Information on EC 1.13.11.2 - catechol 2,3-dioxygenase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea

EC NUMBER
COMMENTARY
1.13.11.2
-
RECOMMENDED NAME
GeneOntology No.
catechol 2,3-dioxygenase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
catechol + O2 = 2-hydroxymuconate-6-semialdehyde
show the reaction diagram
ordered bi uni mechanism
-
catechol + O2 = 2-hydroxymuconate-6-semialdehyde
show the reaction diagram
mechanism
Pseudomonas putida mt-2
-
catechol + O2 = 2-hydroxymuconate-6-semialdehyde
show the reaction diagram
mechanism
-
catechol + O2 = 2-hydroxymuconate-6-semialdehyde
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
oxidation
-
-
-
-
oxidation
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
2-nitrotoluene degradation
-
Benzoate degradation
-
catechol degradation to 2-oxopent-4-enoate I
-
catechol degradation to 2-oxopent-4-enoate II
-
Chlorocyclohexane and chlorobenzene degradation
-
Metabolic pathways
-
Microbial metabolism in diverse environments
-
Styrene degradation
-
toluene degradation to 2-oxopent-4-enoate (via toluene-cis-diol)
-
toluene degradation to 2-oxopent-4-enoate I (via o-cresol)
-
Xylene degradation
-
SYSTEMATIC NAME
IUBMB Comments
catechol:oxygen 2,3-oxidoreductase (decyclizing)
Requires FeII. The enzyme initiates the meta-cleavage pathway of catechol degradation.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
2,3-dihydroxybenzenesulfonate 2,3-dioxygenase
-
-
3-sulfocatechol-2,3-dioxygenase
-
-
3SC23O
-
-
A23O
Q842G7
-
A23O
Pseudomonas putida MT4
Q842G7
-
-
BupB
Q842G7
-
BupB
Pseudomonas putida MT4
Q842G7
-
-
C2,3O
Pseudomonas stutzeri OX1
-
-
-
C23o
Alcaligenes faecalis IS-46
A5HMH3
-
-
C23o
Planococcus sp.
-
-
C23o
-
-
-
C23o
Pseudomonas putida SH1
P06622
-
-
C23o
Pseudomonas sp. CGMCC2953, Pseudomonas sp. phDV1, Pseudomonas sp. ZJF08
-
-
-
C23o
Ralstonia pickettii PKO1
-
-
-
C23o
Stenotrophomonas maltophilia KB2
-
-
-
C23o
C3W4L8, C3W4L9, C3W4M0, C3W4M1, C3W4M2, C3W4M3, C3W4M4, C3W4M5, C3W4M6, C3W4M7
-
C23o
Variovorax sp.
-
-
C23o
-
-
-
CatE
Bacillus subtilis 168
-
-
-
catechol 2,3-di-2,3-pyrocatechase
-
-
-
-
catechol 2,3-dioxygenase
A5HMH3
-
catechol 2,3-dioxygenase
Alcaligenes faecalis IS-46
A5HMH3
-
-
catechol 2,3-dioxygenase
-
-
catechol 2,3-dioxygenase
-
-
catechol 2,3-dioxygenase
Ralstonia pickettii PKO1
-
-
-
catechol 2,3-dioxygenase
-
-
catechol 2,3-dioxygenase
Stenotrophomonas maltophilia KB2
-
-
-
catechol 2,3-oxygenase
-
-
-
-
catechol oxygenase
-
-
-
-
catechol-2,3-dioxygenase
P06622
-
catechol-2,3-dioxygenase
-
-
catechol-2,3-dioxygenase
Pseudomonas sp. CGMCC2953
-
-
-
CbzE
Q9Z417
-
CbzE
Pseudomonas putida GJ31
Q9Z417
-
-
CD-2,3
-
-
CD-2,3
-
-
-
EC 1.13.1.2
-
-
formerly
-
ECDO
Geobacillus stearothermophilus BR219
-
-
-
extradiol dioxygenase MhpB
-
-
Extradiol-cleaving catecholic dioxygenase
-
-
Extradiol-cleaving catecholic dioxygenase
Geobacillus stearothermophilus BR219
-
-
-
meta-cleavage dioxygenase
-
-
meta-cleavage dioxygenase
-
-
-
metapyrocatechase
-
-
-
-
oxygenase
-
-
-
-
PheB
-
one of the XylE-group enzyms
PheB
Geobacillus stearothermophilus BR219
-
one of the XylE-group enzyms
-
pyrocatechol 2,3-dioxygenase
-
-
-
-
Saci_2295
Q4J6K0
locus name
Saci_2295
Q4J6K0
locus name
-
SSO1223
Q97YT4
locus name
SSO1223
Q97YT4
locus name
-
SsoC2,3O
Q97YT4
-
SsoC2,3O
Q97YT4
-
-
ssol_2912
V5W6K5
gene name
ssol_2912
V5W6K5
gene name
-
tbuE
Ralstonia pickettii PKO1
-
-
-
TdnC
Q52264
-
TdnC
Pseudomonas putida UCC2
Q52264
-
-
XylE
-
one extradiol-cleaving catecholic dioxygenases group
XylE
Geobacillus stearothermophilus BR219
-
one extradiol-cleaving catecholic dioxygenases group
-
XylE
Pseudomonas putida mt2
-
-
-
metapyrocatechase
-
-
additional information
-
-
Pseudomonas stutzeri NA1 has the nahH gene encoding extradiol catechol 2,3-dioxygenase
CAS REGISTRY NUMBER
COMMENTARY
9029-46-3
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
strain YAA, recombinantly expressed in Escherichia coli JM109
-
-
Manually annotated by BRENDA team
strain YAA, recombinantly expressed in Escherichia coli JM109
-
-
Manually annotated by BRENDA team
strain IS-46
UniProt
Manually annotated by BRENDA team
Alcaligenes faecalis IS-46
strain IS-46
UniProt
Manually annotated by BRENDA team
strain 0-1
-
-
Manually annotated by BRENDA team
Alcaligenes sp. 0-1
strain 0-1
-
-
Manually annotated by BRENDA team
glucose grown cells do not possess catechol 2,3-dioxygenase activity in appreciable quantity
-
-
Manually annotated by BRENDA team
Bacillus subtilis 168
-
-
-
Manually annotated by BRENDA team
Burkholderia cepacia G4
strain G4
-
-
Manually annotated by BRENDA team
JS765
-
-
Manually annotated by BRENDA team
strain 335
-
-
Manually annotated by BRENDA team
Cupriavidus necator 335
strain 335
-
-
Manually annotated by BRENDA team
epigeic earthworm used in vermicomposting processes. Comparing initial wet olive cake and wet olive cake inoculated with Eisenia fetida catechol dioxygenase activity is detected. The catechol-dioxygenase apppears to be due to high microbial activity, catechol-dioxygenase is only detected when a vermincomposting process takes place on the wet olive cake.
-
-
Manually annotated by BRENDA team
ATCC 23975
-
-
Manually annotated by BRENDA team
strain JM83
-
-
Manually annotated by BRENDA team
strains ED 8654 and JM 103
-
-
Manually annotated by BRENDA team
Escherichia coli JM83
strain JM83
-
-
Manually annotated by BRENDA team
Geobacillus stearothermophilus BR219
strain BR219
-
-
Manually annotated by BRENDA team
Geobacillus thermoleovorans A2
strain A2
-
-
Manually annotated by BRENDA team
no activity in Pleurotus ostreatus
fungi, strain 3020 DSV7240
-
-
Manually annotated by BRENDA team
no activity in Pseudomonas aeruginosa
strain RW41
-
-
Manually annotated by BRENDA team
no activity in Pseudomonas aeruginosa RW41
strain RW41
-
-
Manually annotated by BRENDA team
no actvity in Fusarium sp.
strain BI, no catechol 2,3-dioxygenase is dectectable. Activity is measured by production of maleylpyruvate (increase in A375 nm) for catechol 2,3-dosygenase.
-
-
Manually annotated by BRENDA team
no actvity in Fusarium sp. BI
strain BI, no catechol 2,3-dioxygenase is dectectable. Activity is measured by production of maleylpyruvate (increase in A375 nm) for catechol 2,3-dosygenase.
-
-
Manually annotated by BRENDA team
isolated from the marine sediment, chromosomal-encoded gene nahH
-
-
Manually annotated by BRENDA team
Ochrobactrum sp. CH-19
isolated from the marine sediment, chromosomal-encoded gene nahH
-
-
Manually annotated by BRENDA team
Planococcus sp.
-
UniProt
Manually annotated by BRENDA team
Planococcus sp.
gene c23o
-
-
Manually annotated by BRENDA team
gene c23o
-
-
Manually annotated by BRENDA team
Pseudomonas aeruginosa ZD 4-3
ZD 4-3
-
-
Manually annotated by BRENDA team
PfF PC20, PfB PC21 - PfB PC23, PfC PC24 - PfB PC26, PfB PC28, PfC PC31, PfB PC32 - PfB PC34, PfB PC37, PfB PC38 and PfF P69 contain catechol 2,3-dioxygenase genes. The strains PfF PC17 and PfF p69 do not contain catechol 2,3-dioxygenase genes
-
-
Manually annotated by BRENDA team
strain CFS 215
-
-
Manually annotated by BRENDA team
Pseudomonas fluorescens CFS 215
strain CFS 215
-
-
Manually annotated by BRENDA team
strain Pmen PC1 - strain Pmen PC12 and Pmen PC19, all analysed stains contain catechol 2,3-dioxygenase genes
-
-
Manually annotated by BRENDA team
ATCC 23973
-
-
Manually annotated by BRENDA team
C-1, ATCC 23974
-
-
Manually annotated by BRENDA team
F1 and PaW1
-
-
Manually annotated by BRENDA team
KT 2440; PaW94
-
-
Manually annotated by BRENDA team
mt-2 paW1, ATCC 23973
-
-
Manually annotated by BRENDA team
mt-2, used for identifying potential sites of introducing disulfide bond of C23O from Pseudomonas sp.
UniProt
Manually annotated by BRENDA team
PpG 1064
-
-
Manually annotated by BRENDA team
pWWO-161 and UWC1
-
-
Manually annotated by BRENDA team
strain GJ31
SwissProt
Manually annotated by BRENDA team
strain mt-2
UniProt
Manually annotated by BRENDA team
strain mt2
-
-
Manually annotated by BRENDA team
strain MT4, recombinantly expressed in Escherichia coli
SwissProt
Manually annotated by BRENDA team
strain Ppu PC13 - Ppu PC16, Ppu PC30, Ppu PC35, Ppu PC36 and Ppu PC39 contain catechol 2,3-dioxygenase genes. The stains Ppu PC14-PC16 and Ppu PC30 do not contain catechol 2,3-dioxygenase genes
-
-
Manually annotated by BRENDA team
strain UCC2
SwissProt
Manually annotated by BRENDA team
UWC1-pQM899
-
-
Manually annotated by BRENDA team
Pseudomonas putida GJ31
GJ31
-
-
Manually annotated by BRENDA team
Pseudomonas putida GJ31
strain GJ31
SwissProt
Manually annotated by BRENDA team
Pseudomonas putida KT 2440
KT 2440
-
-
Manually annotated by BRENDA team
Pseudomonas putida mt-2
-
SwissProt
Manually annotated by BRENDA team
Pseudomonas putida mt2
strain mt2
-
-
Manually annotated by BRENDA team
Pseudomonas putida MT4
strain MT4, recombinantly expressed in Escherichia coli
SwissProt
Manually annotated by BRENDA team
Pseudomonas putida PaW94
PaW94
-
-
Manually annotated by BRENDA team
Pseudomonas putida PpG 1064
PpG 1064
-
-
Manually annotated by BRENDA team
Pseudomonas putida Ppu PC13
strain Ppu PC13 - Ppu PC16, Ppu PC30, Ppu PC35, Ppu PC36 and Ppu PC39 contain catechol 2,3-dioxygenase genes. The stains Ppu PC14-PC16 and Ppu PC30 do not contain catechol 2,3-dioxygenase genes
-
-
Manually annotated by BRENDA team
Pseudomonas putida SH1
-
UniProt
Manually annotated by BRENDA team
Pseudomonas putida T-2
T-2
-
-
Manually annotated by BRENDA team
Pseudomonas putida UCC2
strain UCC2
SwissProt
Manually annotated by BRENDA team
Pseudomonas putida UWC1-pQM899
UWC1-pQM899
-
-
Manually annotated by BRENDA team
enzyme subgroup I.2.A, hybrid enzymes with type I.2.B enzyme from Sphingomonas sp.
