Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
6-chlorohydroxyquinol + O2
2-chloromaleylacetate
benzene-1,2,4-triol + O2
3-hydroxy-cis,cis-muconate
benzene-1,2,4-triol + O2
3-hydroxy-cis-cis-muconate
benzene-1,2,4-triol + O2
maleylacetate
catechol + O2
2-hydroxymuconic 6-semialdehyde
extradiol ring cleavage
-
?
catechol + O2
cis,cis-muconate
catechol + O2
cis,cis-muconic acid
hydroxyquinol + O2
maleylacetate
additional information
?
-
3-methylcatechol + O2
?
-
-
-
?
3-methylcatechol + O2
?
-
-
-
?
4-chlorocatechol + O2
?
-
-
-
?
4-chlorocatechol + O2
?
-
-
-
?
6-chlorohydroxyquinol + O2
2-chloromaleylacetate
-
33.5% relative activity of that measured with hydroxyquinol
-
?
6-chlorohydroxyquinol + O2
2-chloromaleylacetate
-
33.5% relative activity of that measured with hydroxyquinol
-
?
6-chlorohydroxyquinol + O2
2-chloromaleylacetate
-
-
-
?
6-chlorohydroxyquinol + O2
2-chloromaleylacetate
-
-
-
?
benzene-1,2,4-triol + O2
3-hydroxy-cis,cis-muconate
-
-
-
?
benzene-1,2,4-triol + O2
3-hydroxy-cis,cis-muconate
-
-
-
?
benzene-1,2,4-triol + O2
3-hydroxy-cis,cis-muconate
-
-
-
-
?
benzene-1,2,4-triol + O2
3-hydroxy-cis,cis-muconate
-
-
-
-
?
benzene-1,2,4-triol + O2
3-hydroxy-cis-cis-muconate
-
-
-
?
benzene-1,2,4-triol + O2
3-hydroxy-cis-cis-muconate
-
-
-
?
benzene-1,2,4-triol + O2
3-hydroxy-cis-cis-muconate
-
-
-
?
benzene-1,2,4-triol + O2
3-hydroxy-cis-cis-muconate
-
-
-
?
benzene-1,2,4-triol + O2
3-hydroxy-cis-cis-muconate
-
-
-
?
benzene-1,2,4-triol + O2
3-hydroxy-cis-cis-muconate
-
-
-
-
?
benzene-1,2,4-triol + O2
3-hydroxy-cis-cis-muconate
-
-
-
-
?
benzene-1,2,4-triol + O2
3-hydroxy-cis-cis-muconate
-
-
-
-
?
benzene-1,2,4-triol + O2
3-hydroxy-cis-cis-muconate
-
-
-
?
benzene-1,2,4-triol + O2
3-hydroxy-cis-cis-muconate
Fomes pinicola
-
-
-
?
benzene-1,2,4-triol + O2
3-hydroxy-cis-cis-muconate
-
-
-
?
benzene-1,2,4-triol + O2
3-hydroxy-cis-cis-muconate
Lenzites trabea
-
-
-
?
benzene-1,2,4-triol + O2
3-hydroxy-cis-cis-muconate
Poria ambigua
-
-
-
?
benzene-1,2,4-triol + O2
3-hydroxy-cis-cis-muconate
Sporotrichum pulverulentum
-
-
-
-
?
benzene-1,2,4-triol + O2
3-hydroxy-cis-cis-muconate
-
-
-
-
?
benzene-1,2,4-triol + O2
3-hydroxy-cis-cis-muconate
-
-
-
-
?
benzene-1,2,4-triol + O2
3-hydroxy-cis-cis-muconate
-
-
-
?
benzene-1,2,4-triol + O2
3-hydroxy-cis-cis-muconate
-
-
-
?
benzene-1,2,4-triol + O2
maleylacetate
-
-
maleylacetate, i.e. cis-hexenedioate, is the isomer of 3-hydroxy-cis-cis-muconate
?
benzene-1,2,4-triol + O2
maleylacetate
6.8-fold activity of that for catechol
-
-
?
