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2,3-difluorohydroquinone + O2
?
2,5-difluorohydroquinone + O2
?
2,6-dibromohydroquinone + O2
2-bromomaleylacetate + Br-
-
-
-
?
2,6-dichloro-p-hydroquinone + O2
2-chloromaleylacetate + Cl-
-
-
-
?
2,6-dichlorohydroquinone + O2
2-chloromaleylacetate + Cl-
complete conversion of substrate
-
-
?
2,6-dichlorohydroquinone + O2
?
-
-
0.5-0.6 equiv. of chloride is released during turnover of substrate
-
?
2,6-dimethylhydroquinone + O2
2-methylmaleylacetone + ?
-
-
-
?
2-(1-methyl1-octyl)-hydroquinone + O2
?
2-chloro-6-methylhydroquinone
?
-
complete conversion of substrate, yields a mixture of 1,2- and 1,6-cleavage products. The two modes of cleavage have different Km values for oxygen, consistent with a mechanism in which the substrate binds in two catalytically productive orientations
-
?
2-chlorohydroquinone + O2
?
2-ethylhydroquinone + O2
?
2-hexylhydroquinone + O2
?
2-methoxyhydroquinone + O2
?
59% of the activity with hydroquinone
-
-
?
2-methylhydroquinone + O2
?
139% of the activity with hydroquinone
-
-
?
2-pentylhydroquinone + O2
?
19% of the activity with hydroquinone
-
-
?
2-propylhydroquinone + O2
?
23% of the activity with hydroquinone
-
-
?
2-tert-butylhydroquinone + O2
?
5% of the activity with hydroquinone
-
-
?
3,5-difluorohydroquinone + O2
?
bromohydroquinone + O2
maleylacetate + Br-
-
-
-
?
chlorohydroquinone + O2
?
-
70% of the activity with hydroquinone
-
-
?
chlorohydroquinone + O2
maleylacetate + Cl-
-
-
-
?
hydroquinone + O2
4-hydroxymuconic acid semialdehyde
hydroquinone + O2
4-hydroxymuconic semialdehyde
hydroquinone + O2
gamma-hydroxymuconic acid semialdehyde
methoxyhydroquinone + O2
?
-
50% of the activity with hydroquinone
-
-
?
methylhydroquinone + O2
?
-
120% of the activity with hydroquinone
-
-
?
methylhydroquinone + O2
maleylacetone + ?
-
-
-
?
additional information
?
-
2,3-difluorohydroquinone + O2

?
-
80% of the activity with hydroquinone
-
-
?
2,3-difluorohydroquinone + O2
?
-
80% of the activity with hydroquinone
-
-
?
2,5-difluorohydroquinone + O2

?
-
75% of the activity with hydroquinone
-
-
?
2,5-difluorohydroquinone + O2
?
-
75% of the activity with hydroquinone
-
-
?
2-(1-methyl1-octyl)-hydroquinone + O2

?
less than 2% of the activity with hydroquinone
-
-
?
2-(1-methyl1-octyl)-hydroquinone + O2
?
less than 2% of the activity with hydroquinone
-
-
?
2-chlorohydroquinone + O2

?
-
ring cleavage product is an acylchloride, which reacts with water to give maleylacetate
-
?
2-chlorohydroquinone + O2
?
29% of the activity with hydroquinone
-
-
?
2-chlorohydroquinone + O2
?
29% of the activity with hydroquinone
-
-
?
2-ethylhydroquinone + O2

?
83% of the activity with hydroquinone
-
-
?
2-ethylhydroquinone + O2
?
83% of the activity with hydroquinone
-
-
?
2-hexylhydroquinone + O2

?
less than 2% of the activity with hydroquinone
-
-
?
2-hexylhydroquinone + O2
?
less than 2% of the activity with hydroquinone
-
-
?
3,5-difluorohydroquinone + O2

?
-
90% of the activity with hydroquinone
-
-
?
3,5-difluorohydroquinone + O2
?
-
90% of the activity with hydroquinone
-
-
?
bromohydroquinone + O2

?
-
30% of the activity with hydroquinone
-
-
?
bromohydroquinone + O2
?
-
30% of the activity with hydroquinone
-
-
?
hydroquinone + O2

4-hydroxymuconic acid semialdehyde
-
-
-
-
?
hydroquinone + O2
4-hydroxymuconic acid semialdehyde
-
-
-
-
?
hydroquinone + O2
4-hydroxymuconic acid semialdehyde
-
-
-
?
hydroquinone + O2
4-hydroxymuconic acid semialdehyde
consumption of an equimolar amount of molecular oxygen
-
-
?
hydroquinone + O2

