HOME
login
history
all enzymes
BRENDA home
History
Information on EC 1.13.11.2 - catechol 2,3-dioxygenase
for references in articles please use BRENDA:EC1.13.11.2Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
1.13.11.2 catechol 2,3-dioxygenaseIUBMB Comments
Requires FeII. The enzyme initiates the meta-cleavage pathway of catechol degradation.
Specify your search results
Word Map
- 1.13.11.2
- heme
- putida
- rubisco
-
ferredoxins
- l-arginine
- flavin
-
biodegradation
- toluene
- ribulose-1,5-bisphosphate
- ribulose
-
rieske
- tetrahydrobiopterin
-
dioxygenation
- naphthalene
- fmn
- 2-oxoglutarate
-
ferrous
-
non-heme
- biphenyls
- semialdehyde
-
nitric-oxide
-
mixed-function
- rhodococcus
-
bioremediation
-
1,5-bisphosphate
- sphingomonas
-
bisphosphate
-
photorespiration
- carbazole
-
2-oxoglutarate-dependent
- phenanthrene
- l-citrulline
- 4-methylcatechol
- comamonas
- biliverdin
- xylene
- bh4
-
photorespiratory
-
dihydroxylation
- l-arg
-
diiron
-
4.1.1.39
- pterin
- testosteroni
-
heme-heme
- ethylbenzene
-
cyclo
-
monooxygenation
- rhodochrous
- environmental protection
- fluorene
- degradation
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
oxygenase, catechol-2,3-dioxygenase, metapyrocatechase, catechol 2,3-oxygenase, meta-cleavage dioxygenase, catechol 2,3 dioxygenase, c2,3o, 3sc23o, extradiol-cleaving catecholic dioxygenase, cd-2,3, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
A23O
AtdB
BupB
C2,3O
C23D
C23o
C23O1
C23O2
CatE
catechol 2,3-di-2,3-pyrocatechase
-
-
-
-
catechol 2,3-dioxygenase
catechol 2,3-oxygenase
-
-
-
-
catechol oxygenase
-
-
-
-
catechol-2,3-dioxygenase
CD-2,3
EC 1.13.1.2
-
-
formerly
-
ECDO
Extradiol-cleaving catecholic dioxygenase
meta-cleavage dioxygenase
metapyrocatechase
oxygenase
-
-
-
-
PheB
pyrocatechol 2,3-dioxygenase
-
-
-
-
Saci_2295
SSO1223
SsoC2,3O
ssol_2912
tbuE
TdnC
XylE
additional information
-
-
Pseudomonas stutzeri NA1 has the nahH gene encoding extradiol catechol 2,3-dioxygenase
C23o
-
metapyrocatechase
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
catechol + O2 = 2-hydroxymuconate-6-semialdehyde
ordered bi uni mechanism
-
catechol + O2 = 2-hydroxymuconate-6-semialdehyde
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
redox reaction
-
-
-
-
reduction
-
-
-
-
oxidation
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
MetaCyc
2-nitrotoluene degradation, catechol degradation to 2-hydroxypentadienoate I, catechol degradation to 2-hydroxypentadienoate II, toluene degradation to 2-hydroxypentadienoate (via 4-methylcatechol), toluene degradation to 2-hydroxypentadienoate (via toluene-cis-diol), toluene degradation to 2-hydroxypentadienoate I (via o-cresol)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
catechol:oxygen 2,3-oxidoreductase (decyclizing)
Requires FeII. The enzyme initiates the meta-cleavage pathway of catechol degradation.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
9029-46-3
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3-formylcatechol + O2
3-formyl-2-hydroxymuconate semialdehyde
-
-
-
?
3-methoxycatechol + O2
2-hydroxy-3-methoxy-6-oxohexa-2,4-dienoate
-
-
-
-
?
3-phenylcatechol + O2
2-hydroxy-3-phenylmuconate semialdehyde
-
-
-
?
3-sulfocatechol + O2 + H2O
(2E,4Z)-2-hydroxymuconate + bisulfite + H+
-
-
-
-
?