benzene-1,2,4-triol + O2
maleylacetate
-
-
maleylacetate, i.e. cis-hexenedioate, is the isomer of 3-hydroxy-cis-cis-muconate
?
benzene-1,2,4-triol + O2
maleylacetate
-
-
maleylacetate, i.e. cis-hexenedioate, is the isomer of 3-hydroxy-cis-cis-muconate
?
benzene-1,2,4-triol + O2
maleylacetate
-
-
maleylacetate, i.e. cis-hexenedioate, is the isomer of 3-hydroxy-cis-cis-muconate
?
benzene-1,2,4-triol + O2
maleylacetate
-
-
-
-
?
benzene-1,2,4-triol + O2
maleylacetate
-
-
-
-
?
benzene-1,2,4-triol + O2
maleylacetate
-
-
-
-
?
benzene-1,2,4-triol + O2
maleylacetate
-
-
maleylacetate, i.e. cis-hexenedioate, is the isomer of 3-hydroxy-cis-cis-muconate
?
benzene-1,2,4-triol + O2
maleylacetate
Fomes pinicola
-
-
maleylacetate, i.e. cis-hexenedioate, is the isomer of 3-hydroxy-cis-cis-muconate
?
benzene-1,2,4-triol + O2
maleylacetate
-
-
maleylacetate, i.e. cis-hexenedioate, is the isomer of 3-hydroxy-cis-cis-muconate
?
benzene-1,2,4-triol + O2
maleylacetate
Lenzites trabea
-
-
maleylacetate, i.e. cis-hexenedioate, is the isomer of 3-hydroxy-cis-cis-muconate
?
benzene-1,2,4-triol + O2
maleylacetate
Poria ambigua
-
-
maleylacetate, i.e. cis-hexenedioate, is the isomer of 3-hydroxy-cis-cis-muconate
?
benzene-1,2,4-triol + O2
maleylacetate
-
-
-
-
?
benzene-1,2,4-triol + O2
maleylacetate
-
-
-
-
?
benzene-1,2,4-triol + O2
maleylacetate
Sporotrichum pulverulentum
-
-
-
-
?
benzene-1,2,4-triol + O2
maleylacetate
-
-
-
-
?
benzene-1,2,4-triol + O2
maleylacetate
-
-
-
-
?
benzene-1,2,4-triol + O2
maleylacetate
-
-
maleylacetate, i.e. cis-hexenedioate, is the isomer of 3-hydroxy-cis-cis-muconate
?
benzene-1,2,4-triol + O2
maleylacetate
-
-
maleylacetate, i.e. cis-hexenedioate, is the isomer of 3-hydroxy-cis-cis-muconate
?
catechol + O2
?
-
-
-
?
catechol + O2
?
-
-
-
-
?
catechol + O2
?
-
-
-
-
?
catechol + O2
cis,cis-muconate
-
-
-
?
catechol + O2
cis,cis-muconate
-
-
-
?
catechol + O2
cis,cis-muconic acid
intradiol ring cleavage
-
?
catechol + O2
cis,cis-muconic acid
-
-
-
-
?
hydroxyquinol + O2
?
-
-
-
-
?
hydroxyquinol + O2
?
-
-
-
-
?
hydroxyquinol + O2
maleylacetate
-
-
-
?
hydroxyquinol + O2
maleylacetate
-
-
-
?
hydroxyquinol + O2
maleylacetate
-
intradiol ringcleavage
-
-
?
additional information
?
-
-
when the cells are grown on a mixture of 4-chlorophenol, 4-nitrophenol and phenol, 4-chlorophenol degradation apparently is delayed until 4-nitrophenol is almost completely depleted. Phenol is degraded more slowly than the other compounds and not until 4-nitrophenol and 4-chlorophenol are depleted, despite this being the least toxic compound of the three
-
-
?
additional information
?
-
-
decomposition of aromatic hydrocarbon intermediates by recombinant hydroxyquinol 1,2-dioxygenase. Substrate specificity of Ar 1,2-HQD indicates that the catalytic function of this enzyme is similar to that of the type-II catechol 1,2-dioxygenase (1,2-CTD)
-
-
?
additional information
?
