,4-dihydroxyphenylacetic acid, 3,4-dihydroxycinnamic acid, protocatechuic acid, protoacatechualdehyde, pyrogallol
-
-
?
additional information
?
-
-
extradiol cleavage of 3-methylcatechol, no substrate: 3-chlorocatechol, protocatechuic acid
-
-
?
additional information
?
-
-
both intradiol and extradiol cleavage of 3-methylcatechol
-
-
?
additional information
?
-
-
poor or no activity with 3-methylcatechol, 4-methylcatechol, and 4-nitrocatechol
-
-
?
additional information
?
-
-
poor or no activity with 3-methylcatechol, 4-methylcatechol, and 4-nitrocatechol
-
-
?
additional information
?
-
-
intradiol cleavage of 3-and 4-methylcatechol, no extradiol cleavage of 3-methylcatechol or 3-chlorocatechol, slight intradiol cleavage activity for 3- and 4-substituted halocatechols, CD-II shows no activity for 4-chlorocatechol, no substrate: protocatechuic acid
-
-
?
additional information
?
-
-
inducible on benzamide, not on L-malate
-
-
?
additional information
?
-
-
intradiol cleavage of 3-and 4-methylcatechol, no extradiol cleavage of 3-methylcatechol or 3-chlorocatechol, slight intradiol cleavage activity for 3- and 4-substituted halocatechols, CD-II shows no activity for 4-chlorocatechol, no substrate: protocatechuic acid
-
-
?
additional information
?
-
-
inducible on benzamide, not on L-malate
-
-
?
additional information
?
-
-
no substrates: 3-methylcatechol, isopropylcatechol
-
-
?
additional information
?
-
CatA2: no activity with 3-chlorocatechol
-
-
?
additional information
?
-
CatA2: no activity with 3-chlorocatechol
-
-
?
additional information
?
-
CatA2: no activity with 3-chlorocatechol
-
-
?
additional information
?
-
CatA2: no activity with 3-chlorocatechol
-
-
?
additional information
?
-
-
ratios of intradiol to extradiol activity of CD I and CD II 1000:120 and 100:3 respectively
-
-
?
additional information
?
-
-
inducible on aniline, not on L-malate
-
-
?
additional information
?
-
-
ratios of intradiol to extradiol activity of CD I and CD II 1000:120 and 100:3 respectively
-
-
?
additional information
?
-
-
inducible on aniline, not on L-malate
-
-
?
additional information
?
-
-
the enzyme is involved in degradation of 4-chlorobenzenesulfonic acid, 4CBSA, the major polar by-product of the chemical synthesis of 1,1,1-trichloro-2,2-bis-(4-chlorophenyl) ethane, DDT, overview, 4-chlorobenzenesulfonic acid catabolic pathway, overview
-
-
?
additional information
?
-
-
no activity with 4-sulfocatechol
-
-
?
additional information
?
-
-
no substrates: adrenolutine, p-aminocatechol, protocatechuic acid, 2,3-dihydroxybenzoic acid, 2,4-dihydroxybenzoic acid, trans-5,6-dihydroxycyclohexadiene, pyrogallol, dopa, homogentisic acid, gentisic acid
-
-
?
additional information
?
-
-
no substrates: adrenolutine, p-aminocatechol, protocatechuic acid, 2,3-dihydroxybenzoic acid, 2,4-dihydroxybenzoic acid, trans-5,6-dihydroxycyclohexadiene, pyrogallol, dopa, homogentisic acid, gentisic acid
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
both intradiol and extradiol cleavage activities toward 3-substituted catechols
-
-
?
additional information
?
-
-
enzyme intermediates
-
-
?
additional information
?
-
-
no substrates: 4-nitrocatechol, protocatechuic acid, ratios of intradiol and extradiol cleavage activities for 3-methylcatechol and 3-methoxycatechol 22 : 4.3
-
-
?
additional information
?
-
-
catechol 1,2-dioxygenase is induced by benzoate
-
-
?
additional information
?
-
no activity with vanillic acid
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
both intradiol and extradiol cleavage activities toward 3-substituted catechols
-
-
?
additional information
?
-
-
catechol 1,2-dioxygenase is induced by benzoate
-
-
?
additional information
?
-
no activity with vanillic acid
-
-
?
additional information
?
-
no activity with 3-chlorocatechol
-
-
?
additional information
?
-
no activity with 3-chlorocatechol
-
-
?
additional information
?
-
-
extradiol cleavage in addition to intradiol fission at a ratio 1:14 with pyrocatechase I, not with pyrocatechase II
-
-
?
additional information
?
-
-
extradiol cleavage in addition to intradiol fission at a ratio 1:14 with pyrocatechase I, not with pyrocatechase II
-
-
?
additional information
?
-
-
no intradiol cleavage of 3- and 4-chlorocatechol or 4-fluorocatechol, no substrates: protocatechuic acid
-
-
?
additional information
?
-
-
no intradiol cleavage of 3- and 4-chlorocatechol or 4-fluorocatechol, no substrates: protocatechuic acid
-
-
?
additional information
?