4-hydroxymuconic semialdehyde
-
-
-
-
?
hydroquinone + O2
4-hydroxymuconic semialdehyde
-
-
-
-
?
hydroquinone + O2
4-hydroxymuconic semialdehyde
-
-
-
-
?
hydroquinone + O2

gamma-hydroxymuconic acid semialdehyde
-
-
-
?
hydroquinone + O2
gamma-hydroxymuconic acid semialdehyde
-
-
-
?
additional information

?
-
-
no substrate: hydroxyquinol, catechol, 2-aminophenol,4-aminophenol, protocatechuate, and gentisate
-
-
-
additional information
?
-
-
no substrate: hydroxyquinol, catechol, 2-aminophenol,4-aminophenol, protocatechuate, and gentisate
-
-
-
additional information
?
-
-
no substrate: tetrafluorohydroquinone, 1,2,4-trihydroxybenzene, gentisate, catechol, resorcinol, pyrogallol, and phenol
-
-
-
additional information
?
-
-
no substrate: tetrafluorohydroquinone, 1,2,4-trihydroxybenzene, gentisate, catechol, resorcinol, pyrogallol, and phenol
-
-
-
additional information
?
-
exhibits a high degree of substrate specificity for 2,6-disubstituted hydroquinones, with halogens greatly preferred at those positions. The asymmetric substrate 2-chloro-6-methylhydroquinone yields a mixture of 87% 1,2-cleavage and 13% 1,6-cleavage products with different Km values for oxygen, consistent with a mechanism in which the substrate binds in two catalytically productive orientations. Monosubstituted hydroquinones show a limited amount of ring cleavage but rapidly inactivate the enzyme in an O2-dependent fashion, suggesting that oxidation of the Fe(II) may be the cause
-
-
-
additional information
?
-
no substrates: 2,5-dichloro-p-hydroquinone, 6-chlorohydroxyquinol, hydroxyquinol, 2-chloro-p-hydroquinone, catechol, and 4-fluorocatechol
-
-
-
additional information
?
-
enzyme cleaves aromatic rings with two hydroxyl groups ar para positions preferably. No substrate: catechol
-
-
-
additional information
?
-
enzyme catalyzes the ring fission of hydroquinone to 4-hydroxymuconic semialdehyde and the degradation of chlorinated and several alkylated hydroquinones
-
-
-
additional information
?
-
enzyme catalyzes the ring fission of hydroquinone to 4-hydroxymuconic semialdehyde and the degradation of chlorinated and several alkylated hydroquinones
-
-
-
additional information
?
-
-
enzyme catalyzes the ring fission of hydroquinone to 4-hydroxymuconic semialdehyde and the degradation of chlorinated and several alkylated hydroquinones
-
-
-
additional information
?
-
enzyme catalyzes the ring fission of hydroquinone to 4-hydroxymuconic semialdehyde and the degradation of chlorinated and several alkylated hydroquinones
-
-
-
additional information
?
-
enzyme catalyzes the ring fission of hydroquinone to 4-hydroxymuconic semialdehyde and the degradation of chlorinated and several alkylated hydroquinones
-
-
-
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2,2'-dipyridyl
-
inactivation
2,6-dibromophenol
-
competitive
3,4-dihydroxybenzoate
0.2 mM, 94% inhibition; 0.2 mM, 94% inhibition
3-bromocatechol
-
inactivation
4-coumaric acid
0.2 mM, 97% inhibition; 0.2 mM, 97% inhibition
4-Hydroxybenzonitrile
-
0.2 mM, no residual activity
4-hydroxycinnamate
-
0.2 mM, no residual activity
4-nitrophenol
-
0.2 mM, no residual activity
bromohydroquinone
-
substrate inhibition
caffeic acid
0.2 mM, 98% inhibition; 0.2 mM, 98% inhibition
catechol
0.2 mM, 93% inhibition; 0.2 mM, 93% inhibition
chlorohydroquinone
-
substrate inhibition
hydrogen peroxide
-
inactivation
Hydroxyhydroquinone
-
0.2 mM, 9% residual activity
methoxyhydroquinone
-
strong substrtae inhibition
o-phenanthroline
-
inactivation
ortho-disubstituted phenols
-
-
-
phenol
0.2 mM, 98% inhibition; 0.2 mM, 98% inhibition
resorcinol
0.2 mM, 99% inhibition; 0.2 mM, 99% inhibition
vanillate
0.2 mM, 86% inhibition; 0.2 mM, 86% inhibition
Vanillyl alcohol
0.2 mM, 62% inhibition; 0.2 mM, 62% inhibition
additional information
-
weak or no inhibition: 2-hydroxy-, 3-hydroxy-, 2,3-dihydroxy-, 2,5-dihydroxy-, 2,6-dihydroxy-, 3,4-dihydroxy-, 3,4,5-trihydroxy-, 3-chloro-4-hydroxy-, tetrafluoro-4-hydroxy-, 3-amino-4-hydroxy-, 4-hydroxy-3-methoxy-, 4-amino- and methyl 4-hydroxybenzoate; 6-hydroxynicotinate, 4-hydroxypropiophenone, 4-hydroxymandelate, 4-hydroxyphenylglycine, 4-hydroxybenzenesulfonic acid, and 4-methyl-, 4-methoxy-, and 4-aminophenol
-
4-hydroxybenzoate