-
-
Manually annotated by BRENDA team
isolated from the marine sediment, plasmid-encoded gene nahH
UniProt
Manually annotated by BRENDA team
strain CGMCC2953
-
-
Manually annotated by BRENDA team
strain KB35B
-
-
Manually annotated by BRENDA team
strain KL28
Uniprot
Manually annotated by BRENDA team
strain ND6
-
-
Manually annotated by BRENDA team
strain phDV1
-
-
Manually annotated by BRENDA team
strain ZJF08
-
-
Manually annotated by BRENDA team
strains 1YB2 and 1YdBTEX2
Uniprot
Manually annotated by BRENDA team
Pseudomonas sp. CGMCC2953
strain CGMCC2953
-
-
Manually annotated by BRENDA team
isolated from the marine sediment, plasmid-encoded gene nahH
UniProt
Manually annotated by BRENDA team
strain KB35B
-
-
Manually annotated by BRENDA team
Pseudomonas sp. KL28
strain KL28
Uniprot
Manually annotated by BRENDA team
strain ND6
-
-
Manually annotated by BRENDA team
Pseudomonas sp. OC1
OC1
-
-
Manually annotated by BRENDA team
strain phDV1
-
-
Manually annotated by BRENDA team
Pseudomonas sp. W31
W31
-
-
Manually annotated by BRENDA team
strain ZJF08
-
-
Manually annotated by BRENDA team
amino acid sequence of nahH from Pseudomonas stutzeri NA1 shows 96% sequence identity with the catechol 2,3-dioxygenase gene from Pseudomonas putida strain H.; strain NA1. Absorption spectra and gas chromatography/mass spectrometry analyses of intermediate metabolites of salicylate or catechol degradation by a crude extract of Pseudomonas stutzeri NA1 reveals the presence of the meta-ring cleavage product 2-hydroxymuconate semialdehyde as a major constituent.
-
-
Manually annotated by BRENDA team
strain OX1
SwissProt
Manually annotated by BRENDA team
Pseudomonas stutzeri NA1.
amino acid sequence of nahH from Pseudomonas stutzeri NA1 shows 96% sequence identity with the catechol 2,3-dioxygenase gene from Pseudomonas putida strain H.; strain NA1. Absorption spectra and gas chromatography/mass spectrometry analyses of intermediate metabolites of salicylate or catechol degradation by a crude extract of Pseudomonas stutzeri NA1 reveals the presence of the meta-ring cleavage product 2-hydroxymuconate semialdehyde as a major constituent.
-
-
Manually annotated by BRENDA team
Pseudomonas stutzeri OX1
OX1
-
-
Manually annotated by BRENDA team
Pseudomonas stutzeri OX1
strain OX1
SwissProt
Manually annotated by BRENDA team
strain PK01
-
-
Manually annotated by BRENDA team
Ralstonia pickettii PK01
strain PK01
-
-
Manually annotated by BRENDA team
Ralstonia pickettii PKO1
-
-
-
Manually annotated by BRENDA team
strain PA, activity detected with 2-hydroxyboenzothiazole as growth substrate
-
-
Manually annotated by BRENDA team
Rhodococcus pyridinivorans PA
strain PA, activity detected with 2-hydroxyboenzothiazole as growth substrate
-
-
Manually annotated by BRENDA team
Rhodococcus rhodochrous CTM
strain CTM
-
-
Manually annotated by BRENDA team
strain DK17
-
-
Manually annotated by BRENDA team
strain DK17
-
-
Manually annotated by BRENDA team
enzyme subgroup I.2.B, hybrid enzymes with type I.2.A enzyme from Pseudomonas sp.
-
-
Manually annotated by BRENDA team
isolated from the marine sediment, chromosomal-encoded gene nahH
-
-
Manually annotated by BRENDA team
isolated from the marine sediment, chromosomal-encoded gene nahH
-
-
Manually annotated by BRENDA team
Stenotrophomonas maltophilia KB2
-
-
-
Manually annotated by BRENDA team
Stenotrophomonas maltophilia KB2
-
UniProt
Manually annotated by BRENDA team
Stenotrophomonas maltophilia KB2
strain KB2
-
-
Manually annotated by BRENDA team
strain 98/2
SwissProt
Manually annotated by BRENDA team
Variovorax sp.
strain isolated from a heavy metal-polluted soil
-
-
Manually annotated by BRENDA team
strain isolated from a heavy metal-polluted soil
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
evolution
A7LB47
the enzyme belongs to the single-ring substrate subfamily of the extradiol dioxygenase
evolution
Stenotrophomonas maltophilia KB2
-
the enzyme belongs to the single-ring substrate subfamily of the extradiol dioxygenase
-
malfunction
-
inactivation of TodE and the subsequent accumulation of 3-vinylcatechol results in toxicity and cell death
metabolism
-
the enzyme catalyzes a step in the degradation of phenanthrene, overview
metabolism
Q34135
the enzyme catalyzes a step in the degradation of phenanthrene, overview
metabolism
-
the enzyme catalyzes a step in the degradation of phenanthrene, overview
physiological function
-
catechol-2,3-dioxygenase contributes to quinone resistance
physiological function
-
overexpressing TodE is necessary to allow Pseudomonas putida strain F1 to grow on styrene
physiological function
Planococcus sp.
-
catechol 2,3-dioxygenases play a role in the degradation of monoaromatic hydrocarbons
physiological function
V5W6K5
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
physiological function
Bacillus subtilis 168
-
catechol-2,3-dioxygenase contributes to quinone resistance
-
physiological function
-
catechol 2,3-dioxygenases play a role in the degradation of monoaromatic hydrocarbons
-
physiological function
-
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
-
metabolism
-
the enzyme catalyzes a step in the degradation of phenanthrene, overview
-
additional information
Planococcus sp.
E7DDG2
Planococcus sp. strain S5 grown on 1 or 2 mM phenol shows activity of both a catechol 1,2- and catechol 2,3-dioxygenase while at a higher concentrations of phenol only catechol 2,3-dioxygenase activity is observed
additional information
-
there is a hydrophobic channel in the active site of catechol 2,3-dioxygenase. Through this channel catechol penetrates into the active site of the enzyme
additional information
Planococcus sp.
-
the enzyme is a member of the superfamily I, subfamily 2A of extradiol dioxygenases
additional information
-
Planococcus sp. strain S5 grown on 1 or 2 mM phenol shows activity of both a catechol 1,2- and catechol 2,3-dioxygenase while at a higher concentrations of phenol only catechol 2,3-dioxygenase activity is observed; the enzyme is a member of the superfamily I, subfamily 2A of extradiol dioxygenases
-
additional information
Stenotrophomonas maltophilia KB2
-
there is a hydrophobic channel in the active site of catechol 2,3-dioxygenase. Through this channel catechol penetrates into the active site of the enzyme
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2,3-dihydroxybiphenyl + O2
?
show the reaction diagram
-
-
-
-
?
2,3-dihydroxybiphenyl + O2
?
show the reaction diagram
-
-
-
-
?
2,3-dihydroxybiphenyl + O2
?
show the reaction diagram
-
-
-
-
?
2,3-dihydroxybiphenyl + O2
?
show the reaction diagram
-
-
-
-
?
2,3-dihydroxybiphenyl + O2
?
show the reaction diagram
P17262
poor substrate
-
-
?
2,3-dihydroxybiphenyl + O2
?
show the reaction diagram
Q842G7
1.3% of the activity with 2,3-dihydroxybiphenyl
-
-
?
2,3-dihydroxybiphenyl + O2
?
show the reaction diagram
-
5% of the activity with catechol
-
-
?
2,3-dihydroxybiphenyl + O2
?
show the reaction diagram
-
-
-
-
?
2,3-dihydroxybiphenyl + O2
?
show the reaction diagram
Pseudomonas putida MT4
Q842G7
1.3% of the activity with 2,3-dihydroxybiphenyl
-
-
?
2,3-dihydroxybiphenyl + O2
?
show the reaction diagram
Rhodococcus rhodochrous CTM
-
-
-
-
?
2,3-dihydroxybiphenyl + O2
?
show the reaction diagram
-
5% of the activity with catechol
-
-
?
2,3-dihydroxybiphenyl + O2
?
show the reaction diagram
-
-
-
-
?
2,3-dihydroxybiphenyl + O2
?
show the reaction diagram
Cupriavidus necator 335
-
-
-
-
?
2,4-dichlorophenol + O2
?
show the reaction diagram
-
-
-
-
?
2,4-dichlorophenol + O2
?
show the reaction diagram
Stenotrophomonas maltophilia KB2
-
-
-
-
?
2-chlorophenol + O2
?
show the reaction diagram
-
-
-
-
?
2-chlorophenol + O2
?
show the reaction diagram
Stenotrophomonas maltophilia KB2
-
-
-
-
?
2-methylphenol + O2
?
show the reaction diagram
-
-
-
-
?
2-methylphenol + O2
?
show the reaction diagram
Stenotrophomonas maltophilia, Stenotrophomonas maltophilia KB2
A7LB47
-
-
-
?
3,4-dihydroxybenzoate + O2
?
show the reaction diagram
-
-
-
-
?
3,4-dihydroxybenzoate + O2
?
show the reaction diagram
-
weak
-
-
?
3,4-dihydroxybenzoate + O2
?
show the reaction diagram
Cupriavidus necator 335
-
-
-
-
?
3,4-dimethylcatechol + O2
2-hydroxy-5-methyl-6-oxo-hepta-2,4-dienoate
show the reaction diagram
-
-
-
-
?
3,5-dichlorocatechol + O2
?
show the reaction diagram
-
-
-
-
?
3,5-dichlorocatechol + O2
?
show the reaction diagram
Stenotrophomonas maltophilia, Stenotrophomonas maltophilia KB2
-
immobilized enzyme, no activity with the free enzyme
-
-
?
3,5-dimethylcatechol + O2
2-hydroxy-3,5-dimethyl-6-oxohexa-2,4-dienoic acid
show the reaction diagram
Pseudomonas stutzeri, Pseudomonas stutzeri OX1
-
-
-
-
?
3-chlorocatechol + O2
2-chloro-2-hydroxy-6-oxohexa-2,4-dienoate
show the reaction diagram
-
-
-
-
?
3-chlorocatechol + O2
2-chloro-2-hydroxy-6-oxohexa-2,4-dienoate
show the reaction diagram
-
not
-
-
-
3-chlorocatechol + O2
2-chloro-2-hydroxy-6-oxohexa-2,4-dienoate
show the reaction diagram
-
weak
-
-
?
3-chlorocatechol + O2
2-chloro-2-hydroxy-6-oxohexa-2,4-dienoate
show the reaction diagram
-
weak
-
-
?
3-chlorocatechol + O2
2-chloro-2-hydroxy-6-oxohexa-2,4-dienoate
show the reaction diagram
Geobacillus thermoleovorans, Geobacillus thermoleovorans A2
-
weak
-
-
?
3-chlorocatechol + O2
2-chloro-2-hydroxy-6-oxohexa-2,4-dienoate
show the reaction diagram
Pseudomonas putida GJ31
-
-
-
-
?
3-chlorocatechol + O2
2-chloro-2-hydroxy-6-oxohexa-2,4-dienoate
show the reaction diagram
-
weak
-
-
?
3-chlorocatechol + O2
3-chloro-2-hydroxymuconate semialdehyde
show the reaction diagram
P06622
rapid inactivation of enzyme during turnover
-
-
?
3-chlorocatechol + O2
3-chloro-2-hydroxymuconate semialdehyde
show the reaction diagram
Q52264, Q9Z417
about 9% of the rate with catechol
-
-
?
3-chlorocatechol + O2
3-chloro-2-hydroxymuconate semialdehyde
show the reaction diagram
Q52264, Q9Z417
about 95% of the rate with catechol
-
-
?