-
-
no substrates: 3,4-dihydroxybenzoate, 3-methoxy-4-hydroxybenzoate, 2,4-dihydroxybenzoate, 3,5-dihydroxybenzoate, 3,4,5-trihydroxybenzoate
-
-
?
additional information
?
-
-
no substrates: 3,4-dihydroxybenzoate, 3-methoxy-4-hydroxybenzoate, 2,4-dihydroxybenzoate, 3,5-dihydroxybenzoate, 3,4,5-trihydroxybenzoate
-
-
?
additional information
?
-
-
poor substrates: 4-chloropyrocatechol, 3-methoxypyrocatechol
-
-
?
additional information
?
-
-
intradiol cleavage of 3- and 4-methylcatechol, but not extradiol cleavage of 3-methylcatechol
-
-
?
additional information
?
-
-
inducible on aniline, not on L-malate
-
-
?
additional information
?
-
-
intradiol cleavage of 3- and 4-methylcatechol, but not extradiol cleavage of 3-methylcatechol
-
-
?
additional information
?
-
-
inducible on aniline, not on L-malate
-
-
?
additional information
?
-
the enzyme is involved in the aerobic biodegradation of chloroaromatic compounds
-
-
?
additional information
?
-
-
the enzyme is involved in the aerobic biodegradation of chloroaromatic compounds
-
-
?
additional information
?
-
the enzyme is involved in the aerobic biodegradation of chloroaromatic compounds
-
-
?
additional information
?
-
-
the enzyme is involved in the aerobic biodegradation of chloroaromatic compounds
-
-
?
additional information
?
-
-
poor substrates: 4-chloropyrocatechol, 3-methoxypyrocatechol
-
-
?
additional information
?
-
-
poor substrates: 4-chloropyrocatechol, 3-methoxypyrocatechol
-
-
?
additional information
?
-
-
poor substrates: 4-chloropyrocatechol, 3-methoxypyrocatechol
-
-
?
additional information
?
-
-
poor substrates: 4-chloropyrocatechol, 3-methoxypyrocatechol
-
-
?
additional information
?
-
-
synthesized constitutively. When the bacterium is incubated on a medium with D-glucose, L-malate, isoleucine, leucine, etc., it synthesizes more catechol 1,2-dioxygenase than that in cells grown on aniline
-
-
?
additional information
?
-
-
strain KB2 degrades 13 mM 3,4-dihydroxybenzoate, 10 mM benzoic acid and 12 mM phenol within 24 h of incubation
-
-
?
additional information
?
-
substrate specificity, overview. No activity with 3-chlorocatechol, 4-chlorocatechol, 3,5-dichlorocatechol, 4,5-dichlorocatechol, and hydroquinone
-
-
?
additional information
?
-
-
substrate specificity, overview. No activity with 3-chlorocatechol, 4-chlorocatechol, 3,5-dichlorocatechol, 4,5-dichlorocatechol, and hydroquinone
-
-
?
additional information
?
-
-
strain KB2 degrades 13 mM 3,4-dihydroxybenzoate, 10 mM benzoic acid and 12 mM phenol within 24 h of incubation
-
-
?
additional information
?
-
substrate specificity, overview. No activity with 3-chlorocatechol, 4-chlorocatechol, 3,5-dichlorocatechol, 4,5-dichlorocatechol, and hydroquinone
-
-
?
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Hayaishi, O.
Direct oxygenation by O2. Oxygenases
The Enzymes, 2nd Ed (Boyer, P. D. , Lardy, H. , Myrbck, K. , eds. )
8
353-371
1963
Pseudomonas fluorescens
-
brenda
Hayaishi, O.; Katagiri, M.; Rothberg, S.
Studies on oxygenases: pyrocatechase
J. Biol. Chem.
229
905-920
1957
Pseudomonas fluorescens
brenda
Ninnekar, H.Z.; Vaidyanathan, C.S.
Catechol 1,2-dioxygenase from Aspergillus niger
J. Indian Inst. Sci.
63C
131-136
1981
Aspergillus niger
-
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Patel, R.N.; Hou, C.T.; Felix, A.; Lillard, M.O.
Catechol 1,2-dioxygenase from Acinetobacter calcoaceticus: purification and properties
J. Bacteriol.
127
536-544
1976
Acinetobacter calcoaceticus, Acinetobacter calcoaceticus ADP-96
brenda
Dorn, E.; Knackmuss, H.J.
Chemical structure and biodegradability of halogenated aromatic compounds. Two catechol 1,2-dioxygenases from a 3-chlorobenzoate-grown pseudomonad
Biochem. J.
174
73-84
1978
Pseudomonas sp., Pseudomonas sp. B 13
brenda
Nakai, C.; Kagamiyama, H.; Saeki, Y.; Nozaki, M.
Nonidentical subunits of pyrocatechase from Pseudomonas arvilla C-1
Arch. Biochem. Biophys.
195
12-22
1979
Pseudomonas putida, Pseudomonas putida C-1
brenda
Kojima, Y.; Fujisawa, H.; Nakazawa, T.; Kanetsuna, F.; Taniuchi H.; Nozaki, M.; Hayaishi, O.
