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Information on EC 1.13.11.2 - catechol 2,3-dioxygenase and Organism(s) Pseudomonas putida and UniProt Accession P06622
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1.13.11.2 catechol 2,3-dioxygenaseIUBMB Comments
Requires FeII. The enzyme initiates the meta-cleavage pathway of catechol degradation.
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Word Map
- 1.13.11.2
- heme
- putida
- carboxylase
- hydroxylase
- rubisco
- ferredoxins
- ribulose-1,5-bisphosphate
- l-arginine
-
non-heme
-
rieske
- tetrahydrobiopterin
-
dioxygenation
- ribulose
- toluene
- 2-oxoglutarate
- naphthalene
- biphenyls
- rhodococcus
- fmn
- nnos
-
bioremediation
-
mixed-function
-
nitric-oxide
- phenanthrene
-
photorespiration
-
photorespiratory
-
1,5-bisphosphate
- biliverdin
- bh4
- l-citrulline
- sphingomonas
-
ring-hydroxylating
- comamonas
-
dihydroxylation
- carbazole
- xylene
- l-arg
-
2-oxoglutarate-dependent
-
heme-heme
-
diiron
-
ironii
- 4-methylcatechol
-
monooxygenation
- rubp
- testosteroni
- sphingobium
- ethylbenzene
-
4.1.1.39
- degradation
- environmental protection
- fluoranthene
- rhodochrous
The taxonomic range for the selected organisms is: Pseudomonas putida
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
oxygenase, catechol 2,3-dioxygenase, catechol-2,3-dioxygenase, metapyrocatechase, catechol 2,3-oxygenase, meta-cleavage dioxygenase, catechol 2,3 dioxygenase, c23os, c2,3o, 3sc23o, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
catechol 2,3-di-2,3-pyrocatechase
-
-
-
-
catechol 2,3-oxygenase
-
-
-
-
catechol oxygenase
-
-
-
-
metapyrocatechase
-
-
-
-
oxygenase
-
-
-
-
pyrocatechol 2,3-dioxygenase
-
-
-
-
XylE
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
catechol + O2 = 2-hydroxymuconate-6-semialdehyde
ordered bi uni mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
oxidation
reduction
-
-
-
-
oxidation
-
-
-
-
PATHWAY SOURCE
PATHWAYS
KEGG
-
-, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
catechol:oxygen 2,3-oxidoreductase (decyclizing)
Requires FeII. The enzyme initiates the meta-cleavage pathway of catechol degradation.
CAS REGISTRY NUMBER
COMMENTARY
9029-46-3
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3-chlorocatechol + O2
3-chloro-2-hydroxymuconate semialdehyde
rapid inactivation of enzyme during turnover
-
-
?
3-formylcatechol + O2
3-formyl-2-hydroxymuconate semialdehyde
-
-
-
?
3-phenylcatechol + O2
2-hydroxy-3-phenylmuconate semialdehyde
-
-
-
?
4-bromocatechol + O2
4-bromo-2-hydroxymuconate semialdehyde
-
-
-
?
4-chlorocatechol + O2
4-chloro-2-hydroxymuconate semialdehyde
-
-
-
?
4-formylcatechol + O2
4-formyl-2-hydroxymuconate semialdehyde
-
-
-
?
4-hydroxymethylcatechol + O2
2-hydroxy-4-hydroxymethylmuconate semialdehyde
rapid inactivation of enzyme during turnover
-
-
?
4-nitrocatechol + O2
2-hydroxy-4-nitromuconate semialdehyde
-
-
-
?
2,3-dihydroxybiphenyl + O2
?
1.3% of the activity with 2,3-dihydroxybiphenyl
-
-
?
3-chlorocatechol + O2
2-chloro-2-hydroxy-6-oxohexa-2,4-dienoate
-
-
-
-
?
3-methoxycatechol + O2
2-hydroxy-3-methoxy-6-oxohexa-2,4-dienoate
-
-
-
-
?
3-methylcatechol + O2
?
33% of the activity with 4-chlorocatechol
-
-
?
4-chlorocatechol + O2
?
39% of the activity with 4-chlorocatechol
-
-
?
4-methylcatechol + O2
?
activity is 5.72fold higher than with catechol
-
-
?