3-chlorocatechol + O2
3-chloro-2-hydroxymuconate semialdehyde
show the reaction diagram
Pseudomonas putida UCC2
Q52264
about 9% of the rate with catechol
-
-
?
3-chlorocatechol + O2
3-chloro-2-hydroxymuconate semialdehyde
show the reaction diagram
Pseudomonas putida GJ31
Q9Z417
about 95% of the rate with catechol
-
-
?
3-formylcatechol + O2
3-formyl-2-hydroxymuconate semialdehyde
show the reaction diagram
P06622
-
-
-
?
3-hydroxycatechol + O2
3-hydroxymuconic acid
show the reaction diagram
-
-
-
?
3-hydroxycatechol + O2
3-hydroxymuconic acid
show the reaction diagram
-
-
-
-
?
3-methoxycatechol + O2
2-hydroxy-3-methoxy-6-oxohexa-2,4-dienoate
show the reaction diagram
-
-
-
-
?
3-methoxycatechol + O2
2-hydroxy-3-methoxymuconate semialdehyde
show the reaction diagram
-, Q8KLV4
rapid inactivation of enzyme during turnover
-
-
?
3-methoxycatechol + O2
2-hydroxy-3-methoxymuconate semialdehyde
show the reaction diagram
Pseudomonas stutzeri OX1
Q8KLV4
rapid inactivation of enzyme during turnover
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
show the reaction diagram
-
-
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
show the reaction diagram
-
-
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
show the reaction diagram
-
-
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
show the reaction diagram
-
-
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
show the reaction diagram
-
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
show the reaction diagram
-
-
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
show the reaction diagram
-
-
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
show the reaction diagram
-
-
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
show the reaction diagram
-
-
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
show the reaction diagram
-
weak
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
show the reaction diagram
-
weak
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
show the reaction diagram
Q52264, Q9Z417
about 105% of the rate with catechol
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
show the reaction diagram
Q97YT4, -
about 30% of the rate with catechol
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
show the reaction diagram
Q52264, Q9Z417
about 43% of the rate with catechol
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
show the reaction diagram
Pseudomonas putida KT 2440
-
-
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
show the reaction diagram
Escherichia coli JM83
-
-
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
show the reaction diagram
Pseudomonas putida UCC2
Q52264
about 105% of the rate with catechol
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
show the reaction diagram
Geobacillus thermoleovorans A2
-
weak
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
show the reaction diagram
Pseudomonas fluorescens CFS 215, Ralstonia pickettii PK01
-
-
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
show the reaction diagram
Pseudomonas putida GJ31
Q9Z417
about 43% of the rate with catechol
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
show the reaction diagram
Burkholderia cepacia G4, Pseudomonas sp. W31
-
-
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
show the reaction diagram
Alcaligenes sp. 0-1
-
-
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
show the reaction diagram
-
-
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
show the reaction diagram
Pseudomonas putida PaW94
-
-
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
show the reaction diagram
Cupriavidus necator 335
-
-
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
show the reaction diagram
Q97YT4, -
about 30% of the rate with catechol
-
-
?
3-methylcatechol + O2
?
show the reaction diagram
-
-
-
-
?
3-methylcatechol + O2
?
show the reaction diagram
Q97YT4, -
-
-
-
?
3-methylcatechol + O2
?
show the reaction diagram
Planococcus sp.
E7DDG2
-
-
-
?
3-methylcatechol + O2
?
show the reaction diagram
Pseudomonas putida, Pseudomonas putida MT4
Q842G7
33% of the activity with 4-chlorocatechol
-
-
?
3-methylcatechol + O2
?
show the reaction diagram
Q97YT4
-
-
-
?
3-methylcatechol + O2
?
show the reaction diagram
Stenotrophomonas maltophilia KB2
-
-
-
-
?
3-methylcatechol + O2
?
show the reaction diagram
E7DDG2
-
-
-
?
3-methylcatechol + O2
2-hydroxy-3-methylmuconate semialdehyde
show the reaction diagram
Q83U22
-
-
-
?
3-methylcatechol + O2
2-hydroxy-3-methylmuconate semialdehyde
show the reaction diagram
P17262
poor substrate
-
-
?
3-methylcatechol + O2
2-hydroxy-3-methylmuconate semialdehyde
show the reaction diagram
-
most effective substrate
-
-
?
3-methylcatechol + O2
2-hydroxy-3-methylmuconate semialdehyde
show the reaction diagram
-
19% of the activity with catechol
-
-
?
3-methylcatechol + O2
2-hydroxy-3-methylmuconate semialdehyde
show the reaction diagram
Q97YT4, -
about 30% of activity with catechol
-
-
?
3-methylcatechol + O2
2-hydroxy-3-methylmuconate semialdehyde
show the reaction diagram
-
most effective substrate
-
-
?
3-methylcatechol + O2
2-hydroxy-3-methylmuconate semialdehyde
show the reaction diagram
-
19% of the activity with catechol
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoic acid
show the reaction diagram
Pseudomonas stutzeri, Pseudomonas stutzeri OX1
-
-
-
-
?
3-methylcatechol + O2
cis,cis-2-hydroxy-6-oxohepta-2,4-dienoate + H+
show the reaction diagram
Ralstonia pickettii, Ralstonia pickettii PKO1
-
-
-
-
?
3-methylphenol + O2
?
show the reaction diagram
-
-
-
-
?
3-methylphenol + O2
?
show the reaction diagram
Stenotrophomonas maltophilia, Stenotrophomonas maltophilia KB2
A7LB47
-
-
-
?
3-phenylcatechol + O2
2-hydroxy-3-phenylmuconate semialdehyde
show the reaction diagram
P06622
-
-
-
?
3-sulfocatechol + O2 + H2O
(2E,4Z)-2-hydroxymuconate + bisulfite + H+
show the reaction diagram
-
-
-
-
?
3-vinylcatechol + O2
?
show the reaction diagram
-
-
-
-
?
4,5-dichlorocatechol + O2
?
show the reaction diagram
-
-
-
-
?
4-alkylcatechol + O2
?
show the reaction diagram
P17262
initial step of long-chain alkylphenol cleavage pathway, alkyl chain length C1-C5 is accepted as substrate
-
-
?
4-bromocatechol + O2
4-bromo-2-hydroxymuconate semialdehyde
show the reaction diagram
P06622
-
-
-
?
4-chlorocatechol + O2
?
show the reaction diagram
Q97YT4, -
-
-
-
?
4-chlorocatechol + O2
?
show the reaction diagram
Planococcus sp.
E7DDG2
-
-
-
?
4-chlorocatechol + O2
?
show the reaction diagram
Q842G7
39% of the activity with 4-chlorocatechol
-
-
?
4-chlorocatechol + O2
?
show the reaction diagram
-
46% of the activity with catechol
-
-
?
4-chlorocatechol + O2
?
show the reaction diagram
V5W6K5
the enzyme shows the highest activity against catechol and 4-chlorocatechol
-
-
?
4-chlorocatechol + O2
?
show the reaction diagram
Pseudomonas putida MT4
Q842G7
39% of the activity with 4-chlorocatechol
-
-
?
4-chlorocatechol + O2
?
show the reaction diagram
-
46% of the activity with catechol
-
-
?
4-chlorocatechol + O2
?
show the reaction diagram
E7DDG2
-
-
-
?
4-chlorocatechol + O2
?
show the reaction diagram
Q97YT4, -
-
-
-
?
4-chlorocatechol + O2
?
show the reaction diagram
V5W6K5
the enzyme shows the highest activity against catechol and 4-chlorocatechol
-
-
?
4-chlorocatechol + O2
5-chloro-2-hydroxymuconic semialdehyde
show the reaction diagram
-
-
-
?
4-chlorocatechol + O2
5-chloro-2-hydroxymuconic semialdehyde
show the reaction diagram
-
-
-
-
?
4-chlorocatechol + O2
5-chloro-2-hydroxymuconic semialdehyde
show the reaction diagram
-
-
-
-
?
4-chlorocatechol + O2
5-chloro-2-hydroxymuconic semialdehyde
show the reaction diagram
Q7BH44
-
-
-
?
4-chlorocatechol + O2
5-chloro-2-hydroxymuconic semialdehyde
show the reaction diagram
-
weak
-
-
?
4-chlorocatechol + O2
4-chloro-2-hydroxymuconate
show the reaction diagram
Q83U22
-
-
-
?
4-chlorocatechol + O2
4-chloro-2-hydroxymuconate semialdehyde
show the reaction diagram
P06622
-
-
-
?
4-chlorocatechol + O2
4-chloro-2-hydroxymuconate semialdehyde
show the reaction diagram
Q52264, Q9Z417
about 16% of the rate with catechol
-
-
?
4-chlorocatechol + O2
4-chloro-2-hydroxymuconate semialdehyde
show the reaction diagram
Q52264, Q9Z417
about 75% of the rate with catechol
-
-
?
4-chlorocatechol + O2
4-chloro-2-hydroxymuconate semialdehyde
show the reaction diagram
Q97YT4, -
at the same rate as catechol
-
-
?
4-chlorocatechol + O2
4-chloro-2-hydroxymuconate semialdehyde
show the reaction diagram
Pseudomonas putida UCC2
Q52264
about 16% of the rate with catechol
-
-
?
4-chlorocatechol + O2
4-chloro-2-hydroxymuconate semialdehyde
show the reaction diagram
Pseudomonas putida GJ31
Q9Z417
about 75% of the rate with catechol
-
-
?
4-chlorophenol + O2
?
show the reaction diagram
-
-
-
-
?
4-ethylcatechol + O2
4-ethyl-2-hydroxymuconate semialdehyde
show the reaction diagram
P17262
effective substrate
-
-
?
4-ethylcatechol + O2
4-ethyl-2-hydroxymuconate semialdehyde
show the reaction diagram
-, Q8KLV4
rapid inactivation of enzyme during turnover
-
-
?
4-ethylcatechol + O2
4-ethyl-2-hydroxymuconate semialdehyde
show the reaction diagram
Pseudomonas stutzeri OX1
Q8KLV4
rapid inactivation of enzyme during turnover
-
-
?
4-fluorocatechol + O2
3-fluoro-2-hydroxy-6-oxohexa-2,4-dienoate
show the reaction diagram
-
-
-
-
?
4-formylcatechol + O2
4-formyl-2-hydroxymuconate semialdehyde
show the reaction diagram
P06622
-
-
-
?
4-formylcatechol + O2
4-formyl-2-hydroxymuconate semialdehyde
show the reaction diagram
-, Q8KLV4
rapid inactivation of enzyme during turnover
-
-
?
4-formylcatechol + O2
4-formyl-2-hydroxymuconate semialdehyde
show the reaction diagram
Pseudomonas stutzeri OX1
Q8KLV4
rapid inactivation of enzyme during turnover
-
-
?
4-hydroxymethylcatechol + O2
2-hydroxy-4-hydroxymethylmuconate semialdehyde
show the reaction diagram
P06622
rapid inactivation of enzyme during turnover
-
-
?
4-methylcatechol + O2
2-hydroxy-4-methyl-6-oxohexa-2,4-dienoate
show the reaction diagram
Q52264, Q9Z417
about 47% of the rate with catechol
-
-
?
4-methylcatechol + O2
2-hydroxy-4-methyl-6-oxohexa-2,4-dienoate
show the reaction diagram
Q97YT4, -
about 65% of the rate with catechol
-
-
?
4-methylcatechol + O2
2-hydroxy-4-methyl-6-oxohexa-2,4-dienoate
show the reaction diagram
Q52264, Q9Z417
about 89% of the rate with catechol
-
-
?
4-methylcatechol + O2
2-hydroxy-4-methyl-6-oxohexa-2,4-dienoate
show the reaction diagram
Pseudomonas putida UCC2
Q52264
about 47% of the rate with catechol
-
-
?
4-methylcatechol + O2
2-hydroxy-4-methyl-6-oxohexa-2,4-dienoate
show the reaction diagram
Pseudomonas putida GJ31
Q9Z417
about 89% of the rate with catechol
-
-
?
4-methylcatechol + O2
2-hydroxy-4-methyl-6-oxohexa-2,4-dienoate
show the reaction diagram
Q97YT4, -
about 65% of the rate with catechol
-
-
?