Studies on pyrocatechase. I. Purification and spectral properties
J. Biol. Chem.
242
3270-3278
1967
Pseudomonas putida, Pseudomonas putida C-1
brenda
Itoh, M.
Characteristics of a new catechol 1,2-oxygenase from Trichosporon cutaneum WY 2-2
Agric. Biol. Chem.
45
2787-2796
1981
Cutaneotrichosporon cutaneum, Cutaneotrichosporon cutaneum WY 2-2
-
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Walsh, T.A.; Ballou, D.P.; Mayer, R.; Que, L.
Rapid reaction studies on the oxygenation reactions of catechol dioxygenase
J. Biol. Chem.
258
14422-14427
1983
Pseudomonas putida
brenda
Aoki, K.; Konohana, T.; Shinke, R.; Nishira, H.
Purification and characterization of catechol 1,2-dioxygenase from aniline-assimilating Rhodococcus erythropolis AN-13
Agric. Biol. Chem.
48
2087-2095
1984
Rhodococcus erythropolis, Rhodococcus erythropolis AN-13
-
brenda
Aoki, K.; Konohana, T.; Shinke, R.; Nishira, H.
Two catechol 1,2-dioxygenases from aniline-assimilating bacterium, Frateuria species ANA-18
Agric. Biol. Chem.
48
2097-2104
1984
Frateuria sp., Frateuria sp. ANA-18
-
brenda
Chen, Y.P.; Glenn, A.R.; Dilworth, M.J.
Aromatic metabolism in Rhizobium trifolii: catechol 1,2-dioxygenase
Arch. Microbiol.
141
225-228
1985
Rhizobium leguminosarum, Rhizobium leguminosarum TA1
-
brenda
Pascal, R.A.; Huang, D.S.
Reactions of 3-ethylcatechol and 3-(methylthio)catechol with catechol dioxygenases
Arch. Biochem. Biophys.
248
130-137
1986
Pseudomonas putida
brenda
Krug, M.; Straube, G.
Degradation of phenolic compounds by the yeast Candida tropicalis HP 15. II. Some properties of the first two enzymes of the degradation pathway
J. Basic Microbiol.
26
271-281
1986
Candida tropicalis, Candida tropicalis HP 15
brenda
Gomi, K.; Horiguchi, S.
Purification and characterization of pyrocatechase from the catechol-assimilating yeast
Agric. Biol. Chem.
52
585-587
1988
Candida maltosa
-
brenda
Nakai, C.; Nakazawa, T.; Nozaki, M.
Purification and properties of catechol 1,2-dioxygenase (pyrocatechase) from Pseudomonas putida mt-2 in comparison with that from Pseudomonas arvilla C-1
Arch. Biochem. Biophys.
267
701-713
1988
Pseudomonas putida
brenda
Nakai, C.; Horiike, K.; Kuramitsu, S.; Kagamiyama, H.; Nozaki, M.
Three isoenzymes of catechol 1,2-dioxygenase (pyrocatechase) alphaalpha, alphabeta, and betabeta from Pseudomonas arvilla C-1
J. Biol. Chem.
265
660-665
1980
Pseudomonas putida, Pseudomonas putida C-1
brenda
Chen, Y.P.; Lovell, C.R.
Purification and properties of catechol 1,2-dioxygenase from Rhizobium leguminosarum biovar viceae USDA 2370
Appl. Environ. Microbiol.
56
1971-1973
1990
Rhizobium leguminosarum
brenda
Smith, M.R.; Ratledge, C.; Crook, S.
Properties of cyanogen bromide-activated, agarose-immobilized catechol 1,2-dioxygenase from freeze-dried extracts of Nocardia sp. NCIB 10503
Enzyme Microb. Technol.
12
945-949
1990
Nocardia sp.
-
brenda
Ngai, K.L.; Neidle, E.L.; Ornston, L.N.
Catechol and chlorocatechol 1,2-dioxygenases
Methods Enzymol.
188
122-126
1990
Acinetobacter calcoaceticus
brenda
Neidle, E.L.; Ornston, L.N.
Cloning and expression of Acinetobacter calcoaceticus catechol 1,2-dioxygenase structural gene catA in Escherichia coli
J. Bacteriol.
168
815-820
1986
Acinetobacter calcoaceticus
brenda
Nakagawa, H.; Inoue, H.; Takeda, Y.
Characteristics of catechol oxygenase from Brevibacterium fuscum
J. Biochem.
54
65-74
1963
Brevibacterium fuscum
brenda
Sauret-Ignazi, G.; Gagnon, J.; Beguin, C.; Barrelle, M.; Markowicz, J.; Pelmont, J.; Toussaint, A.
Characterization of a chromosomally encoded catechol 1,2-dioxygenase (E.C. 1.13.11.1) from Alcaligenes eutrophus CH34
Arch. Microbiol.
166
42-50
1996
Cupriavidus necator
brenda
Briganti, F.; Pessione, E.; Giunta, C.; Scozzafava, A.