-
decomposition of aromatic hydrocarbon intermediates by recombinant hydroxyquinol 1,2-dioxygenase. Substrate specificity of Ar 1,2-HQD indicates that the catalytic function of this enzyme is similar to that of the type-II catechol 1,2-dioxygenase (1,2-CTD)
-
-
?
additional information
?
-
CphA-1 exhibits no activity with 4-chlorocatechol, hydroquinone, or resorcinol
-
-
?
additional information
?
-
CphA-1 exhibits no activity with 4-chlorocatechol, hydroquinone, or resorcinol
-
-
?
additional information
?
-
-
CphA-1 exhibits no activity with 4-chlorocatechol, hydroquinone, or resorcinol
-
-
?
additional information
?
-
CphA-2 exhibits no activity with 4-chlorocatechol, hydroquinone, or resorcinol
-
-
?
additional information
?
-
CphA-2 exhibits no activity with 4-chlorocatechol, hydroquinone, or resorcinol
-
-
?
additional information
?
-
-
CphA-2 exhibits no activity with 4-chlorocatechol, hydroquinone, or resorcinol
-
-
?
additional information
?
-
-
when the cells are grown on a mixture of 4-chlorophenol, 4-nitrophenol and phenol, 4-chlorophenol degradation apparently is delayed until 4-nitrophenol is almost completely depleted. Phenol is degraded more slowly than the other compounds and not until 4-nitrophenol and 4-chlorophenol are depleted, despite this being the least toxic compound of the three
-
-
?
additional information
?
-
-
decomposition of aromatic hydrocarbon intermediates by recombinant hydroxyquinol 1,2-dioxygenase. Substrate specificity of Ar 1,2-HQD indicates that the catalytic function of this enzyme is similar to that of the type-II catechol 1,2-dioxygenase (1,2-CTD)
-
-
?
additional information
?
-
decomposition of aromatic hydrocarbon intermediates by recombinant hydroxyquinol 1,2-dioxygenase. Substrate specificity of Ar 1,2-HQD indicates that the catalytic function of this enzyme is similar to that of the type-II catechol 1,2-dioxygenase (1,2-CTD)
-
-
?
additional information
?
-
-
Pseudomonas sp. PDS-7 is capable of utilizing p-nitrophenol as the sole carbon, nitogen and energy source, concentration up to 80 mg/l
-
-
?
additional information
?
-
-
PnpG is not active against protocatechuate and gentisate
-
-
?
additional information
?
-
-
Pseudomonas sp. PDS-7 is capable of utilizing p-nitrophenol as the sole carbon, nitogen and energy source, concentration up to 80 mg/l
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.37
-
substrate hydroxyquinol
0.45
-
substrate catechol
15.3
recombinant enzyme, crude enzyme extract, substrate hydroxyquinol, pH 7.5, 25°C
479.5
purified recombinant enzyme, substrate 3-methylcatechol, pH 7.5, 25°C
479.6
65.2fold purified enzyme, with 3-methylcatechol as substrate, at pH 7.5 and 25°C
5.5
recombinant enzyme, crude enzyme extract, substrate 4-chlorocatechol, pH 7.5, 25°C
7.06
-
reactivated with 0.01 mM Fe2+
284.6
51.7fold purified enzyme, with 4-chlorocatechol as substrate, at pH 7.5 and 25°C
284.6
purified recombinant enzyme, substrate 4-chlorocatechol, pH 7.5, 25°C
391
62.5fold purified enzyme, with catechol as substrate, at pH 7.5 and 25°C
391
purified recombinant enzyme, substrate catechol , pH 7.5, 25°C
795.6
52fold purified enzyme, with hydroxyquinol as substrate, at pH 7.5 and 25°C
795.6
purified recombinant enzyme, substrate hydroxyquinol, pH 7.5, 25°C
additional information
-
additional information
-
-
additional information
cell extracts from 4-chlorophenol-grown cells deplete hydoxyquinol from the medium with an activity of 96 microM/min/mg protein. No depletion of hydroxyquinol is measured in extracts of Succinate-grown cells.