4-methylcatechol + O2
2-hydroxy-3-methyl-6-oxohexa-2,4-dienoate
show the reaction diagram
-
-
-
-
-
4-methylcatechol + O2
2-hydroxy-3-methyl-6-oxohexa-2,4-dienoate
show the reaction diagram
-
-
-
-
?
4-methylcatechol + O2
2-hydroxy-3-methyl-6-oxohexa-2,4-dienoate
show the reaction diagram
-
-
-
-
?
4-methylcatechol + O2
2-hydroxy-3-methyl-6-oxohexa-2,4-dienoate
show the reaction diagram
-
-
-
-
?
4-methylcatechol + O2
2-hydroxy-3-methyl-6-oxohexa-2,4-dienoate
show the reaction diagram
-
-
-
-
?
4-methylcatechol + O2
2-hydroxy-3-methyl-6-oxohexa-2,4-dienoate
show the reaction diagram
-
-
-
-
?
4-methylcatechol + O2
2-hydroxy-3-methyl-6-oxohexa-2,4-dienoate
show the reaction diagram
-
weak
-
-
-
4-methylcatechol + O2
2-hydroxy-3-methyl-6-oxohexa-2,4-dienoate
show the reaction diagram
-
highly specific for
-
-
?
4-methylcatechol + O2
2-hydroxy-3-methyl-6-oxohexa-2,4-dienoate
show the reaction diagram
-
hypoxic strains with significantly higher affinities
-
-
?
4-methylcatechol + O2
2-hydroxy-3-methyl-6-oxohexa-2,4-dienoate
show the reaction diagram
Pseudomonas putida KT 2440
-
-
-
-
?
4-methylcatechol + O2
2-hydroxy-3-methyl-6-oxohexa-2,4-dienoate
show the reaction diagram
Escherichia coli JM83
-
-
-
-
?
4-methylcatechol + O2
2-hydroxy-3-methyl-6-oxohexa-2,4-dienoate
show the reaction diagram
Geobacillus thermoleovorans A2
-
weak
-
-
-
4-methylcatechol + O2
2-hydroxy-3-methyl-6-oxohexa-2,4-dienoate
show the reaction diagram
Pseudomonas fluorescens CFS 215, Ralstonia pickettii PK01, Burkholderia cepacia G4, Pseudomonas sp. W31
-
hypoxic strains with significantly higher affinities
-
-
?
4-methylcatechol + O2
2-hydroxy-3-methyl-6-oxohexa-2,4-dienoate
show the reaction diagram
-
-
-
-
?
4-methylcatechol + O2
2-hydroxy-3-methyl-6-oxohexa-2,4-dienoate
show the reaction diagram
Pseudomonas putida PaW94
-
-
-
-
?
4-methylcatechol + O2
2-hydroxy-3-methyl-6-oxohexa-2,4-dienoate
show the reaction diagram
Cupriavidus necator 335
-
-
-
-
?
4-methylcatechol + O2
2-hydroxy-4-methylmuconate semialdehyde
show the reaction diagram
Q83U22
-
-
-
?
4-methylcatechol + O2
2-hydroxy-4-methylmuconate semialdehyde
show the reaction diagram
-
-
-
-
?
4-methylcatechol + O2
2-hydroxy-4-methylmuconate semialdehyde
show the reaction diagram
P17262
very effective substrate
-
-
?
4-methylcatechol + O2
2-hydroxy-4-methylmuconate semialdehyde
show the reaction diagram
-, Q8KLV4
rapid inactivation of enzyme during turnover
-
-
?
4-methylcatechol + O2
?
show the reaction diagram
-
-
-
-
?
4-methylcatechol + O2
?
show the reaction diagram
Q97YT4, -
-
-
-
?
4-methylcatechol + O2
?
show the reaction diagram
Planococcus sp.
E7DDG2
-
-
-
?
4-methylcatechol + O2
?
show the reaction diagram
-
57% of the activity with catechol
-
-
?
4-methylcatechol + O2
?
show the reaction diagram
Q97YT4, -
about 65% of activity with catechol
-
-
?
4-methylcatechol + O2
?
show the reaction diagram
Q842G7
activity is 5.72fold higher than with catechol
-
-
?
4-methylcatechol + O2
?
show the reaction diagram
-
57% of the activity with catechol
-
-
?
4-methylcatechol + O2
?
show the reaction diagram
Q97YT4
-
-
-
?
4-methylcatechol + O2
?
show the reaction diagram
E7DDG2
-
-
-
?
4-methylcatechol + O2
2-hydroxy-5-methyl-6-oxohexa-2,4-dienoate + H+
show the reaction diagram
-
-
-
-
?
4-Methylphenol + O2
?
show the reaction diagram
Stenotrophomonas maltophilia, Stenotrophomonas maltophilia KB2
A7LB47
-
-
-
?
4-n-butylcatechol + O2
?
show the reaction diagram
Q842G7
activity is 1.85fold higher than with catechol
-
-
?
4-n-heptylcatechol + O2
?
show the reaction diagram
Q842G7
45% of the activity with catechol
-
-
?
4-n-hexylcatechol + O2
?
show the reaction diagram
Q842G7
53% of the activity with catechol
-
-
?
4-n-nonylcatechol + O2
?
show the reaction diagram
Q842G7
10% of the activity with catechol
-
-
?
4-nitrocatechol + O2
2-hydroxy-4-nitromuconate semialdehyde
show the reaction diagram
P06622
-
-
-
?
4-nitrocatechol + O2
2-hydroxy-4-nitromuconate semialdehyde
show the reaction diagram
-, Q8KLV4
rapid inactivation of enzyme during turnover
-
-
?
alkylcatechol + O2
?
show the reaction diagram
Q83U22
degradation of aromatic compounds
-
-
?
butanol + O2
?
show the reaction diagram
-
-
-
-
?
catechol + O2
?
show the reaction diagram
Pseudomonas sp., Pseudomonas sp. CGMCC2953
-
assay at pH 7.5, 30C
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
-
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
-
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
-
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
-
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
-
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
-
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
Q83U22
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
-
-
-
-
-
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
-
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
-
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
-
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
-
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
P06622
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
-
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
-
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
-
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
-
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
-
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
-
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
-
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
-
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
Q7BH44
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
Pseudomonas putida mt-2
P23103
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
Pseudomonas putida mt-2
-
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
-, Q8KLV4
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
Q97YT4, -
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
Q52264, Q9Z417
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
Q842G7
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
P06622
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
C3W4L8, C3W4L9, C3W4M0, C3W4M1, C3W4M2, C3W4M3, C3W4M4, C3W4M5, C3W4M6, C3W4M7
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
P17262
poor substrate
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
-
poor substrate
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
-, Q8KLV4
most effective substrate
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
-
highly specific for
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
-
highly specific for
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
-
highly specific for
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
-
highly specific for
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
-
highly specific for
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
-
hypoxic strains have enzymes with significantly higher affinities for catechol than for nonhypoxic strains
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
Q52264, Q9Z417
best substrates
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
-
metacleavage enzyme of catechol metabolism
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
Pseudomonas putida mt-2
-
key role in the degradation of aromatic molecules
-
-
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
cleavage of aromatic compounds, involved in alpha-ketoadiapate pathway
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
Q83U22
degradation of aromatic compounds
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
P06622
degradation of aromatic compounds
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
-
degradation of aromatic compounds, involved in toluene and ortho-xylene metabolism
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
-
involved in biodegradation of benzothiazoles
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
P17262
involved in metabolism of aromatic compounds
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
-
key enzyme for the degradation of aromatic compounds
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
-
enzyme is induced by benzenesulfonate, catechol or toluene p-sulfonate
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
-
catechol 2,3-dioxygenase is involved in the meta phenol degradation pathway
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
Q97YT4, -
and 4-chlorocatechol, best substrates
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
-
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
show the reaction diagram
-
benzoate degadation pathway
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
-
extradiol dioxygenase reaction
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
V5W6K5
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, the enzyme shows the highest activity against catechol and 4-chlorocatechol
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
-
poor substrate, degradation of aromatic compounds, involved in toluene and ortho-xylene metabolism
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
Pseudomonas putida T-2
-
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
Pseudomonas putida MT4
Q842G7
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
Pseudomonas putida KT 2440
-
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
Bacillus subtilis 168
-
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
Pseudomonas putida UWC1-pQM899
-
highly specific for
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
Escherichia coli JM83
-
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
-
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
show the reaction diagram
Pseudomonas sp. OC1
-
highly specific for
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
Pseudomonas putida UCC2
Q52264
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
Geobacillus thermoleovorans A2
-
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
Pseudomonas fluorescens CFS 215
-
hypoxic strains have enzymes with significantly higher affinities for catechol than for nonhypoxic strains, 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
show the reaction diagram
Rhodococcus pyridinivorans PA
-
involved in biodegradation of benzothiazoles
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
Pseudomonas putida SH1
P06622
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
Pseudomonas stutzeri OX1
-
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
Pseudomonas stutzeri OX1
Q8KLV4
-, most effective substrate
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
Rhodococcus rhodochrous CTM
-
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
Ralstonia pickettii PK01
-
hypoxic strains have enzymes with significantly higher affinities for catechol than for nonhypoxic strains, 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
show the reaction diagram
Pseudomonas putida GJ31
-
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
Pseudomonas putida GJ31
Q9Z417
best substrates
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
Pseudomonas putida PpG 1064
-
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
-
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
Burkholderia cepacia G4
-
-, hypoxic strains have enzymes with significantly higher affinities for catechol than for nonhypoxic strains
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
-
-, cleavage of aromatic compounds, involved in alpha-ketoadiapate pathway
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
Pseudomonas sp. W31
-
hypoxic strains have enzymes with significantly higher affinities for catechol than for nonhypoxic strains, 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
show the reaction diagram
Alcaligenes sp. 0-1
-
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
-
catechol 2,3-dioxygenase is involved in the meta phenol degradation pathway
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
-
highly specific for
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
Pseudomonas putida PaW94
-
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
Cupriavidus necator 335
-
highly specific for
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
Q97YT4, -
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
Q97YT4, -
and 4-chlorocatechol, best substrates
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
V5W6K5
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, the enzyme shows the highest activity against catechol and 4-chlorocatechol
-
-
?
catechol + O2
2-hydroxymuconic semialdehyde
show the reaction diagram
Stenotrophomonas maltophilia, Stenotrophomonas maltophilia KB2
-
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
show the reaction diagram
-
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
show the reaction diagram
-
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
show the reaction diagram
Planococcus sp.
-
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
show the reaction diagram
-
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
show the reaction diagram
Q97YT4, -
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
show the reaction diagram
Variovorax sp.
-
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
show the reaction diagram
Planococcus sp.
E7DDG2
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
show the reaction diagram
Q34135
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
show the reaction diagram
A7LB47
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
show the reaction diagram
Q97YT4, -
the enzyme is constitutively transcribed
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
show the reaction diagram
-
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
show the reaction diagram
Ochrobactrum sp. CH-19, Staphylococcus sp. KW-07
-
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
show the reaction diagram
Q97YT4
-, the enzyme is constitutively transcribed
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
show the reaction diagram
Stenotrophomonas maltophilia KB2
A7LB47
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
show the reaction diagram
-
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
show the reaction diagram
E7DDG2
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
show the reaction diagram
Q34135
-
-
-
?
ethanol + O2
?
show the reaction diagram
-
-
-
-
?
hydroquinone + O2
?
show the reaction diagram
Stenotrophomonas maltophilia, Stenotrophomonas maltophilia KB2
-
immobilized enzyme, no activity with the free enzyme
-
-
?
phenol + O2
?
show the reaction diagram
Variovorax sp.
-
-
-
-
?
phenol + O2
?
show the reaction diagram
Planococcus sp.
E7DDG2
-
-
-
?
phenol + O2
?
show the reaction diagram
Variovorax sp.