Purification, biochemical properties and substrate specificity of a catechol 1,2-dioxygenase from a phenol degrading Acinetobacter radioresistens
FEBS Lett.
416
61-64
1997
Acinetobacter radioresistens
brenda
Ridder, L.; Briganti, F.; Boersma, M.G.; Boeren, S.; Vis, E.H.; Scozzafava, A.; Veeger, C.; Rietjens, I.M.C.M.
Quantitative structure/activity relationship for the rate of conversion of C4-substituted catechols by catechol-1,2-dioxygenase from Pseudomonas putida (arvilla) C1
Eur. J. Biochem.
257
92-100
1998
Pseudomonas putida, Pseudomonas putida C-1
brenda
Strachan, P.D.; Freer, A.A.; Fewson, C.A.
Purification and characterization of catechol 1,2-dioxygenase from Rhodococcus rhodochrous NCIMB 13259 and cloning and sequencing of its catA gene
Biochem. J.
333
741-747
1998
Rhodococcus rhodochrous, Rhodococcus rhodochrous NCIMB 13259
-
brenda
Murakami, S.; Wang, C.L.; Naito, A.; Shinke, R.; Aoki, K.
Purification and characterization of four catechol 1,2-dioxygenase isoenzymes from the benzamide-assimilating bacterium Arthrobacter species BA-5-17
Microbiol. Res.
153
163-171
1998
Arthrobacter sp., Arthrobacter sp. BA-5-17
brenda
Solyanikova, I.P.; Golovlev, E.L.; Lisnyak, O.V.; Golovleva, L.A.
Isolation and characterization of catechol 1,2-dioxygenases from Rhodococcus rhodnii strain 135 and Rhodococcus rhodochrous strain 89: comparison with analogous enzymes of the ordinary and modified ortho-cleavage pathways
Biochemistry (Moscow)
64
824-831
1999
Rhodococcus rhodnii, Rhodococcus erythropolis, Rhodococcus rhodochrous, Rhodococcus rhodnii 135, Rhodococcus rhodochrous 89
brenda
Wang, C.L.; Takenaka, S.; Murakami, S.; Aoki, K.
Production of catechol from benzoate by the wild strain Ralstonia species Ba-0323 and characterization of its catechol 1,2-dioxygenase
Biosci. Biotechnol. Biochem.
65
1957-1964
2001
Ralstonia sp., Ralstonia sp. Ba-0323
brenda
Briganti, F.; Pessione, E.; Giunta, C.; Mazzoli, R.; Scozzafava, A.
Purification and catalytic properties of two catechol 1,2-dioxygenase isozymes from benzoate-grown cells of Acinetobacter radioresistens
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19
709-716
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Acinetobacter radioresistens
brenda
Earhart, C.A.; Hall, M.D.; Michaud-Soret, I.; Que, L.Jr.; Ohlendorf, D.H.
Crystallization of catechol-1,2 dioxygenase from Pseudomonas arvilla C-1
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236
377-378
1994
Pseudomonas putida
brenda
Pieper, D.H.; Stadler-Fritzsche, K.; Engesser, K.H.; Knackmuss, H.J.
Metabolism of 2-chloro-4-methylphenoxyacetate by Alcaligenes eutrophus JMP 134
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160
169-178
1993
Cupriavidus necator, Cupriavidus necator JMP 134-1
brenda
Haroune, N.; Combourieu, B.; Besse, P.; Sancelme, M.; Reemtsma, T.; Kloepfer, A.; Diab, A.; Knapp, J.S.; Baumberg, S.; Delort, A.M.
Benzothiazole degradation by Rhodococcus pyridinovorans strain PA: evidence of a catechol 1,2-dioxygenase activity
Appl. Environ. Microbiol.
68
6114-6120
2002
Rhodococcus pyridinivorans, Rhodococcus pyridinivorans PA
brenda
Shen, X.H.; Liu, Z.P.; Liu, S.J.
Functional identification of the gene locus (ncg1231) and characterization of catechol 1,2-dioxygenase in Corynebacterium glutamicum
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26
575-580
2004
Corynebacterium glutamicum
brenda
Yoshikawa, N.; Ohta, K.; Mizuno, S.; Ohkishi, H.
Production of cis,cis-muconic acid from benzoic acid
BIOTECHNOL. BIOPROCESS ENG.
16
131-147
1993
Arthrobacter sp.
brenda
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Differential expression of two catechol 1,2-dioxygenases in Burkholderia sp. strain TH2
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184
5714-5722
2002
Burkholderia sp. (Q8GAY6), Burkholderia sp. (Q8GAZ6), Burkholderia sp. TH2 (Q8GAY6), Burkholderia sp. TH2 (Q8GAZ6)
brenda
Ferraroni, M.; Solyanikova, I.P.; Kolomytseva, M.P.; Scozzafava, A.; Golovleva, L.; Briganti, F.