4-n-butylcatechol + O2
?
activity is 1.85fold higher than with catechol
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
degradation of aromatic compounds
-
-
?
3-chlorocatechol + O2
3-chloro-2-hydroxymuconate semialdehyde
about 9% of the rate with catechol
-
-
?
3-chlorocatechol + O2
3-chloro-2-hydroxymuconate semialdehyde
about 95% of the rate with catechol
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
-
-
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
about 105% of the rate with catechol
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
about 43% of the rate with catechol
-
-
?
4-chlorocatechol + O2
4-chloro-2-hydroxymuconate semialdehyde
about 16% of the rate with catechol
-
-
?
4-chlorocatechol + O2
4-chloro-2-hydroxymuconate semialdehyde
about 75% of the rate with catechol
-
-
?
4-methylcatechol + O2
2-hydroxy-3-methyl-6-oxohexa-2,4-dienoate
-
-
-
-
?
4-methylcatechol + O2
2-hydroxy-3-methyl-6-oxohexa-2,4-dienoate
-
highly specific for
-
-
?
4-methylcatechol + O2
2-hydroxy-3-methyl-6-oxohexa-2,4-dienoate
-
hypoxic strains with significantly higher affinities
-
-
?
4-methylcatechol + O2
2-hydroxy-4-methyl-6-oxohexa-2,4-dienoate
about 47% of the rate with catechol
-
-
?
4-methylcatechol + O2
2-hydroxy-4-methyl-6-oxohexa-2,4-dienoate
about 89% of the rate with catechol
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
highly specific for
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
hypoxic strains have enzymes with significantly higher affinities for catechol than for nonhypoxic strains
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
best substrates
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
enzyme is a important component in the degradation pathways of toluene and xylene and catalyses the dioxygenolytic cleavage of the aromatic ring
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
benzoate degadation pathway
-
-
?
additional information
?
-
no cleavage of 4-carboxycatechol, 4-carboxymethylcatechol and 4-tert-butylcatechol
-
-
?
additional information
?
-
no activity with 4-tert-butylcatechol
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
catechol + O2
2-hydroxymuconate semialdehyde
degradation of aromatic compounds
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
enzyme is a important component in the degradation pathways of toluene and xylene and catalyses the dioxygenolytic cleavage of the aromatic ring
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
benzoate degadation pathway
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
Fe2+
-
activity is closely related to specific content of iron in this protein
Fe2+
-
enzyme might undergo oxidation of its active-site ferrous iron atom
Fe2+
-
3.7 mol of iron per mol of enzyme or 0.93 mol per mol of the subunit
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3-vinylcatechol
-
C23O activity (TodE) is almost completely abrogated by exposure to 0.2 mM 3-vinylcatechol
additional information
-
C23O activity (TodE) is unaffected by styrene, toluene, and 3-methylcatechol
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
Km determination for enzymes from hypoxic and nonhypoxic pseudomonads, Km for oxygen approximately five-fold lower under hypoxic conditions for hypoxic strains
-
additional information
additional information
-
Km of wild-type and mutant enzymes
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
-
the hypoxic strains have enzymes with significantly higher substrate turnover rates for the nonhypoxic strains
-
additional information
additional information
-
kcat values of enzyme and hybrid proteins
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
15
crude extract, in 20 mM NaH2PO4, pH 7.5, containing 1 mM catechol at 50°C
802
after 52.7fold purification, in 20 mM NaH2PO4, pH 7.5, containing 1 mM catechol at 50°C
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25 - 80
the enzyme activity increases starting from 25°C and reaches its maximum at 50°C, the enzyme starts to denature at 55°C and the structure is destroyed by the time the temperature reaches 80°C
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
mt-2, used for identifying potential sites of introducing disulfide bond of C23O from Pseudomonas sp.