-
activity in cadmium-induced cells
-
-
?
phenol + O2
?
show the reaction diagram
-
-, activity in cadmium-induced cells
-
-
?
phenol + O2
?
show the reaction diagram
E7DDG2
-
-
-
?
phenol + O2
2-hydroxymuconic semialdehyde
show the reaction diagram
Alcaligenes faecalis, Alcaligenes faecalis IS-46
A5HMH3
utilize phenol as sole carbon and energy source, concentration of phenol diversify from 25 mg/l to 1000 mg/l, assay at 28C, pH 6.8-7.0
-
-
?
propanol + O2
?
show the reaction diagram
-
-
-
-
?
protocatechualdehyde + O2
?
show the reaction diagram
-
-
-
-
?
protocatechualdehyde + O2
?
show the reaction diagram
-
weak
-
-
?
protocatechuate + O2
?
show the reaction diagram
-
-
-
-
?
tetrachlorohydroquinone + O2
?
show the reaction diagram
-
immobilized enzyme, no activity with the free enzyme
-
-
?
methanol + O2
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
P06622
no cleavage of 4-carboxycatechol, 4-carboxymethylcatechol and 4-tert-butylcatechol
-
-
-
additional information
?
-
Pseudomonas putida, Pseudomonas putida MT4
Q842G7
no activity with 4-tert-butylcatechol
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2,4-dichlorophenol + O2
?
show the reaction diagram
Stenotrophomonas maltophilia, Stenotrophomonas maltophilia KB2
-
-
-
-
?
2-chlorophenol + O2
?
show the reaction diagram
Stenotrophomonas maltophilia, Stenotrophomonas maltophilia KB2
-
-
-
-
?
2-methylphenol + O2
?
show the reaction diagram
Stenotrophomonas maltophilia, Stenotrophomonas maltophilia KB2
A7LB47
-
-
-
?
3-methylphenol + O2
?
show the reaction diagram
Stenotrophomonas maltophilia, Stenotrophomonas maltophilia KB2
A7LB47
-
-
-
?
4-alkylcatechol + O2
?
show the reaction diagram
P17262
initial step of long-chain alkylphenol cleavage pathway
-
-
?
4-Methylphenol + O2
?
show the reaction diagram
Stenotrophomonas maltophilia, Stenotrophomonas maltophilia KB2
A7LB47
-
-
-
?
alkylcatechol + O2
?
show the reaction diagram
Q83U22
degradation of aromatic compounds
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
-
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
-
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
-
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
-
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
-, Q8KLV4
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
C3W4L8, C3W4L9, C3W4M0, C3W4M1, C3W4M2, C3W4M3, C3W4M4, C3W4M5, C3W4M6, C3W4M7
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
-
metacleavage enzyme of catechol metabolism
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
Pseudomonas putida mt-2
-
key role in the degradation of aromatic molecules
-
-
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
cleavage of aromatic compounds, involved in alpha-ketoadiapate pathway
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
Q83U22
degradation of aromatic compounds
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
P06622
degradation of aromatic compounds
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
-
degradation of aromatic compounds, involved in toluene and ortho-xylene metabolism
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
-
involved in biodegradation of benzothiazoles
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
P17262
involved in metabolism of aromatic compounds
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
-
key enzyme for the degradation of aromatic compounds
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
-
enzyme is induced by benzenesulfonate, catechol or toluene p-sulfonate
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
-
catechol 2,3-dioxygenase is involved in the meta phenol degradation pathway
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
-
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
show the reaction diagram
-
benzoate degadation pathway
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
V5W6K5
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-6-semialdehyde
show the reaction diagram
-
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
show the reaction diagram
Planococcus sp.
-
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
show the reaction diagram
-
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
show the reaction diagram
Variovorax sp.
-
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
show the reaction diagram
Planococcus sp.
E7DDG2
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
show the reaction diagram
Q34135
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
show the reaction diagram
A7LB47
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
show the reaction diagram
Q97YT4, -
the enzyme is constitutively transcribed
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
-
degradation of aromatic compounds, involved in toluene and ortho-xylene metabolism
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
-
catechol 2,3-dioxygenase is a critical enzyme in the multistep biodegradation of 3,4-dichloroaniline by Pseudomonas sp. KB35B
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
show the reaction diagram
-
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
show the reaction diagram
Ochrobactrum sp. CH-19
-
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
Pseudomonas fluorescens CFS 215
-
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
show the reaction diagram
Rhodococcus pyridinivorans PA
-
involved in biodegradation of benzothiazoles
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
Pseudomonas stutzeri OX1
-
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
Pseudomonas stutzeri OX1
Q8KLV4
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
Ralstonia pickettii PK01
-
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
show the reaction diagram
Burkholderia cepacia G4
-
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
-
cleavage of aromatic compounds, involved in alpha-ketoadiapate pathway
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
Pseudomonas sp. W31
-
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-6-semialdehyde
show the reaction diagram
-
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
-
catechol 2,3-dioxygenase is involved in the meta phenol degradation pathway
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
show the reaction diagram
Q97YT4
the enzyme is constitutively transcribed
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
show the reaction diagram
Stenotrophomonas maltophilia KB2
A7LB47
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
show the reaction diagram
-
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
show the reaction diagram
E7DDG2
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
show the reaction diagram
Q34135
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
show the reaction diagram
V5W6K5
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
-
-
?
phenol + O2
?
show the reaction diagram
Variovorax sp., Variovorax sp. 12S
-
activity in cadmium-induced cells
-
-
?
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Fe2+
-
1 atom of iron per molecule
Fe2+
-
active site Fe2+
Fe2+
-
1 atom of iron per molecule
Fe2+
-
FeCl2 and FeSO4 activate metapyrocatechase 2, no effect on metapyrocatechase 1
Fe2+
-
3 gatom of iron per mol of enzyme; activity is closely related to specific content of iron in this protein
Fe2+
Pseudomonas putida mt-2
-
4 gatom of iron per mol of enzyme
Fe2+
-
one atom of iron per monomer of the wild-type enzyme
Fe2+
-
0.6 mol of iron per mol of protein
Fe2+
-
one iron per enzyme subunit, AAS, iron is tightly bound
Fe2+
Pseudomonas putida mt-2
-
the active site comprises three Fe2+ ligands His153, His214 and Glu265
Fe2+
-
3.7 mol of iron per mol of enzyme or 0.93 mol per mol of the subunit
Fe2+
-
the activity loss following H2O2 treatment is directly correlated with nearly stoichiometric titration of the active site Fe2+
Fe2+
-
enzyme might undergo oxidation of its active-site ferrous iron atom
Fe2+
-
incubation of the purified enzyme (PheB) with Fe2+ and ascorbate increases its activity by approximately sevenfold
Fe2+
P06622
the enzyme contains Fe2+ as a cofactor
Fe2+
A7LB47
Fe2 ion binding is facilitated via four ligands: two histidine residues, one glutamate residue and one molecule of water, overview
Fe2+
Q97YT4, -
the enzyme contains about 2 mol of Fe2+ per mole of protein
Iron
-
bound to protein
K+
-
included in assay medium
additional information
-
not: Co2+, Mn2+, Cu2+, Cr3+, Zn2+, Ni2+, Cd2+, Ca2+
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
(1R,2R)-trans-1,2-cyclohexanediol
-
-
(1S,2S)-trans-1,2-cyclohexanediol
-
-
1-naphthoquinoline
-
-
2-chlorophenol
Pseudomonas putida mt-2
-
-
2-chlorophenol
-
-
2-hydroxyacetophenone
-
-
2-hydroxybenzyl alkohol
-
-
2-methoxyphenol
-
-
3-chlorocatechol
-
-
3-chlorocatechol
Pseudomonas putida mt-2
-
in the presence of O2
3-fluorocatechol
Pseudomonas putida mt-2
-
in the presence of O2
3-Methylcatechol
-
suicide inhibition
3-vinylcatechol
-
C23O activity (TodE) is almost completely abrogated by exposure to 0.2 mM 3-vinylcatechol
-
4-Chlorocatechol
-
-
4-Chlorocatechol
Pseudomonas putida mt-2
-
-
4-Methyl-2-nitrophenol
-
-
4-Methylcatechol
-
suicide inhibition
4-Methylcatechol
-
-
8-hydroxyquinoline
-
weak
benzyl alkohol
-
-
catechol
-
suicide inhibition
catechol
-
wild-type enzyme: substrate inhibition. Mutant enzyme E286K: no substrate inhibition
Cd2+
Variovorax sp.
-
minimal inhibitory concentrations cadmium to Variovorax sp. 12S strain in different media, overview
CuSO4
-
the immobilized enzyme is less sensitive compared to the free enzyme
diethyldicarbonate
-
-
H2O2
Q8KLV4
partially reversible by addition of Fe(NH4)2(SO4)2
H2O2
Variovorax sp.
-
inactivation at 5%
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
hydrogen peroxide
Q97YT4, -
0.1 M, complete inactivation
m-fluorophenol
-
-
m-Hydroxybenzoate
-
-
m-Nitrophenol
-
-
m-phenanthroline
-
-
NaN3
-
the immobilized enzyme is less sensitive compared to the free enzyme
o-aminophenol
-
-
o-fluorophenol
-
-
o-phenanthroline
-
weak
o-phenanthroline
-
-
o-phenanthroline
-
-
o-phenanthroline
-
not
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
not
p-fluorophenol
-
-
p-nitrophenol
-
-
Tiron
Pseudomonas putida mt-2
-
weak, in the absence of O2
monoiodoacetate
-
weak
additional information
Q97YT4, -
not inhibitory: EDTA, o-phenanthroline, 2,2'-dipyridyl
-
additional information
-
C23O activity (TodE) is unaffected by styrene, toluene, and 3-methylcatechol
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
ascorbate
-
incubation of the purified enzyme (PheB) with Fe2+ and ascorbate increases its activity by approximately sevenfold
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.00187
-
3,5-dichlorocatechol
-
-
0.0055
-
3,5-dimethylcatechol
-
mutant T249A
0.0074
-
3,5-dimethylcatechol
-
mutant T249G
0.0097
-
3,5-dimethylcatechol
-
mutant T249S
0.0215
-
3,5-dimethylcatechol
-
wildtype
0.0237
-
3,5-dimethylcatechol
-
mutant T249G
0.0381
-
3,5-dimethylcatechol
-
mutant T249A
0.0575
-
3,5-dimethylcatechol
-
mutant T249S
0.0738
-
3,5-dimethylcatechol
-
wildtype
0.00204
-
3-methoxycatechol
-
-
0.001
-
3-Methylcatechol
-
-
0.0015
-
3-Methylcatechol
Q83U22
strain 1YB2, pH 7.5, 25C
0.00164
-
3-Methylcatechol
-
-
0.0017
-
3-Methylcatechol
Q97YT4, -
pH 7.5,25 C
0.0018
-
3-Methylcatechol
-
-
0.0024
-
3-Methylcatechol
-
-
0.0032
-
3-Methylcatechol
Q83U22
strain 1YdBTEX2, pH 7.5, 25C
0.0036
-
3-Methylcatechol
Q97YT4, -
pH 7.5, 60C
0.0038
-
3-Methylcatechol
-
wildtype
0.01
-
3-Methylcatechol
-
metapyrocatechase 2
0.0106
-
3-Methylcatechol
-
-
0.0115
-
3-Methylcatechol
-
mutant T249S
0.0143
-
3-Methylcatechol
-
mutant T249A
0.0266
-
3-Methylcatechol
-
mutant T249G
0.06
-
3-Methylcatechol
-
metapyrocatechase 1
0.0009
-
4-Chlorocatechol
Q83U22
strain 1YB2, pH 7.5, 25C
0.00102
-
4-Chlorocatechol
-
-
0.0016
-
4-Chlorocatechol
Q83U22
strain 1YdBTEX2, pH 7.5, 25C
0.0625
-
4-Fluorocatechol
-
-
0.00129
-
4-Methylcatechol
-
-
0.0017
-
4-Methylcatechol
-
-
0.0019
-
4-Methylcatechol
Q83U22
strain 1YB2, pH 7.5, 25C
0.0025
-
4-Methylcatechol
-
pH 8.0, 35C, immobilized enzyme
0.003
-
4-Methylcatechol
Q97YT4, -
pH 7.5, 25C
0.0052
-
4-Methylcatechol
Q83U22
strain 1YdBTEX2, pH 7.5, 25C
0.006
-
4-Methylcatechol
-
-
0.008
-
4-Methylcatechol
-
metapyrocatechase 2
0.0084
-
4-Methylcatechol
Q842G7
25C, pH 7.2
0.0109
-
4-Methylcatechol
-
-
0.012
-
4-Methylcatechol
Q97YT4, -
pH 7.5, 60C
0.02
-
4-Methylcatechol
-
metapyrocatechase 1
0.0425
-
4-Methylcatechol
-
pH 8.0, 35C, free enzyme
0.05
-
4-Methylcatechol
-
-
1.1
-
4-Methylcatechol
-
-
0.0065
-
4-n-butylcatechol
Q842G7
25C, pH 7.2
0.001
-
catechol
-
wildtype
0.0011
-
catechol
Q83U22
strain 1YB2, pH 7.5, 25C
0.0014
-
catechol
-
-
0.00147
-
catechol
-
25C, pH 7.2, wild-type enzyme
0.0015
-
catechol
Q8KLV4
wild type enzyme, pH 7.5, 25C
0.0016
-
catechol
Q97YT4, -
pH 7.5, 25C
0.00187
-
catechol
-
-
0.002
-
catechol
-
metapyrocatechase 2
0.00248
-
catechol
-
25C, pH 7.2, mutant enzyme E286K
0.0025
-
catechol
-
-
0.0025
-
catechol
Q83U22
strain 1YdBTEX2, pH 7.5, 25C
0.0029
-
catechol
-
native enzyme, pH 7.5, 25C
0.0038
-
catechol
-
native enzyme, pH 7.5, 25C
0.0039
-
catechol
-
-
0.004
-
catechol
-
-
0.0041
-
catechol
-
metapyrocatechase 1
0.005
-
catechol
Q8KLV4
Y255F mutant enzyme, pH 7.5, 25C
0.0059
-
catechol
Q97YT4, -
pH 7.5, 60C
0.01
-
catechol
-
wild type C23O
0.011
-
catechol
-
57C
0.015
-
catechol
-
-
0.02
-
catechol
-
hybrid enzyme, pH 7.5, 25C
0.022
-
catechol
-
-
0.0225
-
catechol
-
mutant T249S
0.0234
-
catechol
Q842G7
25C, pH 7.2
0.037
-
catechol
-
mutant T249A
0.037
-
catechol
Planococcus sp.