Crystal Structure of 4-chlorocatechol 1,2-dioxygenase from the chlorophenol-utilizing Gram-positive Rhodococcus opacus 1CP
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279
27646-27655
2004
Rhodococcus opacus (O67987), Rhodococcus opacus, Rhodococcus opacus 1CP (O67987), Rhodococcus opacus 1CP
brenda
Matsumura, E.; Ooi, S.; Murakami, S.; Takenaka, S.; Aoki, K.
Constitutive synthesis, purification, and characterization of catechol 1,2-dioxygenase from the aniline-assimilating bacterium Rhodococcus sp. AN-22
J. Biosci. Bioeng.
98
71-76
2004
Arthrobacter sp., Frateuria sp., Rhodococcus erythropolis, Rhodococcus sp., Frateuria sp. ANA-18, Arthrobacter sp. BA-5-17, Rhodococcus erythropolis AN-13
brenda
Ahuatzi-Chacon, D.; Ordorica-Morales, G.; Ruiz-Ordaz, N.; Cristiani-Urbina, E.; Juarez-Ramirez, C.; Galindez-Mayer, J.
Kinetic study of phenol hydroxylase and catechol 1,2-dioxygenase dioxygenase biosynthesis by Candida tropicalis cells grown on different phenolic substrates.
World J. Microbiol. Biotechnol.
20
695-702
2004
Candida tropicalis
brenda
Dodge, A.G.; Wackett, L.P.
Metabolism of bismuth subsalicylate and intracellular accumulation of bismuth by Fusarium sp. strain BI
Appl. Environ. Microbiol.
71
876-882
2005
Fusarium sp., Fusarium sp. BI
brenda
Tsai, S.C.; Li, Y.K.
Purification and characterization of a catechol 1,2-dioxygenase from a phenol degrading Candida albicans TL3
Arch. Microbiol.
187
199-206
2007
Candida albicans, Candida albicans TL3
brenda
Earhart, C.A.; Vetting, M.W.; Gosu, R.; Michaud-Soret, I.; Que, L.; Ohlendorf, D.H.
Structure of catechol 1,2-dioxygenase from Pseudomonas arvilla
Biochem. Biophys. Res. Commun.
338
198-205
2005
Pseudomonas putida
brenda
Karigar, C.; Mahesh, A.; Nagenahalli, M.; Yun, D.J.
Phenol degradation by immobilized cells of Arthrobacter citreus
Biodegradation
17
47-55
2006
Arthrobacter citreus
brenda
Saxena, P.; Thakur, I.S.
Purification and characterization of catechol 1,2-dioxygenase of Pseudomonas fluorescens for degradation of 4-chlorobenzoic acid
Indian J. Biotechnol.
4
134-138
2005
Pseudomonas fluorescens, Pseudomonas fluorescens IST8
-
brenda
Horsman, G.P.; Jirasek, A.; Vaillancourt, F.H.; Barbosa, C.J.; Jarzecki, A.A.; Xu, C.; Mekmouche, Y.; Spiro, T.G.; Lipscomb, J.D.; Blades, M.W.; Turner, R.F.; Eltis, L.D.
Spectroscopic studies of the anaerobic enzyme-substrate complex of catechol 1,2-dioxygenase
J. Am. Chem. Soc.
127
16882-16891
2005
Acinetobacter sp. (P07773)
brenda
Cha, C.
Catechol 1,2-dioxygenase from Rhodococcus rhodochrous N75 capable of metabolizing alkyl-substituted catechols
J. Microbiol. Biotechnol.
16
778-785
2006
Rhodococcus rhodochrous, Rhodococcus rhodochrous N75
-
brenda
Ferraroni, M.; Kolomytseva, M.P.; Solyanikova, I.P.; Scozzafava, A.; Golovleva, L.A.; Briganti, F.
Crystal structure of 3-chlorocatechol 1,2-dioxygenase key enzyme of a new modified ortho-pathway from the Gram-positive Rhodococcus opacus 1CP grown on 2-chlorophenol
J. Mol. Biol.
360
788-799
2006
Rhodococcus opacus (Q8G9L3), Rhodococcus opacus, Rhodococcus opacus 1CP (Q8G9L3), Rhodococcus opacus 1CP
brenda
Liao, Y.; Zhou, X.; Yu, J.; Cao, Y.; Li, X.; Kuai, B.
The key role of chlorocatechol 1,2-dioxygenase in phytoremoval and degradation of catechol by transgenic Arabidopsis
Plant Physiol.
142
620-628
2006
Plesiomonas sp.
brenda
Wang, C.; You, S.; Wang, S.
Purification and characterization of a novel catechol 1,2-dioxygenase from Pseudomonas aeruginosa with benzoic acid as a carbon source
Proc. Biochem.
41
1594-1601
2006
Pseudomonas aeruginosa, Pseudomonas aeruginosa TKU002
-
brenda
Kim, Y.H.; Cho, K.; Yun, S.H.; Kim, J.Y.; Kwon, K.H.; Yoo, J.S.; Kim, S.I.