4-bromocatechol + O2
4-bromo-2-hydroxymuconate semialdehyde
-
-
-
?
4-hydroxymethylcatechol + O2
2-hydroxy-4-hydroxymethylmuconate semialdehyde
rapid inactivation of enzyme during turnover
-
-
?
4-methylcatechol + O2
2-hydroxy-5-methyl-6-oxohexa-2,4-dienoate + H+
-
-
-
-
?
4-n-butylcatechol + O2
?
Q842G7
activity is 1.85fold higher than with catechol
-
-
?
tetrachlorohydroquinone + O2
?
-
immobilized enzyme, no activity with the free enzyme
-
-
?
2,3-dihydroxybiphenyl + O2
?
Q842G7
1.3% of the activity with 2,3-dihydroxybiphenyl
-
-
?
2,3-dihydroxybiphenyl + O2
?
Q842G7
1.3% of the activity with 2,3-dihydroxybiphenyl
-
-
?
3,4-dimethylcatechol + O2
2-hydroxy-5-methyl-6-oxo-hepta-2,4-dienoate
-
-
-
-
?
3,4-dimethylcatechol + O2
2-hydroxy-5-methyl-6-oxo-hepta-2,4-dienoate
-
-
-
-
?
3,5-dichlorocatechol + O2
?
-
immobilized enzyme, no activity with the free enzyme
-
-
?
3,5-dichlorocatechol + O2
?
-
immobilized enzyme, no activity with the free enzyme
-
-
?
3,5-dimethylcatechol + O2
2-hydroxy-3,5-dimethyl-6-oxohexa-2,4-dienoic acid
-
-
-
-
?
3,5-dimethylcatechol + O2
2-hydroxy-3,5-dimethyl-6-oxohexa-2,4-dienoic acid
-
-
-
-
?
3-chlorocatechol + O2
2-chloro-2-hydroxy-6-oxohexa-2,4-dienoate
-
weak
-
-
?
3-chlorocatechol + O2
2-chloro-2-hydroxy-6-oxohexa-2,4-dienoate
-
weak
-
-
?
3-chlorocatechol + O2
2-chloro-2-hydroxy-6-oxohexa-2,4-dienoate
-
weak
-
-
?
3-chlorocatechol + O2
2-chloro-2-hydroxy-6-oxohexa-2,4-dienoate
-
-
-
-
?
3-chlorocatechol + O2
2-chloro-2-hydroxy-6-oxohexa-2,4-dienoate
-
weak
-
-
?
3-chlorocatechol + O2
3-chloro-2-hydroxymuconate semialdehyde
rapid inactivation of enzyme during turnover
-
-
?
3-chlorocatechol + O2
3-chloro-2-hydroxymuconate semialdehyde
about 9% of the rate with catechol
-
-
?
3-chlorocatechol + O2
3-chloro-2-hydroxymuconate semialdehyde
about 95% of the rate with catechol
-
-
?
3-chlorocatechol + O2
3-chloro-2-hydroxymuconate semialdehyde
about 9% of the rate with catechol
-
-
?
3-methoxycatechol + O2
2-hydroxy-3-methoxymuconate semialdehyde
rapid inactivation of enzyme during turnover
-
-
?
3-methoxycatechol + O2
2-hydroxy-3-methoxymuconate semialdehyde
rapid inactivation of enzyme during turnover
-
-
?
3-methylcatechol + O2
2-hydroxy-3-methylmuconate semialdehyde
-
19% of the activity with catechol
-
-
?
3-methylcatechol + O2
2-hydroxy-3-methylmuconate semialdehyde
-
19% of the activity with catechol
-
-
?
3-methylcatechol + O2
2-hydroxy-3-methylmuconate semialdehyde
poor substrate
-
-
?
3-methylcatechol + O2
2-hydroxy-3-methylmuconate semialdehyde
-
most effective substrate
-
-
?
3-methylcatechol + O2
2-hydroxy-3-methylmuconate semialdehyde
-
most effective substrate
-
-
?