UniProt
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
inactivation of TodE and the subsequent accumulation of 3-vinylcatechol results in toxicity and cell death
physiological function
-
overexpressing TodE is necessary to allow Pseudomonas putida strain F1 to grow on styrene
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
140000
31000
35000
-
4 * 35000, SDS-PAGE, 4 * 35195, MS, 4 * 35156 based on DNA sequence
35156
-
4 * 35000, SDS-PAGE, 4 * 35195, MS, 4 * 35156 based on DNA sequence
35195
-
4 * 35000, SDS-PAGE, 4 * 35195, MS, 4 * 35156 based on DNA sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homotetramer
-
4 * 35000, SDS-PAGE, 4 * 35195, MS, 4 * 35156 based on DNA sequence
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
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
L226S
-
increased activity with 4-ethylcatechol, reduced binding of the ferrous ion cofactor, modified the catalytic activity toward 3-methylcatechol
T253I
-
increased activity with 4-ethylcatechol, reduced binding of the ferrous ion cofactor
additional information
additional information
used for identifying potential sites of introducing disulfide bond of C23O from Pseudomonas sp.
additional information
construction of hybrid enzymes by exchange of parts of protein domain 2 with that of enzyme from Pseudomonas putida strain GJ31. Results indicate that the 43 C-terminal amino acids probably determine the substrate specificities
additional information
construction of hybrid enzymes by exchange of parts of protein domain 2 with that of enzyme from Pseudomonas putida strain GJ31. Results indicate that the 43 C-terminal amino acids probably determine the substrate specificities
additional information
-
construction of hybrid enzymes by exchange of parts of protein domain 2 with that of enzyme from Pseudomonas putida strain GJ31. Results indicate that the 43 C-terminal amino acids probably determine the substrate specificities
additional information
construction of hybrid enzymes by exchange of parts of protein domain 2 with that of enzyme from Pseudomonas putida strain UCC2. Results indicate that the 43 C-terminal amino acids probably determine the substrate specificities
additional information
construction of hybrid enzymes by exchange of parts of protein domain 2 with that of enzyme from Pseudomonas putida strain UCC2. Results indicate that the 43 C-terminal amino acids probably determine the substrate specificities
additional information
-
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
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 50
the half-life of the enzyme activity at 30°C is about 7 h and the half-life of the enzyme activity at 50°C is 45 min
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
acetone protects against inactivation by air, concentration of 10%
-
immobilization enhances stability against inactivation by heat, acid or alkaline pH and various denaturing agents
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2-mercaptoethanol
-
no significant protection of the enzyme from inactivation
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
like native enzyme the immobilized enzyme is rapidly inactivated by oxidants such as O2 or H2O2
-
439571
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, 10 mM HEPES, pH 7.5, 150 mM NaCl, aerobic conditions, stable for several weeks
0°C, 50 mM Tris-acetone buffer, pH 7.5, the inactivation rate with decreasing enzyme concentration
-
4°C, over a month, without loss of activity, crystals of holoenzyme in the presence of acetone
-
4°C, Tris-acetone buffer, crystalline enzyme was stable for at most six months
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
DEAE-Sepharose column chromatography, phenyl-Superose gel filtration, and Sephacryl S-200 gel filtration
cells are disrupted and centrifugates, protein supernatant is separated by 2D gel electrophoresis
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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
-
RENATURED/Commentary
ORGANISM
UNIPROT
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
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
degradation
degradation
comparison of binding sites and affinities using substrates chlorsulfon and metsulfuron-methyl. Homoprotocatechuate 2,3-dioxygenase from Brevibacterium fuscum and Arthrobacter globiformis are more effective in binding than catechol 2,3-dioxygenase from Pseudomonas putida. B. fuscum and A. globiformis have more potential than P. putida to remediate chlorsulfuron and metsulfuronmethyl
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Inoue, J.; Shaw, J.P.; Rekik, M.; Harayama, S.
Overlapping substrate specificities of benzaldehyde dehydrogenase (the xylC gene product) and 2-hydroxymuconic semialdehyde dehydrogenase (the xylG gene product) encoded by TOL plasmid pWW0 of Pseudomonas putida
J. Bacteriol.
177
1196-1201
1995
Pseudomonas putida
Gibson, D.T.
Assay of enzymes of aromatic metabolism
Methods Microbiol.
6A
463-478
1971
Pseudomonas sp., Pseudomonas putida
-
Arciero, D.M.; Orville, A.M.; Lipscomb, J.D.
Water and nitric oxide binding by protocatechuate 4,5-dioxygenase and catechol 2,3-dioxygenase. Evidence for binding of exogenous ligands to the active site Fe2+ of extradiol dioxygenases
J. Biol. Chem.
260
14035-14044
1985
Pseudomonas putida
Ghosal, D.; You, I.S.; Gunsalus, I.C.