Analysis of aromatic catabolic pathways in Pseudomonas putida KT 2440 using a combined proteomic approach: 2-DE/MS and cleavable isotope-coded affinity tag analysis
Proteomics
6
1301-1318
2006
Pseudomonas putida, Pseudomonas putida KT 2440
brenda
Leveau, J.H.; Lindow, S.E.
Utilization of the plant hormone indole-3-acetic acid for growth by Pseudomonas putida strain 1290
Appl. Environ. Microbiol.
71
2365-2371
2005
Pseudomonas putida
brenda
Sanakis, Y.; Mamma, D.; Christakopoulos, P.; Stamatis, H.
Catechol 1,2-dioxygenase from Pseudomonas putida in organic media - an electron paramagnetic resonance study
Int. J. Biol. Macromol.
33
101-106
2003
Pseudomonas putida
brenda
Bouknight, R.R.; Sadoff, H.L.
Tryptophan catabolism in Bacillus megaterium
J. Bacteriol.
121
70-76
1975
Priestia megaterium
brenda
Camara, B.; Bielecki, P.; Kaminski, F.; dos Santos, V.M.; Plumeier, I.; Nikodem, P.; Pieper, D.H.
A gene cluster involved in degradation of substituted salicylates via ortho cleavage in Pseudomonas sp. strain MT1 encodes enzymes specifically adapted for transformation of 4-methylcatechol and 3-methylmuconate
J. Bacteriol.
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2007
Pseudomonas reinekei (A0F0B5), Pseudomonas reinekei (Q0VH42)
brenda
Tancsics, A.; Szoboszlay, S.; Kriszt, B.; Kukolya, J.; Baka, E.; Marialigeti, K.; Revesz, S.
Applicability of the functional gene catechol 1,2-dioxygenase as a biomarker in the detection of BTEX-degrading Rhodococcus species
J. Appl. Microbiol.
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2008
Rhodococcus sp.
brenda
Cao, B.; Geng, A.; Loh, K.C.
Induction of ortho- and meta-cleavage pathways in Pseudomonas in biodegradation of high benzoate concentration: MS identification of catabolic enzymes
Appl. Microbiol. Biotechnol.
81
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2008
Pseudomonas putida
brenda
Blasco, R.; Ramos, J.L.; Wittich, R.M.
Pseudomonas aeruginosa strain RW41 mineralizes 4-chlorobenzenesulfonate, the major polar by-product from DDT manufacturing
Environ. Microbiol.
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2008
Pseudomonas aeruginosa, Pseudomonas aeruginosa RW41
brenda
Weelink, S.A.; Tan, N.C.; ten Broeke, H.; van den Kieboom, C.; van Doesburg, W.; Langenhoff, A.A.; Gerritse, J.; Junca, H.; Stams, A.J.
Isolation and characterization of Alicycliphilus denitrificans strain BC, which grows on benzene with chlorate as the electron acceptor
Appl. Environ. Microbiol.
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2008
Alicycliphilus sp. BC (A6N2H5)
brenda
Giedraityte, G.; Kalediene, L.
Catechol 1,2-dioxygenase from alpha-naphthol degrading thermophilic Geobacillus sp. strain: Purification and properties
Cent. Eur. J. Biol.
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2009
Geobacillus sp., Geobacillus sp. G27
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brenda
Caglio, R.; Valetti, F.; Caposio, P.; Gribaudo, G.; Pessione, E.; Giunta, C.
Fine-tuning of catalytic properties of catechol 1,2-dioxygenase by active site tailoring
ChemBioChem
10
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2009
Acinetobacter baylyi ADP1 (P07773), Acinetobacter radioresistens (Q9F103), Acinetobacter radioresistens S13 (Q9F103)
brenda
Di Nardo, G.; Roggero, C.; Campolongo, S.; Valetti, F.; Trotta, F.; Gilardi, G.
Catalytic properties of catechol 1,2-dioxygenase from Acinetobacter radioresistens S13 immobilized on nanosponges
Dalton Trans.
33
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2009
Acinetobacter radioresistens, Acinetobacter radioresistens S13
brenda
Brivio, M.; Schlosrich, J.; Ahmad, M.; Tolond, C.; Bugg, T.D.
Investigation of acid-base catalysis in the extradiol and intradiol catechol dioxygenase reactions using a broad specificity mutant enzyme and model chemistry
Org. Biomol. Chem.
7
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2009
Escherichia coli
brenda
Gou, M.; Qu, Y.; Zhou, J.; Li, A.; Salah Uddin, M.
Characterization of catechol 1,2-dioxygenase from cell extracts of Sphingomonas xenophaga QYY
Sci. China, Ser. B, Chem. Life Sci. Earth Sci.
52
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2009
Sphingobium xenophagum, Sphingobium xenophagum QYY
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brenda
Shen, F.T.; Lin, J.L.; Huang, C.C.; Ho, Y.N.; Arun, A.B.; Young, L.S.; Young, C.C.
Molecular detection and phylogenetic analysis of the catechol 1,2-dioxygenase gene from Gordonia spp
Syst. Appl. Microbiol.