3-methylcatechol + O2
2-hydroxy-3-methylmuconate semialdehyde
about 30% of activity with catechol
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
-
-
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
-
-
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
-
weak
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
-
weak
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
-
6.12% activity compared to catechol
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
-
-
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
-
-
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
about 105% of the rate with catechol
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
about 43% of the rate with catechol
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
-
-
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
about 105% of the rate with catechol
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
-
-
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
about 30% of the rate with catechol
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
about 30% of the rate with catechol
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
-
isoform C23O1 shows 49.5% activity compared to catechol, isoform C23O2 shows 239.2% activity compared to catechol
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoic acid
-
-
-
-
?
3-methylcatechol + O2
?
Q842G7
33% of the activity with 4-chlorocatechol
-
-
?
3-methylcatechol + O2
?
Q842G7
33% of the activity with 4-chlorocatechol
-
-
?
3-methylcatechol + O2
cis,cis-2-hydroxy-6-oxohepta-2,4-dienoate + H+
-
-
-
-
?
3-methylcatechol + O2
cis,cis-2-hydroxy-6-oxohepta-2,4-dienoate + H+
-
-
-
-
?
4-alkylcatechol + O2
?
initial step of long-chain alkylphenol cleavage pathway
-
-
?
4-alkylcatechol + O2
?
alkyl chain length C1-C5 is accepted as substrate
-
-
?
4-chlorocatechol + O2
4-chloro-2-hydroxymuconate semialdehyde
E7DDG2
-
-
-
?
4-chlorocatechol + O2
4-chloro-2-hydroxymuconate semialdehyde
-
44.88% activity compared to catechol
-
-
?
4-chlorocatechol + O2
4-chloro-2-hydroxymuconate semialdehyde
-
-
-
?
4-chlorocatechol + O2
4-chloro-2-hydroxymuconate semialdehyde
about 16% of the rate with catechol
-
-
?
4-chlorocatechol + O2
4-chloro-2-hydroxymuconate semialdehyde
about 75% of the rate with catechol
-
-
?
4-chlorocatechol + O2
4-chloro-2-hydroxymuconate semialdehyde
about 16% of the rate with catechol
-
-
?
4-chlorocatechol + O2
4-chloro-2-hydroxymuconate semialdehyde
at the same rate as catechol
-
-
?
4-chlorocatechol + O2
4-chloro-2-hydroxymuconate semialdehyde
-
isoform C23O1 shows 50.8% activity compared to catechol, isoform C23O2 shows 226.4% activity compared to catechol
-
-
?
4-chlorocatechol + O2
5-chloro-2-hydroxymuconic semialdehyde
-
-
-
?
4-chlorocatechol + O2
?
Q842G7
39% of the activity with 4-chlorocatechol
-
-
?
4-chlorocatechol + O2
?
Q842G7
39% of the activity with 4-chlorocatechol
-
-
?
4-chlorocatechol + O2
?
-
the enzyme shows the highest activity against catechol and 4-chlorocatechol
-
-
?
4-chlorocatechol + O2
?
-
the enzyme shows the highest activity against catechol and 4-chlorocatechol
-
-
?
4-ethylcatechol + O2
4-ethyl-2-hydroxymuconate semialdehyde
effective substrate
-
-
?
4-ethylcatechol + O2
4-ethyl-2-hydroxymuconate semialdehyde
rapid inactivation of enzyme during turnover
-
-
?
4-ethylcatechol + O2
4-ethyl-2-hydroxymuconate semialdehyde
rapid inactivation of enzyme during turnover
-
-
?
4-formylcatechol + O2
4-formyl-2-hydroxymuconate semialdehyde
-
-
-
?
4-formylcatechol + O2
4-formyl-2-hydroxymuconate semialdehyde
rapid inactivation of enzyme during turnover
-
-
?
4-formylcatechol + O2
4-formyl-2-hydroxymuconate semialdehyde
rapid inactivation of enzyme during turnover
-
-
?
4-methylcatechol + O2
2-hydroxy-3-methyl-6-oxohexa-2,4-dienoate
-
hypoxic strains with significantly higher affinities
-
-
?