-
pH 5.0, 35C, mutant R296Q
0.04
-
catechol
-
mutated C23O: A229C, H294C
0.04
-
catechol
Planococcus sp.
-
pH 7.0, 35C, mutant A23T/F212S
0.053
-
catechol
Planococcus sp.
-
pH 7.0, 35C, mutant H24R/F168S/Q275R
0.0636
-
catechol
-
mutant T249G
0.09
-
catechol
Planococcus sp.
-
pH 7.0, 35C, wild-type enzyme
0.434
-
catechol
Q8KLV4
H199N mutant enzyme, pH 7.5, 25C
0.007
-
O2
Pseudomonas putida mt-2
-
-
0.063
-
O2
-
immobilized enzyme
0.0427
-
Phenol
Planococcus sp.
E7DDG2
pH 7.5, 40C
0.0228
-
Protocatechualdehyde
-
-
0.714
-
catechol
Q8KLV4
H246N mutant enzyme, pH 7.5, 25C
additional information
-
additional information
-
Km of wild-type and hybride enzymes
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
Pseudomonas putida mt-2
-
-
-
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
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.23
-
3,5-dimethylcatechol
-
mutant T249G
0.36
-
3,5-dimethylcatechol
-
wildtype
0.4
-
3,5-dimethylcatechol
-
mutant T249A; mutant T249G
0.66
-
3,5-dimethylcatechol
-
wildtype
1
-
3,5-dimethylcatechol
-
mutant T249A
1.2
-
3,5-dimethylcatechol
-
mutant T249S
2.65
-
3,5-dimethylcatechol
-
mutant T249S
0.58
-
3-Methylcatechol
Q97YT4, -
pH 7.5,25 C
2.6
-
3-Methylcatechol
-
mutant T249G
5.2
-
3-Methylcatechol
Q97YT4, -
pH 7.5, 60C
6.3
-
3-Methylcatechol
-
mutant T249A
17
-
3-Methylcatechol
Q83U22
strain 1YB2, pH 7.5, 25C
25
-
3-Methylcatechol
Q83U22
strain 1YdBTEX2, pH 7.5, 25C
60.5
-
3-Methylcatechol
-
mutant T249S
118
-
3-Methylcatechol
-
wildtype
190
-
3-Methylcatechol
-
-
490
-
3-Methylcatechol
-
-
17
-
4-Chlorocatechol
Q83U22
strain 1YB2, pH 7.5, 25C
45
-
4-Chlorocatechol
Q83U22
strain 1YdBTEX2, pH 7.5, 25C
0.76
-
4-Methylcatechol
Q97YT4, -
pH 7.5, 25C
4.7
-
4-Methylcatechol
Q97YT4, -
pH 7.5, 60C
53
-
4-Methylcatechol
Q83U22
strain 1YB2, pH 7.5, 25C
64
-
4-Methylcatechol
Q83U22
strain 1YdBTEX2, pH 7.5, 25C
930
-
4-Methylcatechol
-
-
0.46
-
catechol
Q8KLV4
H199N mutant enzyme, pH 7.5, 25C
0.8
-
catechol
-
mutant T249G
1.3
-
catechol
-
mutant T249A
1.3
-
catechol
Q97YT4, -
pH 7.5, 25C
1.6
-
catechol
Q8KLV4
H246N mutant enzyme, pH 7.5, 25C
7.5
-
catechol
-
mutant T249S
7.8
-
catechol
Q97YT4, -
pH 7.5, 60C
8.8
-
catechol
Q8KLV4
Y255F mutant enzyme, pH 7.5, 25C
31.3
-
catechol
-
25C, pH 7.2, wild-type enzyme
34.7
-
catechol
-
25C, pH 7.2, mutant enzyme E286K
38
-
catechol
Q83U22
strain 1YB2, pH 7.5, 25C
128
-
catechol
Q83U22
strain 1YdBTEX2, pH 7.5, 25C
148
-
catechol
-
hybrid enzyme, pH 7.5, 25C
180
-
catechol
-
wildtype
200
-
catechol
Q8KLV4
wild type enzyme, pH 7.5, 25C
238
-
catechol
-
native enzyme, pH 7.5, 25C
493
-
catechol
-
native enzyme, pH 7.5, 25C
690
-
catechol
-
-
930
-
catechol
-
-
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
-
the hypoxic strains have enzymes with significantly higher substrate turnover rates for the nonhypoxic strains
-
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
340
-
3-Methylcatechol
Q97YT4, -
pH 7.5,25 C
3927
1400
-
3-Methylcatechol
Q97YT4, -
pH 7.5, 60C
3927
250
-
4-Methylcatechol
Q97YT4, -
pH 7.5, 25C
4659
400
-
4-Methylcatechol
Q97YT4, -
pH 7.5, 60C
4659
810
-
catechol
Q97YT4, -
pH 7.5, 25C
8337
1300
-
catechol
Q97YT4, -
pH 7.5, 60C
8337
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
34
-
(1R,2R)-trans-1,2-cyclohexanediol
-
-
43
-
(1S,2S)-trans-1,2-cyclohexanediol
-
-
0.00056
-
1-naphthoquinoline
-
-
0.35
-
2-butanone
-
-
0.52
-
2-chlorophenol
-
-
0.56
-
2-Fluorophenol
-
-
0.23
-
2-hydroxyacetophenone
-
-
5.3
-
2-hydroxybenzyl alkohol
-
-
0.23
-
2-methoxyphenol
-
-
0.15
-
2-Pentanone
-
-
0.014
-
3-chlorocatechol
-
-
0.023
-
3-chlorocatechol
Pseudomonas putida mt-2
-
-
3
-
3-Pentanone
-
-
0.017
-
4-Chlorocatechol
Pseudomonas putida mt-2
-
in the presence of mercaptoethanol
0.05
-
4-Chlorocatechol
-
-
0.126
-
4-Methyl-2-nitrophenol
-
-
0.21
-
acetophenone
-
-
4.9
-
Benzoate
-
-
1.4
-
benzyl alkohol
-
-
147
-
ethanol
-
-
90
-
i-Propanol
-
-
0.311
-
m-fluorophenol
-
-
14.7
-
m-Hydroxybenzoate
-
-
0.042
-
m-Nitrophenol
-
-
480
-
methanol
-
-
1.7
-
n-butanol
-
-
0.58
-
n-Pentanol
-
-
21
-
n-Propanol
-
-
0.205
-
nitrobenzene
-
-
0.0049
-
o-aminophenol
-
-
0.056
-
o-fluorophenol
-
-
0.0093
-
o-Nitrophenol
-
-
0.452
-
p-fluorophenol
-
-
0.111
-
p-nitrophenol
-
-
5.2
-
salicylate
-
-
720
-
t-butanol
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.00887
-
Planococcus sp.
-
pH 7.0, 35C, mutant H24R/F168S/Q275R
0.01
-
-
inductor 3,4-dihydroxybenzoic acid, cell-free extract from Stenotrophomonas maltophilia
0.01285
-
Planococcus sp.
-
pH 7.0, 35C, mutant A23T/F212S
0.018
-
-
Intracellular enzyme activity of C23D in crude lysate
0.01973
-
Planococcus sp.
-
pH 7.0, 35C, wild-type enzyme
0.02
-
-
inductor benzoic acid, cell-free extract from Stenotrophomonas maltophilia
0.03187
-
Planococcus sp.
-
pH 5.0, 35C, mutant R296Q
0.04
-
-
inductor vanillic acid, cell-free extract from Stenotrophomonas maltophilia
0.054
-
-
Activity is measured by following the formation of 2-hydroxymuconic semialdehyde spectrophotometrically at 375 nm
0.37
-
-
inductor catechol, cell-free extract from Stenotrophomonas maltophilia
4.92
-
-
inductor phenol, cell-free extract from Stenotrophomonas maltophilia
6.9
-
-
crude extracts of Pseudomonas putida
9.7
-
Q842G7
-
10
-
P17262
with 2,3-dihydroxybiphenyl, pH 7.5, 28C
15
-
P06622
crude extract, in 20 mM NaH2PO4, pH 7.5, containing 1 mM catechol at 50C
20
-
P17262
with catechol, pH 7.5, 28C
20
-
-
activity is measured following the formation of 2-hydroxymuconate semialdehyde at 375 nm and 25C.
35
-
-
metapyrocatechase 2
46
-
-
immobilized enzyme
60.3
-
-
crude extracts of Escherichia coli
68
-
P17262
with 3-methylcatechol, pH 7.5, 28C
90
-
-
metapyrocatechase 1
113.8
-
-
-
270
-
-
free enzyme
300
-
-
highest specific activity at arount 40C for both wild-type and mutated C23O
320
-
Pseudomonas putida mt-2
-
-
320
-
P17262
with 4-ethylcatechol, pH 7.5, 28C
355.8
-
-
substrate 4-methylcatechol, pH 8.0, 35C, free enzyme
400
-
-
wild-type enzyme
536
-
-
crystallized enzyme
593
-
P17262
with 4-methylcatechol, pH 7.5, 28C
802
-
P06622
after 52.7fold purification, in 20 mM NaH2PO4, pH 7.5, containing 1 mM catechol at 50C
936.3
-
-
substrate 4-methylcatechol, pH 8.0, 35C, immobilized enzyme
additional information
-
-
-
additional information
-
-
comparison of wild-type and mutant enzymes
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
0.4 U/mg, purified enzyme
additional information
-
-
pDTG912 and pDTG901 are deletion derivatives of the cosmid pDTG900. pDTG912/A and pDTG912/B are subclones of pDTG912 in pK18. Activity of the enzyme related to pDTG912 = 0.012 micromol/min/mg, activity of the enzyme related to pDTG901 = 0.56 micromol/min/mg, no detectable activity of the enzyme related to pDTG912/A, no detactable activity of the enzyme related to pDTG912/B
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5
-
Planococcus sp.
-
mutant R296Q
6
-
Q8KLV4
rapid loss of activity below pH 6, very slow decrease of activity above pH 6
6.5
8.5
P06622
depending on the substrate
6.5
-
Pseudomonas putida mt-2
-
-
6.5
-
Planococcus sp.