Nucleotide sequence and expression of gene nahH of plasmid NAH7 and homology with gene xylE of TOL pWWO
Gene
55
19-28
1987
Pseudomonas putida, Pseudomonas putida PpG 1064
Hori, K.; Hashimoto, T.; Nozaki, M.
Kinetic studies on the reaction mechanism of dioxygenases
J. Biochem.
74
375-384
1973
Pseudomonas putida
Nozaki, M.; Kagamiyama, H.; Hayaishi, O.
Metapyrocatechase, purification, crystallization and some properties
Biochem. Z.
338
582-590
1963
Pseudomonas putida
Klecka, G.M.; Gibson, D.T.
Inhibition of catechol 2,3-dioxygenase from Pseudomonas putida by 3-chlorocatechol
Appl. Environ. Microbiol.
41
1159-1165
1981
Pseudomonas putida
Lee, Y.L.; Dagley, S.
Comparison of two dioxygenases from Pseudomonas putida
J. Bacteriol.
131
1016-1017
1977
Pseudomonas putida
Saeki, Y.; Nozaki, M.; Senoh, S.
Cleavage of pyrogallol by non-heme iron-containing dioxygenases
J. Biol. Chem.
255
8465-8471
1980
Escherichia coli, Pseudomonas aeruginosa, Pseudomonas putida
Iwaki, M.; Nozaki, M.
Immobilization of metapyrocatechase and its properties in comparison with the soluble enzyme
J. Biochem.
91
1549-1553
1982
Pseudomonas putida
Takemori, S.; Komiyama, T.; Katagiri, M.
Apo- and reconstituted holoenzymes of metapyrocatechase from Pseudomonas putida
Eur. J. Biochem.
23
178-184
1971
Pseudomonas putida, Pseudomonas putida T-2
Winkler, J.; Eltis, L.D.; Dwyer, D.F.; Rohde, M.
Tetrameric structure and cellular location of catechol 2,3-dioxygenase
Arch. Microbiol.
163
65-69
1995
Pseudomonas putida
Cerdan, P.; Wasserfallen, A.; Rekik, M.; Timmis, K.N.; Harayama, S.
Substrate specificity of catechol 2,3-dioxygenase encoded by TOL plasmid pWW0 of Pseudomonas putida and its relationship to cell growth
J. Bacteriol.
176
6074-6081
1994
Pseudomonas putida, Pseudomonas putida KT 2440, Pseudomonas putida PaW94
Edghill, L.A.; Russell, A.D.; Day, M.J.; Furr, J.R.
Rapid evaluation of biocidal activity using a transposon-encoded catechol 2,3-dioxygenase from Pseudomonas putida
J. Appl. Microbiol.
87
91-98
1999
Pseudomonas putida, Pseudomonas putida UWC1-pQM899
Bertini, I.; Briganti, F.; Scozzafava, A.
Aliphatic and aromatic inhibitors binding to the active site of catechol 2,3-dioxygenase from Pseudomonas putida mt-2
FEBS Lett.
343
56-60
1994
Pseudomonas putida
Cerdan, P.; Rekik, M.; Harayama, S.
Substrate specificity differences between two catechol 2,3-dioxygenases encoded by the TOL and NAH plasmids from Pseudomonas putida
Eur. J. Biochem.
229
113-118
1995
Escherichia coli, Pseudomonas putida, Pseudomonas putida KT 2440, Escherichia coli JM83
Kobayashi, T.; Ishida, T.; Horiike, K.; Takahara, Y.; Numao, N.; Nakazawa, A.; Nakazawa, T.; Nozaki, M.
Overexpression of Pseudomonas putida catechol 2,3-dioxygenase with high specific activity by genetically engineered Escherichia coli
J. Biochem.
117
614-622
1995
Pseudomonas putida
Kukor, J.J.; Olsen, R.H.
Catechol 2,3-dioxygenases functional in oxygen-limited (hypoxic) environments
Appl. Environ. Microbiol.
62
1728-1740
1996
Burkholderia cepacia, Pseudomonas sp., Pseudomonas putida, Pseudomonas fluorescens, Ralstonia pickettii, Pseudomonas fluorescens CFS 215, Ralstonia pickettii PK01, Burkholderia cepacia G4, Pseudomonas sp. W31
Tropel, D.; Meyer, C.; Armengaud, J.; Jouanneau, Y.