4-methylcatechol + O2
2-hydroxy-3-methyl-6-oxohexa-2,4-dienoate
-
hypoxic strains with significantly higher affinities
-
-
?
4-methylcatechol + O2
2-hydroxy-3-methyl-6-oxohexa-2,4-dienoate
-
-
-
-
?
4-methylcatechol + O2
2-hydroxy-3-methyl-6-oxohexa-2,4-dienoate
-
-
-
-
?
4-methylcatechol + O2
2-hydroxy-3-methyl-6-oxohexa-2,4-dienoate
-
-
-
-
?
4-methylcatechol + O2
2-hydroxy-3-methyl-6-oxohexa-2,4-dienoate
-
-
-
-
?
4-methylcatechol + O2
2-hydroxy-3-methyl-6-oxohexa-2,4-dienoate
-
weak
-
-
-
4-methylcatechol + O2
2-hydroxy-3-methyl-6-oxohexa-2,4-dienoate
-
weak
-
-
-
4-methylcatechol + O2
2-hydroxy-3-methyl-6-oxohexa-2,4-dienoate
E7DDG2
-
-
-
?
4-methylcatechol + O2
2-hydroxy-3-methyl-6-oxohexa-2,4-dienoate
-
101.91% activity compared to catechol
-
-
?
4-methylcatechol + O2
2-hydroxy-3-methyl-6-oxohexa-2,4-dienoate
-
-
-
-
?
4-methylcatechol + O2
2-hydroxy-3-methyl-6-oxohexa-2,4-dienoate
-
hypoxic strains with significantly higher affinities
-
-
?
4-methylcatechol + O2
2-hydroxy-3-methyl-6-oxohexa-2,4-dienoate
-
hypoxic strains with significantly higher affinities
-
-
?
4-methylcatechol + O2
2-hydroxy-3-methyl-6-oxohexa-2,4-dienoate
-
-
-
-
?
4-methylcatechol + O2
2-hydroxy-3-methyl-6-oxohexa-2,4-dienoate
-
highly specific for
-
-
?
4-methylcatechol + O2
2-hydroxy-3-methyl-6-oxohexa-2,4-dienoate
-
hypoxic strains with significantly higher affinities
-
-
?
4-methylcatechol + O2
2-hydroxy-3-methyl-6-oxohexa-2,4-dienoate
-
-
-
-
?
4-methylcatechol + O2
2-hydroxy-3-methyl-6-oxohexa-2,4-dienoate
-
-
-
-
?
4-methylcatechol + O2
2-hydroxy-3-methyl-6-oxohexa-2,4-dienoate
-
-
-
-
?
4-methylcatechol + O2
2-hydroxy-3-methyl-6-oxohexa-2,4-dienoate
-
hypoxic strains with significantly higher affinities
-
-
?
4-methylcatechol + O2
2-hydroxy-3-methyl-6-oxohexa-2,4-dienoate
-
-
-
-
?
4-methylcatechol + O2
2-hydroxy-3-methyl-6-oxohexa-2,4-dienoate
-
hypoxic strains with significantly higher affinities
-
-
?
4-methylcatechol + O2
2-hydroxy-3-methyl-6-oxohexa-2,4-dienoate
-
hypoxic strains with significantly higher affinities
-
-
?
4-methylcatechol + O2
2-hydroxy-3-methyl-6-oxohexa-2,4-dienoate
-
hypoxic strains with significantly higher affinities
-
-
?
4-methylcatechol + O2
2-hydroxy-3-methyl-6-oxohexa-2,4-dienoate
-
best substrate for isoform C23O2 (280.7% activity compared to catechol), while isoform C23O1 shows 87.4% activity compared to catechol
-
-
?
4-methylcatechol + O2
2-hydroxy-4-methyl-6-oxohexa-2,4-dienoate
about 47% of the rate with catechol
-
-
?
4-methylcatechol + O2
2-hydroxy-4-methyl-6-oxohexa-2,4-dienoate
about 89% of the rate with catechol
-
-
?