-
competitive with hydroquinone
4-hydroxybenzoate
0.2 mM, 46% inhibition; 0.2 mM, 46% inhibition
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Kolvenbach, B.A.; Lenz, M.; Benndorf, D.; Rapp, E.; Fousek, J.; Vlcek, C.; Schaeffer, A.; Gabriel, F.L.; Kohler, H.P.; Corvini, P.F.
Purification and characterization of hydroquinone dioxygenase from Sphingomonas sp. strain TTNP3
AMB Express
1
08
2011
Sphingomonas sp. (F8TW82), Sphingomonas sp. (F8TW83), Sphingomonas sp., Sphingomonas sp. TTNP3 (F8TW82), Sphingomonas sp. TTNP3 (F8TW83)
brenda
Xun, L.; Bohuslavek, J.; Cai, M.
Characterization of 2,6-dichloro-p-hydroquinone 1,2-dioxygenase (PcpA) of Sphingomonas chlorophenolica ATCC 39723
Biochem. Biophys. Res. Commun.
266
322-325
1999
Sphingobium chlorophenolicum (Q9ZBB0)
brenda
Xu, L.; Resing, K.; Lawson, S.; Babbitt, P.; Copley, S.
Evidence that pcpA encodes 2,6-dichlorohydroquinone dioxygenase, the ring cleavage enzyme required for pentachlorophenol degradation in Sphingomonas chlorophenolica strain ATCC 39723
Biochemistry
38
7659-7669
1999
Sphingobium chlorophenolicum
brenda
Machonkin, T.E.; Doerner, A.E.
Substrate specificity of Sphingobium chlorophenolicum 2,6-dichlorohydroquinone 1,2-dioxygenase
Biochemistry
50
8899-8913
2011
Sphingobium chlorophenolicum (Q9ZBB0)
brenda
Shen, W.; Liu, W.; Zhang, J.; Tao, J.; Deng, H.; Cao, H.; Cui, Z.
Cloning and characterization of a gene cluster involved in the catabolism of p-nitrophenol from Pseudomonas putida DLL-E4
Biores. Technol.
101
7516-7522
2010
Pseudomonas putida (C6FI40), Pseudomonas putida (C6FI41), Pseudomonas putida DLL-E4 (C6FI40), Pseudomonas putida DLL-E4 (C6FI41), Pseudomonas putida DLL-E4
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.
brenda
Yin, Y.; Zhou, N.Y.
Characterization of MnpC, a hydroquinone dioxygenase likely involved in the meta-nitrophenol degradation by Cupriavidus necator JMP134
Curr. Microbiol.
61
471-476
2010
Cupriavidus necator, Cupriavidus necator JMP134
brenda
Miyauchi, K.; Adachi, Y.; Nagata, Y.; Takagi, M.
Cloning and sequencing of a novel meta-cleavage dioxygenase gene whose product is involved in degradation of gamma-hexachlorocyclohexane in Sphingomonas paucimobilis
J. Bacteriol.
181
6712-6719
1999
Sphingomonas paucimobilis (Q9WXE6)
brenda
Moonen, M.J.; Synowsky, S.A.; van den Berg, W.A.; Westphal, A.H.; Heck, A.J.; van den Heuvel, R.H.; Fraaije, M.W.; van Berkel, W.J.
Hydroquinone dioxygenase from Pseudomonas fluorescens ACB: a novel member of the family of nonheme-iron(II)-dependent dioxygenases
J. Bacteriol.
190
5199-5209
2008
Pseudomonas fluorescens, Pseudomonas fluorescens ACB
brenda
Machonkin, T.E.; Holland, P.L.; Smith, K.N.; Liberman, J.S.; Dinescu, A.; Cundari, T.R.; Rocks, S.S.
Determination of the active site of Sphingobium chlorophenolicum 2,6-dichlorohydroquinone dioxygenase (PcpA)
J. Biol. Inorg. Chem.
15
291-301
2010
Sphingobium chlorophenolicum (Q9ZBB0)
brenda