additional information
cell extracts from 4-chlorophenol-grown cells deplete hydoxyquinol from the medium with an activity of 96 microM/min/mg protein. No depletion of hydroxyquinol is measured in extracts of Succinate-grown cells.
additional information
-
cell extracts from 4-chlorophenol-grown cells deplete hydoxyquinol from the medium with an activity of 96 microM/min/mg protein. No depletion of hydroxyquinol is measured in extracts of Succinate-grown cells.
additional information
Cph-2 remove hydroxyquinol: CphA-2 = 3.0 microM/min/mg. CphA-2 show some activity with catechol: CphA-2 = 0.15 microM/min/mg.
additional information
Cph-2 remove hydroxyquinol: CphA-2 = 3.0 microM/min/mg. CphA-2 show some activity with catechol: CphA-2 = 0.15 microM/min/mg.
additional information
-
Cph-2 remove hydroxyquinol: CphA-2 = 3.0 microM/min/mg. CphA-2 show some activity with catechol: CphA-2 = 0.15 microM/min/mg.
additional information
CphA-1 remove hydroxyquinol: CphA-1 = 16 microM/min/mg. CphA-1 show some activity with catechol: CphA-1 = 0.67 microM/min/mg.
additional information
CphA-1 remove hydroxyquinol: CphA-1 = 16 microM/min/mg. CphA-1 show some activity with catechol: CphA-1 = 0.67 microM/min/mg.
additional information
-
CphA-1 remove hydroxyquinol: CphA-1 = 16 microM/min/mg. CphA-1 show some activity with catechol: CphA-1 = 0.67 microM/min/mg.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
metabolism
-
the enzyme is involved in degradation of 4-nitrophenol, the catabolism proceeds via two different intermediates, hydroquinone and 4-nitrocatechol, resulting in formation of maleylacetate. Hydroxyquinol 1,2-dioxygenase catalyzes the formation of maleylacetate from hydroxyquinol inthe route via 4-nitrocatechol, overview
metabolism
-
the enzyme is involved in degradation of 4-nitrophenol, the catabolism proceeds via two different intermediates, hydroquinone and 4-nitrocatechol, resulting in formation of maleylacetate. Hydroxyquinol 1,2-dioxygenase catalyzes the formation of maleylacetate from hydroxyquinol inthe route via 4-nitrocatechol, overview
-
physiological function
decomposition of aromatic hydrocarbon intermediates by recombinant hydroxyquinol 1,2-dioxygenase. Substrate hydroxyquinol is an intermediate found in the central pathway of biodegradation of various aromatic compounds by yeast, fungi, and bacteria
physiological function
Rhodococcus oxybenzonivorans
-
presence of a benzophenone-3 catabolic gene cluster including cytochrome P450, flavin-dependent oxidoreductase, hydroxyquinol 1,2-dioxygenase, maleylacetate reductase, and alpha/beta hydrolase genes. The strain degrades benzophenone-3 using a catabolic pathway that progresses via the intermediates benzophenone-1, 2,4,5-trihydroxy-benzophenone, 3-hydroxy-4-benzoyl-2,4-hexadienedioic acid, 4-benzoyl-3-oxoadipic acid, 3-oxoadipic acid, and benzoic acid
physiological function
-
decomposition of aromatic hydrocarbon intermediates by recombinant hydroxyquinol 1,2-dioxygenase. Substrate hydroxyquinol is an intermediate found in the central pathway of biodegradation of various aromatic compounds by yeast, fungi, and bacteria
-
additional information
-
three-dimensional enzyme structure homology modeling using structure PDB ID 1TMXA as template, overview
additional information
three-dimensional enzyme structure homology modeling using structure PDB ID 1TMXA as template, overview
additional information
-
three-dimensional enzyme structure homology modeling using structure PDB ID 1TMXA as template, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Sparnins, V.L.; Burbee, D.G.; Dagley, S.
Catabolism of L-tyrosine in Trichosporon cutaneum
J. Bacteriol.
138
425-430
1979
Cutaneotrichosporon cutaneum
brenda
Daubaras, D.L.; Saido, K.; Chakrabarty, A.M.