4-methylcatechol + O2
2-hydroxy-4-methyl-6-oxohexa-2,4-dienoate
about 47% of the rate with catechol
-
-
?
4-methylcatechol + O2
2-hydroxy-4-methyl-6-oxohexa-2,4-dienoate
about 65% of the rate with catechol
-
-
?
4-methylcatechol + O2
2-hydroxy-4-methyl-6-oxohexa-2,4-dienoate
about 65% of the rate with catechol
-
-
?
4-methylcatechol + O2
2-hydroxy-4-methylmuconate semialdehyde
very effective substrate
-
-
?
4-methylcatechol + O2
2-hydroxy-4-methylmuconate semialdehyde
rapid inactivation of enzyme during turnover
-
-
?
4-methylcatechol + O2
?
Q842G7
activity is 5.72fold higher than with catechol
-
-
?
4-methylcatechol + O2
?
about 65% of activity with catechol
-
-
?
4-nitrocatechol + O2
2-hydroxy-4-nitromuconate semialdehyde
-
-
-
?
4-nitrocatechol + O2
2-hydroxy-4-nitromuconate semialdehyde
rapid inactivation of enzyme during turnover
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
hypoxic strains have enzymes with significantly higher affinities for catechol than for nonhypoxic strains
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
hypoxic strains have enzymes with significantly higher affinities for catechol than for nonhypoxic strains
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
highly specific for
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
highly specific for
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
extradiol dioxygenase reaction
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
highly specific for
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
metacleavage enzyme of catechol metabolism
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
enzyme is a important component in the degradation pathways of toluene and xylene and catalyses the dioxygenolytic cleavage of the aromatic ring
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
metapyrocatechase 1 takes part in oxidation of aromatic compounds, producing catechol as an intermediate, metapyrocatechase 2 is involved in oxidation of methyl-substituted aromatic substrates
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
enzyme is induced by benzenesulfonate, catechol or toluene p-sulfonate
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
hypoxic strains have enzymes with significantly higher affinities for catechol than for nonhypoxic strains
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
enzyme is a important component in the degradation pathways of toluene and xylene and catalyses the dioxygenolytic cleavage of the aromatic ring
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
hypoxic strains have enzymes with significantly higher affinities for catechol than for nonhypoxic strains
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
enzyme is a important component in the degradation pathways of toluene and xylene and catalyses the dioxygenolytic cleavage of the aromatic ring
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
highly specific for
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
hypoxic strains have enzymes with significantly higher affinities for catechol than for nonhypoxic strains
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
best substrates
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
enzyme is a important component in the degradation pathways of toluene and xylene and catalyses the dioxygenolytic cleavage of the aromatic ring
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
degradation of aromatic compounds
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
benzoate degadation pathway
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
key role in the degradation of aromatic molecules
-
-
catechol + O2
2-hydroxymuconate semialdehyde
-
highly specific for
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
highly specific for
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
hypoxic strains have enzymes with significantly higher affinities for catechol than for nonhypoxic strains
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
enzyme is a important component in the degradation pathways of toluene and xylene and catalyses the dioxygenolytic cleavage of the aromatic ring
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
catechol 2,3-dioxygenase is a key enzyme in the catabolism of monocyclic aromatic compounds including aniline and catalyzes the extradiol cleavage of catechol
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
cleavage of aromatic compounds, involved in alpha-ketoadiapate pathway
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
degradation of aromatic compounds
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
involved in metabolism of aromatic compounds
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
key enzyme for the degradation of aromatic compounds
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
catechol 2,3-dioxygenase is involved in the meta phenol degradation pathway
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
catechol 2,3-dioxygenase is a critical enzyme in the multistep biodegradation of 3,4-dichloroaniline by Pseudomonas sp. KB35B