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2009
Gordonia alkanivorans (B5AS37), Gordonia alkanivorans (B5AS38), Gordonia amicalis (B5AS40), Gordonia amicalis (B5AS41), Gordonia bronchialis (B5AS42), Gordonia desulfuricans (B5AS43), Gordonia hydrophobica (B5AS44), Gordonia namibiensis (B5AS45), Gordonia rhizosphera (B5AS46), Gordonia rhizosphera, Gordonia rubripertincta (B5AS47), Gordonia rubripertincta (B5AS48), Gordonia rubripertincta (B5AS49), Gordonia sputi (B5AS50), Gordonia sputi, Gordonia terrae (B5AS51), Gordonia westfalica (B5AS52), Rhodococcus erythropolis (B5AS53), Rhodococcus erythropolis (B5AS54), Williamsia muralis (B5AS55), Rhodococcus erythropolis CC-BC11 (B5AS53), Gordonia rubripertincta JCM 3199 (B5AS49), Gordonia alkanivorans CC-JG39 (B5AS37), Gordonia amicalis CC-MJ-2a (B5AS40), Gordonia amicalis CC-MJ-2a
brenda
Sun, J.; Huang, X.; Chen, Q.; Liang, B.; Qiu, J.; Ali, S.; Li, S.
Isolation and characterization of three Sphingobium sp. strains capable of degrading isoproturon and cloning of the catechol 1,2-dioxygenase gene from these strains
World J. Microbiol. Biotechnol.
25
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2009
Sphingobium sp. (B3VZQ2), Sphingobium sp. (B3VZQ3), Sphingobium sp. YBL3 (B3VZQ4), Sphingobium sp. YBL1 (B3VZQ2)
brenda
Guzik, U.; Gren, I.; Wojcieszynska, D.; Labuzek, S.
Isolation and characterization of a novel strain of stenotrophomonas maltophilia possessing various dioxygenases for monocyclic hydrocarbon degradation
Braz. J. Microbiol.
40
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2009
Stenotrophomonas maltophilia (A7LBQ5), Stenotrophomonas maltophilia, Stenotrophomonas maltophilia KB2 (A7LBQ5), Stenotrophomonas maltophilia KB2
brenda
Micalella, C.; Martignon, S.; Bruno, S.; Pioselli, B.; Caglio, R.; Valetti, F.; Pessione, E.; Giunta, C.; Rizzi, M.
X-ray crystallography, mass spectrometry and single crystal microspectrophotometry: A multidisciplinary characterization of catechol 1,2 dioxygenase
Biochim. Biophys. Acta
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817-823
2011
Acinetobacter radioresistens (Q9F103), Acinetobacter radioresistens LMG S13 (Q9F103), Acinetobacter radioresistens LMG S13
brenda
Matera, I.; Ferraroni, M.; Kolomytseva, M.; Golovleva, L.; Scozzafava, A.; Briganti, F.
Catechol 1,2-dioxygenase from the Gram-positive Rhodococcus opacus 1CP: Quantitative structure/activity relationship and the crystal structures of native enzyme and catechols adducts
J. Struct. Biol.
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2010
Rhodococcus opacus (P95607), Rhodococcus opacus 1CP (P95607), Rhodococcus opacus 1CP
brenda
Guzik, U.; Hupert-Kocurek, K.; Sitnik, M.; Wojcieszynska, D.
High activity catechol 1,2-dioxygenase from Stenotrophomonas maltophilia strain KB2 as a useful tool in cis,cis-muconic acid production
Antonie van Leeuwenhoek
103
1297-1307
2013
Stenotrophomonas maltophilia (A7LBQ5), Stenotrophomonas maltophilia, Stenotrophomonas maltophilia KB2 (A7LBQ5)
brenda
Caglio, R.; Pessione, E.; Valetti, F.; Giunta, C.; Ghibaudi, E.
An EPR, thermostability and pH-dependence study of wild-type and mutant forms of catechol 1,2-dioxygenase from Acinetobacter radioresistens S13
Biometals
26
75-84
2013
Acinetobacter radioresistens, Acinetobacter radioresistens S13
brenda
Li, F.; Zhu, L.
Effect of surfactant-induced cell surface modifications on electron transport system and catechol 1,2-dioxygenase activities and phenanthrene biodegradation by Citrobacter sp. SA01
Biores. Technol.
123
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2012
Citrobacter sp., Citrobacter sp. SA01
brenda
Silva, A.S.; Jacques, R.J.; Andreazza, R.; Bento, F.M.; Roesch, L.F.; Camargo, F.A.
Properties of catechol 1,2-dioxygenase in the cell free extract and immobilized extract of Mycobacterium fortuitum
Braz. J. Microbiol.
44
291-297
2013
Mycolicibacterium fortuitum
brenda
Pandeeti, E.V.; Siddavattam, D.
Purification and characterization of catechol 1,2-dioxygenase from Acinetobacter sp. DS002 and cloning, sequencing of partial catA gene
Indian J. Microbiol.
51
312-318
2011
Acinetobacter sp., Acinetobacter sp. DS002
brenda
Guzik, U.; Gren, I.; Hupert-Kocurek, K.; Wojcieszynska, D.