Purification of hydroxyquinol 1,2-dioxygenase and maleylacetate reductase: the lower pathway of 2,4,5-trichlorophenoxyacetic acid metabolism by Burkholderia cepacia AC1100
Appl. Environ. Microbiol.
62
4276-4279
1996
Burkholderia cepacia
brenda
Buswell, J.A.; Eriksson, K.E.; Gupta, J.K.; Hamp, S.G.; Nordh, I.
Vanillic acid metabolism by selected soft-rot, brown-rot, and white-rot fungi
Arch. Microbiol.
131
366-374
1982
Daedalea quercina, Fomes pinicola, Lenzites trabea, Vitreoporus dichrous, Poria ambigua, Trametes cinnabarina
-
brenda
Boominathan, K.; Mahadevan, A.
Dissimilation of aromatic substances by fungi
Zentralbl. Mikrobiol.
144
37-45
1989
Arcopilus cupreus, Bipolaris oryzae, Fusarium oxysporum
-
brenda
Sze, I.S.Y.; Dagley, S.
Properties of salicylate hydroxylase and hydroxyquinol 1,2-dioxygenase purified from Trichosporon cutaneum
J. Bacteriol.
159
353-359
1984
Cutaneotrichosporon cutaneum
brenda
Buswell, J.A.; Eriksson, K.E.
Aromatic ring cleavage by the white-rot fungus Sporotrichum pulverulentum
FEBS Lett.
104
258-260
1979
Sporotrichum pulverulentum
-
brenda
Zaborina, O.; Latus, M.; Eberspaecher, J.; Golovleva, L.A.; Lingens, F.
Purification and characterization of 6-chlorohydroxyquinol 1,2-dioxygenase from Streptomyces rochei 303: comparison with an analogous enzyme from Azotobacter sp. strain GP1
J. Bacteriol.
177
229-234
1995
Streptomyces rochei, Streptomyces rochei DSM 40242
brenda
Latus, M.; Seitz, H.J.; Eberspaecher, J.; Lingens, F.
Purification and characterization of hydroxyquinol 1,2-dioxygenase from Azotobacter sp. strain GP1
Appl. Environ. Microbiol.
61
2453-2460
1995
Azotobacter sp., Azotobacter sp. GP1 / DSM 6428 / ATCC 49806
brenda
Zaborina, O.; Seitz, H.J.; Sidorov, I.; Eberspaecher, J.; Alexeeva, E.; Golovleva, L.; Lingens, F.
Inhibition analysis of hydroxyquinol-cleaving dioxygenases from the chlorophenol-degrading Azotobacter sp. GP1 and Streptomyces rochei 303
J. Basic Microbiol.
39
61-73
1999
Azotobacter sp., Streptomyces rochei, Streptomyces rochei DSM 40242, Azotobacter sp. GP1 / DSM 6428 / ATCC 49806
-
brenda
Murakami, S.; Okuno, T.; Matsumura, E.; Takenaka, S.; Shinke, R.; Aoki, K.
Cloning of a gene encoding hydroxyquinol 1,2-dioxygenase that catalyzes both intradiol and extradiol ring cleavage of catechol
Biosci. Biotechnol. Biochem.
63
859-865
1999
Arthrobacter sp. (Q9S1B4)
brenda
Benvenuti, M.; Briganti, F.; Scozzafava, A.; Golovleva, L.; Travkin, V.M.; Mangani, S.
Crystallization and preliminary crystallographic analysis of the hydroxyquinol 1,2-dioxygenase from Nocardioides simplex 3E: a novel dioxygenase involved in the biodegradation of polychlorinated aromatic compounds
Acta Crystallogr. Sect. D
55
901-903
1999
Pimelobacter simplex, Pimelobacter simplex 3E
-
brenda
Kitagawa, W.; Kimura, N.; Kamagata, Y.