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
catechol 2,3-dioxygenase is a critical enzyme in the multistep biodegradation of 3,4-dichloroaniline by Pseudomonas sp. KB35B
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
cleavage of aromatic compounds, involved in alpha-ketoadiapate pathway
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
highly specific for
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
catechol 2,3-dioxygenase is involved in the meta phenol degradation pathway
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
highly specific for
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
hypoxic strains have enzymes with significantly higher affinities for catechol than for nonhypoxic strains
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
enzyme is a important component in the degradation pathways of toluene and xylene and catalyses the dioxygenolytic cleavage of the aromatic ring
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
most effective substrate
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
most effective substrate
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
hypoxic strains have enzymes with significantly higher affinities for catechol than for nonhypoxic strains
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
enzyme is a important component in the degradation pathways of toluene and xylene and catalyses the dioxygenolytic cleavage of the aromatic ring
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
hypoxic strains have enzymes with significantly higher affinities for catechol than for nonhypoxic strains
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
enzyme is a important component in the degradation pathways of toluene and xylene and catalyses the dioxygenolytic cleavage of the aromatic ring
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
involved in biodegradation of benzothiazoles
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
involved in biodegradation of benzothiazoles
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
degradation of aromatic compounds, involved in toluene and ortho-xylene metabolism
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
degradation of aromatic compounds, involved in toluene and ortho-xylene metabolism
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
and 4-chlorocatechol, best substrates
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
both the ortho- and the meta-degradation pathways are functional in presence of phenol. However, the activation of the catechol 2,3-dioxygenase, only when phenol is present, and the accumulation of only intermediary compounds related to this pathway lead us to the conclusion that the aromatic ring is preferentially opened through the meta-pathway
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
the enzyme shows the highest activity against catechol and 4-chlorocatechol
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
both the ortho- and the meta-degradation pathways are functional in presence of phenol. However, the activation of the catechol 2,3-dioxygenase, only when phenol is present, and the accumulation of only intermediary compounds related to this pathway lead us to the conclusion that the aromatic ring is preferentially opened through the meta-pathway
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
the enzyme shows the highest activity against catechol and 4-chlorocatechol
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
and 4-chlorocatechol, best substrates
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
key enzyme for the degradation of aromatic compounds
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
E7DDG2
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
-
100% activity
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
-
the enzyme is constitutively transcribed
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
the enzyme is constitutively transcribed
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
-
best substrate for isoform C23O1 (100% activity)
-
-
?
hydroquinone + O2
?
-
immobilized enzyme, no activity with the free enzyme
-
-
?
hydroquinone + O2
?
-
immobilized enzyme, no activity with the free enzyme
-
-
?
phenol + O2
2-hydroxymuconic semialdehyde
A5HMH3
utilize phenol as sole carbon and energy source, concentration of phenol diversify from 25 mg/l to 1000 mg/l, assay at 28°C, pH 6.8-7.0
-
-
?
phenol + O2
2-hydroxymuconic semialdehyde
A5HMH3
utilize phenol as sole carbon and energy source, concentration of phenol diversify from 25 mg/l to 1000 mg/l, assay at 28°C, pH 6.8-7.0
-
-
?
additional information
?
-
no cleavage of 4-carboxycatechol, 4-carboxymethylcatechol and 4-tert-butylcatechol
-
-
-
additional information
?
-
Q842G7
no activity with 4-tert-butylcatechol
-
-
-
additional information
?
-
Q842G7
no activity with 4-tert-butylcatechol
-
-
-
additional information
?
-
-
the two isoforms cannot oxidize 1, 2-dihydroxynaphthalene
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4-alkylcatechol + O2
?