-
mutants A23T/F212S and H24R/F168S/Q275R
7
7.5
Q97YT4, -
-
7
-
-
maximum extradiol product formation
7
-
Planococcus sp.
-
wild-type enzyme
7.2
7.5
Variovorax sp.
-
assay at
7.5
8
P06622
-
7.5
-
-
assay at
7.5
-
-
assay at
7.5
-
Q97YT4, -
assay at
8
-
Planococcus sp.
E7DDG2
-
8
-
-
both free and the immobilized enzyme
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4
9
Q97YT4, -
pH 4.0: 29% of maximal activity, pH 6.5: about 50% of maximal activity, pH 9.0: 61% of maximal activity
5.2
8.6
-
-
5.5
9.5
-
wild-type C23O only 50% residue activity at pH 9.5, mutated C23O still 75% residue activity at pH 9.5
6.8
7
A5HMH3
-
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
24
-
-
assay at
28
-
A5HMH3
assay at
30
-
Variovorax sp.
-
assay at
35
-
Planococcus sp.
-
wild-type and mutant enzymes
50
-
P06622
-
60
-
Planococcus sp.
E7DDG2
-
70
80
Q97YT4, -
-
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
80
P06622
the enzyme activity increases starting from 25C and reaches its maximum at 50C, the enzyme starts to denature at 55C and the structure is destroyed by the time the temperature reaches 80C
30
70
-
wild-type C23O only 45% residue activity at 50C, mutated C23O still 90% residue activity at 50C
50
80
Q97YT4, -
50C: about 50% of maximal activity, 70-80C: maximal activity
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5
-
-
isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
strain P8, ATCC 49451
Manually annotated by BRENDA team
-
monocyclic hydrocarbons, phenol, catechol, benzoic acid, protocatechuic acid and vanillic acid
Manually annotated by BRENDA team
Stenotrophomonas maltophilia KB2
-
monocyclic hydrocarbons, phenol, catechol, benzoic acid, protocatechuic acid and vanillic acid
-
Manually annotated by BRENDA team
Pseudomonas putida SH1
-
-
-
Manually annotated by BRENDA team
Planococcus sp.
E7DDG2
-
Manually annotated by BRENDA team
additional information
-
optimal growth at pH 7.0 and 25C
Manually annotated by BRENDA team
additional information
Q34135
optimal growth at pH 7.0 and 25C
Manually annotated by BRENDA team
additional information
-
optimal growth at pH 7.0 and 25C
Manually annotated by BRENDA team
additional information
-
optimal growth at pH 7.0 and 25C
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
32000
-
-
Tricine SDS-PAGE
35000
-
Q8KLV4
SDS-PAGE
35000
-
Q83U22
SDS-PAGE
35100
-
Q8KLV4
calculated from deduced amino acid sequence
35110
-
Q8KLV4
mass sprectrometry
36000
-
-
SDS-PAGE
110000
-
-
gel filtration
116000
-
-
gel filtration
117000
-
Q8KLV4
gel filtration
128000
-
P06622
gel filtration
132000
134000
-
gel filtration, sedimentation equilibrium analysis, amino acid analysis, metapyrocatechase 2
135000
-
-
gel filtration
136000
144000
-
light scattering method
140000
-
-
sedimentation and diffusion data
140000
-
-
gel filtration
140000
-
Pseudomonas putida mt-2
-
sedimentation equilibrium analysis
143000
144600
-
gel filtration, sedimentation equilibrium analysis, amino acid analysis
147000
-
-
gel filtration
150000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
Q842G7
x * 31000, SDS-PAGE
?
Pseudomonas putida MT4
-
x * 31000, SDS-PAGE
-
homotetramer
Pseudomonas putida mt-2
-
with each subunit folded into two similar domains
homotetramer
-
4 * 35000, SDS-PAGE, 4 * 35195, MS, 4 * 35156 based on DNA sequence
homotetramer
P06622
4 * 39000, SDS-PAGE
polymer
-
x * 34000
polymer
Cupriavidus necator 335
-
x * 34000
-
tetramer
-
4 * 33500 metapyrocatechase 1, SDS-PAGE; 4 * 36000, metapyrocatechase 2, SDS-PAGE
tetramer
Pseudomonas putida mt-2
-
4 * 35000 SDS-PAGE
tetramer
-
four subunits arranged in a tetrahedral conformation
tetramer
-
4 * 35000, SDS-PAGE
tetramer
-
4 * 33000
tetramer
-
4 * 34700, SDS-PAGE
tetramer
-
4 * 37000, SDS-PAGE
tetramer
-
four identical subunits, crystal structure analysis
tetramer
P06622
-
tetramer
Q8KLV4
4 * 35000, SDS-PAGE, mass spectrometry
tetramer
-
4 * 35000, SDS-PAGE
tetramer
-
4 * 35000, SDS-PAGE
-
tetramer
Geobacillus thermoleovorans A2
-
4 * 34700, SDS-PAGE
-
tetramer
-
4 * 35000, SDS-PAGE
-
tetramer
Pseudomonas stutzeri OX1
-
4 * 35000, SDS-PAGE, mass spectrometry
-
trimer
-
3 * 31000, SDS-PAGE
homotetramer
Pseudomonas putida SH1
-
4 * 39000, SDS-PAGE
-
additional information
-
The space group of the crystal is found to be P212121, with unit-cell parameters a = 65.5, b = 119.2, c = 158.7 A, assuming the presence of one tetramer in the asymmetric unit
additional information
-
interaction of inactive enzyme with soluble [2Fe-2S] ferredoxin protein XylT for reactivation through reduction of the iron atom in the active site of the enzyme
additional information
A7LB47
the secondary structure shows presence of externally located alpha-helices and internally located beta-sheets, enzyme molecular modeling, overview
additional information
Geobacillus stearothermophilus BR219
-
The space group of the crystal is found to be P212121, with unit-cell parameters a = 65.5, b = 119.2, c = 158.7 A, assuming the presence of one tetramer in the asymmetric unit
-
additional information
Pseudomonas putida mt2
-
interaction of inactive enzyme with soluble [2Fe-2S] ferredoxin protein XylT for reactivation through reduction of the iron atom in the active site of the enzyme
-
additional information
Stenotrophomonas maltophilia KB2
-
the secondary structure shows presence of externally located alpha-helices and internally located beta-sheets, enzyme molecular modeling, overview
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Crystallization of the iron incubated PheB enzyme. Hanging-drop vapour diffusion method with best crystals after 7 d at 285 K using 0.2 M Li2SO4, 15% PEG 4000 and 0.1 M HEPES pH 7.0 in the reservoir and protein solution with a concentration of 40 mg/ml. The crystal diffracts to 2.3 A resolution
-
-
Pseudomonas putida mt-2
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
-
Q8KLV4
rapid loss of activity below pH 6
7.5
8
-
highest stability
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
50
-
38% relative activity of the wild-type enzyme after 1200 min at 30C, 45% relative activity of mutated enzymes after 1200 min at 30C, 44% relative activity of wild-type enzyme after 80 min at 50C, 52% relative activity of mutated enzyme after 80 min at 50C
30
50
P06622
the half-life of the enzyme activity at 30C is about 7 h and the half-life of the enzyme activity at 50C is 45 min
35
40
A7LB47
rapid decline in activity
35
-
A7LB47
loss of 17.4% activity
45
-
-
20 min, stable
50
-
-
17 min, stable
50
-
Planococcus sp.
E7DDG2
loss of 30% activity after 20 min
55
-
-
5 min, stable
57
-
-
63% loss of activity within 10 min
60
-
-
immediate loss of activity
60
-
Planococcus sp.
E7DDG2
half-life is 10 min
60
-
Q97YT4, -
half-life: 230-240 min
70
-
-
10 min, activity not decreased in the presence of 5% acetone
70
-
-
10 min, 50% loss of original activity under nitrogen atmosphere; 1.5 min, 50% loss of original activity under aerobic conditions
70
-
Q97YT4, -
half-life: 100-110 min
75
-
-
40% loss of original activity
80
-
Q97YT4, -
half-life: about 20 min
85
-
Q4J6K0
the structure of thermophilic C23O remains unchanged up to temperatures of 85C
additional information
-
Q4J6K0
the observed stability of the enzyme can be explained by the presence of a set of residues surrounding the active center of the enzyme. The solution scattering of the enzyme at temperatures between 4 and 85C ideally fits the calculated scattering from the single crystal structure
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
molarity of buffer beyond 0.04 M not suitable
-
25C, half-life of 69 min in air, 37C, half-life of 70 min in argon
-
acetone protects against inactivation by air, concentration of 10%
-
ethanol protects against inactivation by air
-
immobilization enhances stability against inactivation by heat, acid or alkaline pH and various denaturing agents
-
acetone protects against inactivation by air, concentration of 10%
-
the purified enzyme is unstable losing the activity completely at 8 C within 3 days
-
ORGANIC SOLVENT
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
2-mercaptoethanol
-
no significant protection of the enzyme from inactivation
Acetone
-
protects enzyme almost completely from inactivation by air
Ethanol
-
protects enzyme almost completly from inactivation by air
additional information
-
Tris-HCl, inhibitory effect on the activity
additional information
Geobacillus thermoleovorans A2
-
Tris-HCl, inhibitory effect on the activity
-
OXIDATION STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
addition of H2O2 to the enzyme completely destroyes activity
-
439584
more than 95% of enzyme activity is lost after a 5-min exposure to equimolar H2O2
-
439590
significant nitrate-dependent enhanced degradation of toluene under hypoxic i.e. oxygen-limited condition
-
439591
25C, half-life of 69 min in air, 37C, half-life of 70 min in argon
-
680607
acetone protects almost completely against inactivation by air
-
396602, 439563
ethanol protects against inactivation by air
-
439563
extremely sensitive to O2, easily inactivated in presence of air
-
396602
like native enzyme the immobilized enzyme is rapidly inactivated by oxidants such as O2 or H2O2
-
439571
acetone protects almost completely against inactivation by air
-
396602
extremely sensitive to O2, easily inactivated in presence of air
-
396602, 439572
significant nitrate-dependent enhanced degradation of toluene under hypoxic i.e. oxygen-limited condition
-
439591
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C, in lyophilized state for several months, metapyrocatechase 1 and 2
-
0-4C, 0.02 M Tris-HCl, pH 8.0, fairly stable
-
4C, in acetone buffer under nitrogen for several weeks, metapyrocatechase 1 and 2
-
-80C, did not prevent the initial loss of activity
-
0C, 50 mM Tris-acetone buffer, pH 7.5, the inactivation rate with decreasing enzyme concentration
-
4C, 10 h, the mutant enzymes lost 95% of activity
-
4C, 10 mM HEPES, pH 7.5, 150 mM NaCl, aerobic conditions, stable for several weeks
P06622
4C, 3 days, 20% loss of activity of wild-type enzyme
-
4C, over a month, without loss of activity, crystals of holoenzyme in the presence of acetone
-
4C, Tris-acetone buffer, crystalline enzyme was stable for at most six months
-
-10C, 1 week, under nitrogen gas, 72% of the orginal activity
-
0C, 4 h, about 30% loss of activity
-
4C, buffer, containing 5% acetone, pH 6-7,5, 24 h, stable
-
4C, the enzyme retains complete activity for more than 350 min when kept under an N2 atmosphere, whereas it loses about 80% of its activity when stored for the same time in the absence of nitrogen
Q97YT4, -
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
hydrophobic interaction column pre-equilibrated with 30% (w/v) ammonium sulfate and 0.1 M potassium phosphate buffer pH 7.5, protein eluation with ammonium sulfate gradient [30-0% (w/v)]. DEAE column pre-equilibrated with 50 mM potassium phosphate buffer pH 7.5, protein eluation with NaCl gradient (80-400 mM)
-
metapyrocatechase 1 and 2
-
cells are disrupted and centrifugates, protein supernatant is separated by 2D gel electrophoresis
-
DEAE-Sepharose column chromatography, phenyl-Superose gel filtration, and Sephacryl S-200 gel filtration
P06622
recombinant protein
-
ultracentrifugation and Prepease nickel resin chromatography
-
wild-type and mutant enzymes
-
-
Pseudomonas putida mt-2
-
50 mM Tris-SO4 buffer, pH 8.0, at 4 C. Sucrose density gradient, two-step anion exchange chromatography using MonoQ column attached at a Dionex HPLC system.