A novel p-nitrophenol degradation gene cluster from a gram-positive bacterium, Rhodococcus opacus SAO101
J. Bacteriol.
186
4894-4902
2004
Rhodococcus opacus, Rhodococcus opacus SAO101
brenda
Ferraroni, M.; Seifert, J.; Travkin, V.M.; Thiel, M.; Kaschabek, S.; Scozzafava, A.; Golovleva, L.; Schlomann, M.; Briganti, F.
Crystal structure of the hydroxyquinol 1,2-dioxygenase from Nocardioides simplex 3E, a key enzyme involved in polychlorinated aromatics biodegradation
J. Biol. Chem.
280
21144-21154
2005
Pimelobacter simplex (Q5PXQ6), Pimelobacter simplex 3E (Q5PXQ6)
brenda
Nordin, K.; Unell, M.; Jansson, J.K.
Novel 4-chlorophenol degradation gene cluster and degradation route via hydroxyquinol in Arthrobacter chlorophenolicus A6
Appl. Environ. Microbiol.
71
6538-6544
2005
Pseudarthrobacter chlorophenolicus A6 (Q3BEM2), Pseudarthrobacter chlorophenolicus A6 (Q3BEN0), Pseudarthrobacter chlorophenolicus A6
brenda
Unell, M.; Nordin, K.; Jernberg, C.; Stenstrm, J.; Jansson, J.
Degradation of mixtures of phenolic compounds by Arthrobacter chlorophenolicus A6
Biodegradation
19
495-505
2008
Pseudarthrobacter chlorophenolicus, Pseudarthrobacter chlorophenolicus A6 / DSM 12829
brenda
Dong, X.; Hong, Q.; Li, L.; Li, S.
Characterization of a p-nitrophenol degrading bacterium Pseudomonas sp. PDS-7 and cloning of degradation relevant genes
Wei Sheng Wu Xue Bao
48
1486-1492
2008
Pseudomonas sp., Pseudomonas sp. PDS-7
brenda
Wei, M.; Zhang, J.J.; Liu, H.; Zhou, N.Y.
para-Nitrophenol 4-monooxygenase and hydroxyquinol 1,2-dioxygenase catalyze sequential transformation of 4-nitrocatechol in Pseudomonas sp. strain WBC-3
Biodegradation
21
915-921
2010
Pseudomonas sp.
brenda
Zhang, S.; Sun, W.; Xu, L.; Zheng, X.; Chu, X.; Tian, J.; Wu, N.; Fan, Y.
Identification of the para-nitrophenol catabolic pathway, and characterization of three enzymes involved in the hydroquinone pathway, in Pseudomonas sp. 1-7
BMC Microbiol.
12
27
2012
Pseudomonas sp., Pseudomonas sp. 1-7
brenda
Kwon, D.; Suma, Y.; Tiwari, M.; Choi, J.; Kang, L.; Lee, J.; Kim, H.
Decomposition of aromatic hydrocarbon intermediates by recombinant hydroxyquinol 1,2-dioxygenase from Arthrobacter chlorophenolicus A6 and its structure characterization
Int. Biodeter. Biodegrad.
95
67-75
2014
Pseudarthrobacter chlorophenolicus, Pseudarthrobacter chlorophenolicus (Q3BEM2), Pseudarthrobacter chlorophenolicus A6 / DSM 12829, Pseudarthrobacter chlorophenolicus A6 / DSM 12829 (Q3BEM2)
-
brenda
Huang, Y.; Duan, Y.; Zhang, Y.; Fan, P.; Li, Z.; Liu, W.; Cui, Z.
Crystal structure of hydroxyquinol 1,2-dioxygenase PnpC from Pseudomonas putida DLL-E4 and its role of N-terminal domain for catalysis
Biochem. Biophys. Res. Commun.
507
267-273
2018
Pseudomonas putida (C6FI44)
brenda
Baek, J.H.; Kim, K.H.; Lee, Y.; Jeong, S.E.; Jin, H.M.; Jia, B.; Jeon, C.O.
Elucidating the biodegradation pathway and catabolic genes of benzophenone-3 in Rhodococcus sp. S2-17
Environ. Pollut.
299
118890
2022
Rhodococcus oxybenzonivorans
brenda