Q7WYF5
initial step of long-chain alkylphenol cleavage pathway
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
metacleavage enzyme of catechol metabolism
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
enzyme is a important component in the degradation pathways of toluene and xylene and catalyses the dioxygenolytic cleavage of the aromatic ring
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
metapyrocatechase 1 takes part in oxidation of aromatic compounds, producing catechol as an intermediate, metapyrocatechase 2 is involved in oxidation of methyl-substituted aromatic substrates
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
enzyme is induced by benzenesulfonate, catechol or toluene p-sulfonate
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
enzyme is a important component in the degradation pathways of toluene and xylene and catalyses the dioxygenolytic cleavage of the aromatic ring
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
enzyme is a important component in the degradation pathways of toluene and xylene and catalyses the dioxygenolytic cleavage of the aromatic ring
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
enzyme is a important component in the degradation pathways of toluene and xylene and catalyses the dioxygenolytic cleavage of the aromatic ring
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
P06622
degradation of aromatic compounds
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
benzoate degadation pathway
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
key role in the degradation of aromatic molecules
-
-
catechol + O2
2-hydroxymuconate semialdehyde
-
enzyme is a important component in the degradation pathways of toluene and xylene and catalyses the dioxygenolytic cleavage of the aromatic ring
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
catechol 2,3-dioxygenase is a key enzyme in the catabolism of monocyclic aromatic compounds including aniline and catalyzes the extradiol cleavage of catechol
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
cleavage of aromatic compounds, involved in alpha-ketoadiapate pathway
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
Q83U22
degradation of aromatic compounds
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
Q7WYF5
involved in metabolism of aromatic compounds
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
key enzyme for the degradation of aromatic compounds
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
catechol 2,3-dioxygenase is involved in the meta phenol degradation pathway
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
catechol 2,3-dioxygenase is a critical enzyme in the multistep biodegradation of 3,4-dichloroaniline by Pseudomonas sp. KB35B
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
catechol 2,3-dioxygenase is a critical enzyme in the multistep biodegradation of 3,4-dichloroaniline by Pseudomonas sp. KB35B
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
cleavage of aromatic compounds, involved in alpha-ketoadiapate pathway
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
catechol 2,3-dioxygenase is involved in the meta phenol degradation pathway
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
enzyme is a important component in the degradation pathways of toluene and xylene and catalyses the dioxygenolytic cleavage of the aromatic ring
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
enzyme is a important component in the degradation pathways of toluene and xylene and catalyses the dioxygenolytic cleavage of the aromatic ring
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
enzyme is a important component in the degradation pathways of toluene and xylene and catalyses the dioxygenolytic cleavage of the aromatic ring
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
involved in biodegradation of benzothiazoles
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
involved in biodegradation of benzothiazoles
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
degradation of aromatic compounds, involved in toluene and ortho-xylene metabolism
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
degradation of aromatic compounds, involved in toluene and ortho-xylene metabolism
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
both the ortho- and the meta-degradation pathways are functional in presence of phenol. However, the activation of the catechol 2,3-dioxygenase, only when phenol is present, and the accumulation of only intermediary compounds related to this pathway lead us to the conclusion that the aromatic ring is preferentially opened through the meta-pathway
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
both the ortho- and the meta-degradation pathways are functional in presence of phenol. However, the activation of the catechol 2,3-dioxygenase, only when phenol is present, and the accumulation of only intermediary compounds related to this pathway lead us to the conclusion that the aromatic ring is preferentially opened through the meta-pathway
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
key enzyme for the degradation of aromatic compounds
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
C3W4L8, C3W4L9, C3W4M0, C3W4M1, C3W4M2, C3W4M3, C3W4M4, C3W4M5, C3W4M6, C3W4M7
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
E7DDG2
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
-