Ferredoxin-mediated reactivation of the chlorocatechol 2,3-dioxygenase from Pseudomonas putida GJ31
Arch. Microbiol.
177
345-351
2002
Pseudomonas putida
Ishida, T.; Tanaka, H.; Horiike, K.
Quantitative structure-activity relationship for the cleavage of C3/C4-substituted catechols by a prototypal extradiol catechol dioxygenase with broad substrate specificity
J. Biochem.
135
721-730
2004
Pseudomonas putida (P06622), Pseudomonas putida mt-2 / ATCC 33015 / DSM 3931 / NCIB 12182 / NCIMB 12182 (P06622)
Merimaa, M.; Heinaru, E.; Liivak, M.; Vedler, E.; Heinaru, A.
Grouping of phenol hydroxylase and catechol 2,3-dioxygenase genes among phenol- and p-cresol-degrading Pseudomonas species and biotypes
Arch. Microbiol.
186
287-296
2006
Pseudomonas putida, Pseudomonas fluorescens, Pseudomonas mendocina, Pseudomonas putida Ppu PC13
Mars, A.E.; Kingma, J.; Kaschabek, S.R.; Reineke, W.; Janssen, D.B.
Conversion of 3-chlorocatechol by various catechol 2,3-dioxygenases and sequence analysis of the chlorocatechol dioxygenase region of Pseudomonas putida GJ31
J. Bacteriol.
181
1309-1318
1999
Pseudomonas putida (Q52264), Pseudomonas putida (Q9Z417), Pseudomonas putida, Pseudomonas putida UCC2 (Q52264)
Hugo, N.; Armengaud, J.; Gaillard, J.; Timmis, K.N.; Jouanneau, Y.
A novel -2Fe-2S- ferredoxin from Pseudomonas putida mt2 promotes the reductive reactivation of catechol 2,3-dioxygenase.
J. Biol. Chem.
273
9622-9629
1998
Pseudomonas putida, Pseudomonas putida mt2
Takeo, M.; Nishimura, M.; Takahashi, H.; Kitamura, C.; Kato, D.; Negoro, S.
Purification and characterization of alkylcatechol 2,3-dioxygenase from butylphenol degradation pathway of Pseudomonas putida MT4
J. Biosci. Bioeng.
104
309-314
2007
Pseudomonas putida (Q842G7), Pseudomonas putida MT4 (Q842G7)
Cao, B.; Geng, A.; Loh, K.C.
Induction of ortho- and meta-cleavage pathways in Pseudomonas in biodegradation of high benzoate concentration: MS identification of catabolic enzymes
Appl. Microbiol. Biotechnol.
81
99-107
2008
Pseudomonas putida
Wei, J.; Zhou, Y.; Xu, T.; Lu, B.
Rational design of catechol-2, 3-dioxygenase for improving the enzyme characteristics
Appl. Biochem. Biotechnol.
162
116-126
2009
Pseudomonas sp., Pseudomonas putida (P06622), Pseudomonas sp. CGMCC2953
Huang, S.; Hsu, Y.; Wu, C.; Lynn, J.; Li, W.
Thermal effects on the activity and structural conformation of catechol 2,3-dioxygenase from Pseudomonas putida SH1
J. Phys. Chem. B
114
987-992
2010
Pseudomonas putida (P06622), Pseudomonas putida SH1 (P06622), Pseudomonas putida SH1
George, K.W.; Kagle, J.; Junker, L.; Risen, A.; Hay, A.G.
Growth of Pseudomonas putida F1 on styrene requires increased catechol-2,3-dioxygenase activity, not a new hydrolase
Microbiology
157
89-98
2011
Pseudomonas putida
Xie, Y.; Yu, F.; Wang, Q.; Gu, X.; Chen, W.
Cloning of catechol 2,3-dioxygenase gene and construction of a stable genetically engineered strain for degrading crude oil
Indian J. Microbiol.
54
59-64
2014
Pseudomonas putida, Pseudomonas putida BNF1
Bauri, S.; Sen, M.; Das, R.; Mondal, S.
In-silico investigation of the efficiency of microbial dioxygenases in degradation of sulfonylurea group herbicides
Bioremediat. J.
26
76-87
2022
Pseudomonas putida (Q44048)
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