Catechol 1,2-dioxygenase from the new aromatic compounds - degrading Pseudomonas putida strain N6
Int. Biodeter. Biodegrad.
65
504-512
2011
Pseudomonas putida (A7LBQ4), Pseudomonas putida N6 (A7LBQ4)
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brenda
Guzik, U.; Hupert-Kocurek, K.; Sa?ek, K.; Wojcieszynska, D.
Influence of metal ions on bioremediation activity of protocatechuate 3,4-dioxygenase from Stenotrophomonas maltophilia KB2
World J. Microbiol. Biotechnol.
29
267-273
2013
Stenotrophomonas maltophilia, Stenotrophomonas maltophilia KB2
brenda
Wang, Z.; Sun, Y.; Shi, Y.; Song, W.; Zhang, C.
Cloning, expression and characterization of a mesophilic catechol 1,2-dioxygenase from Rhodococcus ruber OA1
Biotechnology
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10-18
2017
Rhodococcus ruber, Rhodococcus ruber OA1
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brenda
Ghosh, S.; Qureshi, A.; Purohit, H.
Enhanced expression of catechol 1,2 dioxygenase gene in biofilm forming Pseudomonas mendocina EGD-AQ5 under increasing benzoate stress
Int. Biodeter. Biodegrad.
118
57-65
2017
Pseudomonas mendocina, Pseudomonas mendocina EGD-AQ5
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brenda
Subbotina, N.; Kolomytseva, M.; Baskunov, B.; Golovlev, L.
Catechol 1,2-dioxygenase induced in Rhodococcus opacus strain 1CP cultured in the presence of 3-hydroxybenzoate
Microbiology (Russian Federation)
85
638-641
2016
Rhodococcus opacus, Rhodococcus opacus 1CP
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brenda
Long, Y.; Yang, S.; Xie, Z.; Cheng, L.
Cloning, expression, and characterization of catechol 1,2-dioxygenase from a phenol-degrading Candida tropicalis JH8 strain
Prep. Biochem. Biotechnol.
46
673-678
2016
Candida tropicalis, Candida tropicalis JH8
brenda
Lin, J.; Milase, R.N.
Purification and characterization of catechol 1,2-dioxygenase from Acinetobacter sp. Y64 strain and Escherichia coli transformants
Protein J.
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2015
Acinetobacter sp. Y64
brenda
Muthu, M.; Ophir, Y.; Macdonald, L.J.; Vaidya, A.; Lloyd-Jones, G.
Versatile catechol dioxygenases in Sphingobium scionense WP01T
Antonie van Leeuwenhoek
111
2293-2301
2018
Sphingobium scionense (A0A346DAQ1), Sphingobium scionense (A0A346DAQ2), Sphingobium scionense, Sphingobium scionense DSM 19371 (A0A346DAQ1), Sphingobium scionense DSM 19371 (A0A346DAQ2)
brenda
Aravind, M.K.; Varalakshmi, P.; John, S.A.; Ashokkumar, B.
Catechol 1,2-dioxygenase from Paracoccus sp. MKU1-A greener and cleaner bio-machinery for cis,cis-muconic acid production by recombinant Escherichia coli
Front. Bioeng. Biotechnol.
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703399
2021
Paracoccus sp. MKU1-A
brenda
Rodriguez-Salazar, J.; Almeida-Juarez, A.G.; Ornelas-Ocampo, K.; Millan-Lopez, S.; Raga-Carbajal, E.; Rodriguez-Mejia, J.L.; Muriel-Millan, L.F.; Godoy-Lozano, E.E.; Rivera-Gomez, N.; Rudino-Pinera, E.; Pardo-Lopez, L.
Characterization of a novel functional trimeric catechol 1,2-dioxygenase from a Pseudomonas stutzeri isolated from the gulf of Mexico
Front. Microbiol.
11
1100
2020
Stutzerimonas stutzeri (A0A6A9R3Z2), Stutzerimonas stutzeri GOM2 (A0A6A9R3Z2)
brenda
Ngoc Thi, T.V.; Hoang Sinh, D.D.; Ha Thanh, L.T.; Huy, N.D.; Tue, N.H.; Shintani, M.; Kimbara, K.; Loc, N.H.
Cloning, expression and characterization of catechol 1,2-dioxygenase from Burkholderia cepacia
J. Gen. Appl. Microbiol.
66
188-194
2020
Burkholderia cepacia (A0A346ARQ0), Burkholderia cepacia (A0A346ARQ5), Burkholderia cepacia, Burkholderia cepacia DF2 (A0A346ARQ0), Burkholderia cepacia DF4 (A0A346ARQ5)
brenda
Han, L.; Chen, S.; Zhou, J.
Expression and cloning of catA encoding a catechol 1,2-dioxygenase from the 2,4-D-degrading strain Cupriavidus campinensis BJ71
Prep. Biochem. Biotechnol.
50
486-493
2020
Cupriavidus campinensis (A0A481S4R2), Cupriavidus campinensis, Cupriavidus campinensis BJ71 (A0A481S4R2)
brenda