the enzyme is constitutively transcribed
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
V5W6K5
the enzyme is constitutively transcribed
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
A7LB47
-
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
Fe3+
-
the enzyme activity increases in the presence of Fe3+ (isoform C23O2 shows 377.37% activity at 5 mM)
Iron
Fe2+
-
incubation of the purified enzyme (PheB) with Fe2+ and ascorbate increases its activity by approximately sevenfold
Fe2+
-
FeCl2 and FeSO4 activate metapyrocatechase 2, no effect on metapyrocatechase 1
Fe2+
-
the activity loss following H2O2 treatment is directly correlated with nearly stoichiometric titration of the active site Fe2+
Fe2+
-
3 gatom of iron per mol of enzyme; activity is closely related to specific content of iron in this protein
Fe2+
-
3.7 mol of iron per mol of enzyme or 0.93 mol per mol of the subunit
Fe2+
-
enzyme might undergo oxidation of its active-site ferrous iron atom
Fe2+
-
the active site comprises three Fe2+ ligands His153, His214 and Glu265
Fe2+
-
the enzyme contains about 2 mol of Fe2+ per mole of protein
Fe2+
Fe2þ ion binding is facilitated via four ligands: two histidine residues, one glutamate residue and one molecule of water, overview
Fe2+
-
the enzyme activity increases in the presence of Fe2+ (isoform C23O1 shows 265.65% activity at 5 mM)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3-vinylcatechol
-
C23O activity (TodE) is almost completely abrogated by exposure to 0.2 mM 3-vinylcatechol
Cd2+
-
minimal inhibitory concentrations cadmium to Variovorax sp. 12S strain in different media, overview
NaN3
-
the immobilized enzyme is less sensitive compared to the free enzyme
catechol
-
wild-type enzyme: substrate inhibition. Mutant enzyme E286K: no substrate inhibition
CuSO4
-
the immobilized enzyme is less sensitive compared to the free enzyme
H2O2
-
complete inhibition at 0.06 mM, addition of ascorbic acid suppresses the inhibitory effect of hydrogen peroxide
H2O2
-
the immobilized enzyme is less sensitive compared to the free enzyme
additional information
-
C23O activity (TodE) is unaffected by styrene, toluene, and 3-methylcatechol
-
additional information
-
not inhibitory: EDTA, o-phenanthroline, 2,2'-dipyridyl
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ascorbate
-
incubation of the purified enzyme (PheB) with Fe2+ and ascorbate increases its activity by approximately sevenfold
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0003
2,2',3-trihydroxybiphenylether
pH and temperature not specified in the publication
0.0012
2,3-Dihydroxybiphenyl
pH and temperature not specified in the publication
0.03
3-methylcatechol
pH and temperature not specified in the publication
additional information
additional information
-
Km of wild-type and hybride enzymes
-
additional information
additional information
-
Km of wild-type and mutant enzymes
-
additional information
additional information
-
Km determination for enzymes from hypoxic and nonhypoxic pseudomonads, Km for oxygen approximately five-fold lower under hypoxic conditions for hypoxic strains
-
additional information
additional information
-
Km determination for enzymes from hypoxic and nonhypoxic pseudomonads, Km for oxygen approximately five-fold lower under hypoxic conditions for hypoxic strains
-
additional information
additional information
-
Km determination for enzymes from hypoxic and nonhypoxic pseudomonads, Km for oxygen approximately five-fold lower under hypoxic conditions for hypoxic strains
-
additional information
additional information
-
Km determination for enzymes from hypoxic and nonhypoxic pseudomonads, Km for oxygen approximately five-fold lower under hypoxic conditions for hypoxic strains
-
additional information
additional information
-
Km determination for enzymes from hypoxic and nonhypoxic pseudomonads, Km for oxygen approximately five-fold lower under hypoxic conditions for hypoxic strains
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
60
2,2',3-trihydroxybiphenylether
pH and temperature not specified in the publication
200
2,3-Dihydroxybiphenyl
pH and temperature not specified in the publication
150
3-methylcatechol
pH and temperature not specified in the publication
additional information
additional information
-
comparison of kcat values of wild-type and mutant enzymes for catechol, 3-methylcatechol and 4-ethylcatechol
-
additional information
additional information
-
kcat values of enzyme and hybrid proteins
-
additional information
additional information
-
kcat values of enzyme and hybrid proteins
-
additional information
additional information
-
the hypoxic strains have enzymes with significantly higher substrate turnover rates for the nonhypoxic strains
-
additional information
additional information
-
the hypoxic strains have enzymes with significantly higher substrate turnover rates for the nonhypoxic strains
-
additional information
additional information
-
the hypoxic strains have enzymes with significantly higher substrate turnover rates for the nonhypoxic strains
-
additional information
additional information
-
the hypoxic strains have enzymes with significantly higher substrate turnover rates for the nonhypoxic strains
-
additional information
additional information
-
the hypoxic strains have enzymes with significantly higher substrate turnover rates for the nonhypoxic strains
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.111
p-nitro