-
Ni-NTA-agarose column
-
recombinant enzyme
-
recombinant enzyme
Q8KLV4
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression in Escherichia coli LE392
A5HMH3
expressed in Escherichia coli strains JM109 and DH5alpha
-
expression in Escherichia coli
-
expressed in Escherichia coli (JM109)
-
expression in Escherichia coli
-
gene nahH, DNA and amino acid sequence determination and analysis, phylogenetic tree
-
DNA and amino acid sequence determination and analysis
Planococcus sp.
E7DDG2
gene c23o, DNA and amino acid sequence determination and analysis of wild-type and mutant enzymes and recombinant expression in Escherichia coli strain BL21
Planococcus sp.
-
cloned in Escherichia coli DH5alpha
-
cloned in Escherichia coli DH5alpha
-
expressed in Escherichia coli BL21(DE3) cells
-
expression in Escherichia coli
-
expression in Escherichia coli W3110
-
expression in Escherichia coli; expression in Escherichia coli
Q52264, Q9Z417
expressed in Escherichia coli
-
expressed in Escherichia coli DH 5alpha
-
expressed in Escherichia coli JM109
Q83U22
expressed in Pseudomonas putida G7.C-1 and Escherichia coli DH5alpha
P17262
expression in Escherichia coli
-
expression in Escherichia coli BL21
-
gene nahH, DNA and amino acid sequence determination and analysis, phylogenetic tree
Q34135
expressed in Escherichia coli BL21(DE3)
Q8KLV4
expressed in Escherichia coli strain BL21(DE3)
-
expression in Escherichia coli
-
expression in Escherichia coli TG1
-
expressed in Escherichia coli
-
expressed in Escherichia coli
-
gene nahH, DNA and amino acid sequence determination and analysis, phylogenetic tree
-
DNA and amino acid sequence determination and analysis
A7LB47
expression in Escherichia coli
Q4J6K0
expression in Escherichia coli
-
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
YodB and its paralog YvaP (CatR) are repressors of the yfiDE (catDE) operon encoding a catechol-2,3-dioxygenase
-
the catDE operon is 13-60fold induced in response to quinone-like electrophiles (catechol and MHQ, 1 mM) and diamide in the wild type
-
YodB and its paralog YvaP (CatR) are repressors of the yfiDE (catDE) operon encoding a catechol-2,3-dioxygenase
Bacillus subtilis 168
-
-
the catDE operon is 13-60fold induced in response to quinone-like electrophiles (catechol and MHQ, 1 mM) and diamide in the wild type
Bacillus subtilis 168
-
-
C23O activity (TodE) is almost completely abrogated by exposure to 0.2 mM 3-vinylcatechol
-
C23O activity (TodE) is is unaffected by styrene, toluene, and 3-methylcatechol
-
by phenol and m-cresol
-
by phenol and m-cresol
Ralstonia pickettii PKO1
-
-
the enzyme in strain KB2 is induced by growth on methylphenols
A7LB47
the enzyme in strain KB2 is induced by growth on methylphenols
Stenotrophomonas maltophilia KB2
-
-
ssol_2912 is undetectable when the strain is harvested from the medium with glucose as the sole carbon source, it greatly increased when the strain is harvested from the media with phenol
V5W6K5
ssol_2912 is undetectable when the strain is harvested from the medium with glucose as the sole carbon source, it greatly increased when the strain is harvested from the media with phenol
-
-
mRNA expression of C23O is increased in 2,4-dichlorophenol-amended soil
-
the enzyme is induced by growth on cadmium
Variovorax sp.
-
the enzyme is induced by growth on cadmium
-
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
E286A
-
mutation results in reduction in activity
E286D
-
activity is similar to wild-type enzyme
E286K
-
specific activity is 2.4fold higher than wild-type activity, in contrast with wild-type enzyme mutant enzyme shows no substrate inhibition
E286R
-
activity is similar to wild-type enzyme
E286A
-
mutation results in reduction in activity
-
E286D
-
activity is similar to wild-type enzyme
-
E286K
-
specific activity is 2.4fold higher than wild-type activity, in contrast with wild-type enzyme mutant enzyme shows no substrate inhibition
-
E286R
-
activity is similar to wild-type enzyme
-
H250G
-
reduced twofold relative kcat value for 3-methylcatechol
R215W
-
site-directed mutagenesis
H250G
Escherichia coli JM83
-
reduced twofold relative kcat value for 3-methylcatechol
-
P229S
-
thermostability decreases compared with that of wild-type enzyme
A23T/F212S
Planococcus sp.
-
random mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme
C103R/K289stop
Planococcus sp.
-
random mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme
F191I/C268R/Y272H/V280A/Y293D /
Planococcus sp.
-
random mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme
G127D/P140T
Planococcus sp.
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random mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme
H24R/F168S/Q275R
Planococcus sp.
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random mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme
L13R
Planococcus sp.
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random mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme
M65T
Planococcus sp.
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random mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme
R296Q
Planococcus sp.
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random mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme; random mutagenesis, the mutant shows significant tolerance to acidic pH with an optimum at pH 5.0, as well as a over 1.5fold increased activity, altered substrate inhibition, and 2.5fold lower KM compared to the wild-type enzyme
G127D/P140T
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random mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme
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L13R
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random mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme
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M65T
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random mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme
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R296Q
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random mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme; random mutagenesis, the mutant shows significant tolerance to acidic pH with an optimum at pH 5.0, as well as a over 1.5fold increased activity, altered substrate inhibition, and 2.5fold lower KM compared to the wild-type enzyme
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A177V
-
increased sensitivity to 3-methylcatechol
A229C
P06622
virtually mutated enzyme
H250G
-
reduced twofold relative kcat value for 3-methylcatechol
H294C
P06622
virtually mutated enzyme
T196I
-
increased sensitivity to 3-methylcatechol
A177V
Pseudomonas putida KT 2440
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increased sensitivity to 3-methylcatechol
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H250G
Pseudomonas putida KT 2440
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reduced twofold relative kcat value for 3-methylcatechol
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L226S
Pseudomonas putida KT 2440
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increased activity with 4-ethylcatechol, reduced binding of the ferrous ion cofactor, modified the catalytic activity toward 3-methylcatechol
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T196I
Pseudomonas putida KT 2440
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increased sensitivity to 3-methylcatechol
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T253I
Pseudomonas putida KT 2440
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increased activity with 4-ethylcatechol, reduced binding of the ferrous ion cofactor
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A177V
Pseudomonas putida PaW94
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increased sensitivity to 3-methylcatechol
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L226S
Pseudomonas putida PaW94
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increased activity with 4-ethylcatechol, reduced binding of the ferrous ion cofactor, modified the catalytic activity toward 3-methylcatechol
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T196I
Pseudomonas putida PaW94
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increased sensitivity to 3-methylcatechol
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A229C
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forming disulfide bonds, more alkalescency stable, improvement of thermostability, widened optimum temperature from 40-50C
A229C
Pseudomonas sp. CGMCC2953
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forming disulfide bonds, more alkalescency stable, improvement of thermostability, widened optimum temperature from 40-50C
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H294C
Pseudomonas sp. CGMCC2953
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forming disulfide bonds, more alkalescency stable, improvement of thermostability, widened optimum temperature from 40-50C
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H199N
Q8KLV4
strongly reduced activity, significant changes in pH profile
H246A
Q8KLV4
strongly reduced activity, significant changes in pH profile
H246N
Q8KLV4
strongly reduced activity, significant changes in pH profile
T249A
-
reduced kcat and increased Km-values
T249G
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reduced kcat and increased Km-values
T249S
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reduced kcat and increased Km-values
Y255F
Q8KLV4
strongly reduced activity
H199N
Pseudomonas stutzeri OX1
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strongly reduced activity, significant changes in pH profile
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H246A
Pseudomonas stutzeri OX1
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strongly reduced activity, significant changes in pH profile
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H246N
Pseudomonas stutzeri OX1
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strongly reduced activity, significant changes in pH profile
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T249A
Pseudomonas stutzeri OX1
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reduced kcat and increased Km-values
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T249G
Pseudomonas stutzeri OX1
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reduced kcat and increased Km-values
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T249S
Pseudomonas stutzeri OX1
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reduced kcat and increased Km-values
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L226S
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increased activity with 4-ethylcatechol, reduced binding of the ferrous ion cofactor, modified the catalytic activity toward 3-methylcatechol
additional information
Q52264, Q9Z417
construction of hybrid enzymes by exchange of parts of protein domain 2 with that of enzyme from Pseudomonas putida strain GJ31. Results indicate that the 43 C-terminal amino acids probably determine the substrate specificities; construction of hybrid enzymes by exchange of parts of protein domain 2 with that of enzyme from Pseudomonas putida strain UCC2. Results indicate that the 43 C-terminal amino acids probably determine the substrate specificities
additional information
P06622
used for identifying potential sites of introducing disulfide bond of C23O from Pseudomonas sp.
T253I
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increased activity with 4-ethylcatechol, reduced binding of the ferrous ion cofactor
additional information
Pseudomonas putida GJ31
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construction of hybrid enzymes by exchange of parts of protein domain 2 with that of enzyme from Pseudomonas putida strain UCC2. Results indicate that the 43 C-terminal amino acids probably determine the substrate specificities
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T253I
Pseudomonas putida PaW94
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increased activity with 4-ethylcatechol, reduced binding of the ferrous ion cofactor
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additional information
Pseudomonas putida UCC2
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construction of hybrid enzymes by exchange of parts of protein domain 2 with that of enzyme from Pseudomonas putida strain GJ31. Results indicate that the 43 C-terminal amino acids probably determine the substrate specificities
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H294C
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forming disulfide bonds, more alkalescency stable, improvement of thermostability, widened optimum temperature from 40-50C
additional information
-
construction of different hybrid enzymes containing different parts of type I.2.A and I.2.B enzyme, only one of the constructed enzymes is found to be active
Y255F
Pseudomonas stutzeri OX1
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strongly reduced activity
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additional information
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construction of different hybrid enzymes containing different parts of type I.2.A and I.2.B enzyme, only one of the constructed enzymes is found to be active
additional information
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immobilization of catechol 2,3-dioxygenase from KB2 strain using calcium alginate, the iimmobilized enzyme shows relatively higher activity against 3-methylcatechol, 4-methylcatechol, 4,5-dichlorocatechol, 3,5-dichlorocatechol, hydroquinone and tetrachlorohydroquinone than soluble enzyme, immobilization protects the enzyme from the inhibition and enhanced its resistance to inactivation during catalysis
additional information
Stenotrophomonas maltophilia KB2
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immobilization of catechol 2,3-dioxygenase from KB2 strain using calcium alginate, the iimmobilized enzyme shows relatively higher activity against 3-methylcatechol, 4-methylcatechol, 4,5-dichlorocatechol, 3,5-dichlorocatechol, hydroquinone and tetrachlorohydroquinone than soluble enzyme, immobilization protects the enzyme from the inhibition and enhanced its resistance to inactivation during catalysis
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Renatured/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
inactivation of XylE enzyme by 4-methylcatechol results in oxidation of the active site iron to a high spin ferric state. Soluble [2Fe-2S] ferredoxin protein XylT reactivates XylE through reduction of the iron atom in the active site of the enzyme. XylE reactivation involves catalytic nonstoichiometric amounts of XylT
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APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
degradation
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because of broad spectrum of dioxygenases types that Stenotrophomonas maltophilia KB2 can exhibit, this strain appears to be very powerful and useful tool in the biotreatment of wastewaters and in soil decontamination
degradation
Stenotrophomonas maltophilia KB2
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because of broad spectrum of dioxygenases types that Stenotrophomonas maltophilia KB2 can exhibit, this strain appears to be very powerful and useful tool in the biotreatment of wastewaters and in soil decontamination
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environmental protection
Variovorax sp.
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C23O appears to be very powerful and useful tools in the biotreatment of wastewaters and soil decontamination
environmental protection
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C23O appears to be very powerful and useful tools in the biotreatment of wastewaters and soil decontamination
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