Information on EC 1.13.11.66 - hydroquinone 1,2-dioxygenase

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The enzyme appears in viruses and cellular organisms

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EC NUMBER
COMMENTARY hide
1.13.11.66
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RECOMMENDED NAME
GeneOntology No.
hydroquinone 1,2-dioxygenase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
benzene-1,4-diol + O2 = (2Z,4E)-4-hydroxy-6-oxohexa-2,4-dienoate
show the reaction diagram
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-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Chlorocyclohexane and chlorobenzene degradation
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Microbial metabolism in diverse environments
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4-nitrophenol degradation I
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4-hydroxyacetophenone degradation
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SYSTEMATIC NAME
IUBMB Comments
benzene-1,4-diol:oxygen 1,2-oxidoreductase (decyclizing)
The enzyme is an extradiol-type dioxygenase, and is a member of the nonheme-iron(II)-dependent dioxygenase family. It catalyses the ring cleavage of a wide range of hydroquinone substrates to produce the corresponding 4-hydroxymuconic semialdehydes.
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
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Manually annotated by BRENDA team
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2,3-difluorohydroquinone + O2
?
show the reaction diagram
2,5-difluorohydroquinone + O2
?
show the reaction diagram
2,6-dibromohydroquinone + O2
2-bromomaleylacetate + Br-
show the reaction diagram
-
-
-
?
2,6-dichloro-p-hydroquinone + O2
2-chloromaleylacetate + Cl-
show the reaction diagram
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-
-
?
2,6-dichlorohydroquinone + O2
2-chloromaleylacetate + Cl-
show the reaction diagram
complete conversion of substrate
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-
?
2,6-dichlorohydroquinone + O2
?
show the reaction diagram
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0.5-0.6 equiv. of chloride is released during turnover of substrate
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?
2,6-dimethylhydroquinone + O2
2-methylmaleylacetone + ?
show the reaction diagram
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-
-
?
2-(1-methyl1-octyl)-hydroquinone + O2
?
show the reaction diagram
2-chloro-6-methylhydroquinone
?
show the reaction diagram
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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
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?
2-chlorohydroquinone + O2
?
show the reaction diagram
2-ethylhydroquinone + O2
?
show the reaction diagram
2-hexylhydroquinone + O2
?
show the reaction diagram
2-methoxyhydroquinone + O2
?
show the reaction diagram
59% of the activity with hydroquinone
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-
?
2-methylhydroquinone + O2
?
show the reaction diagram
139% of the activity with hydroquinone
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-
?
2-pentylhydroquinone + O2
?
show the reaction diagram
19% of the activity with hydroquinone
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-
?
2-propylhydroquinone + O2
?
show the reaction diagram
23% of the activity with hydroquinone
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-
?
2-tert-butylhydroquinone + O2
?
show the reaction diagram
5% of the activity with hydroquinone
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-
?
3,5-difluorohydroquinone + O2
?
show the reaction diagram
bromohydroquinone + O2
?
show the reaction diagram
bromohydroquinone + O2
maleylacetate + Br-
show the reaction diagram
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-
-
?
chlorohydroquinone + O2
?
show the reaction diagram
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70% of the activity with hydroquinone
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?
chlorohydroquinone + O2
maleylacetate + Cl-
show the reaction diagram
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-
-
?
hydroquinone + O2
4-hydroxymuconic acid semialdehyde
show the reaction diagram
hydroquinone + O2
4-hydroxymuconic semialdehyde
show the reaction diagram
hydroquinone + O2
gamma-hydroxymuconic acid semialdehyde
show the reaction diagram
methoxyhydroquinone + O2
?
show the reaction diagram
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50% of the activity with hydroquinone
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?
methylhydroquinone + O2
?
show the reaction diagram
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120% of the activity with hydroquinone
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?
methylhydroquinone + O2
maleylacetone + ?
show the reaction diagram
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?
additional information
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Manganese
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preincubation in presence of 0.1 mM Fe2+ and 1 mM Mn2+ increases activity by 10fold
additional information
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Fe3+, Mn2+, Cu+, Cu2+ do not support enzyme activity
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,2'-dipyridyl
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inactivation
2,6-dibromophenol
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competitive
3,4-dihydroxybenzoate
0.2 mM, 94% inhibition; 0.2 mM, 94% inhibition
3-bromocatechol
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inactivation
4-coumaric acid
0.2 mM, 97% inhibition; 0.2 mM, 97% inhibition
4-hydroxybenzoate
4-Hydroxybenzonitrile
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0.2 mM, no residual activity
4-hydroxycinnamate
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0.2 mM, no residual activity
4-nitrophenol
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0.2 mM, no residual activity
bromohydroquinone
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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
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substrate inhibition
hydrogen peroxide
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inactivation
Hydroxyhydroquinone
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0.2 mM, 9% residual activity
methoxyhydroquinone
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strong substrtae inhibition
o-phenanthroline
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inactivation
ortho-disubstituted phenols
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-
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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
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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
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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ligandation with 4-hydroxybenzoate prevents the enzyme from irreversible inactivation
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0013
2,6-dibromohydroquinone
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pH 7.0, 23°C
0.0135
2,6-dichloro-p-hydroquinone
pH 6.7, 22°C
0.0032
2,6-dichlorohydroquinone
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pH 7.0, 23°C
0.055
2,6-dimethylhydroquinone
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pH 7.0, 23°C
0.0044
2-chloro-6-methylhydroquinone
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pH 7.0, 23°C
0.0085
bromohydroquinone
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pH 7.0, 23°C
0.01
chlorohydroquinone
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pH 7.0, 23°C
0.0022 - 0.255
hydroquinone
0.041
methylhydroquinone
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pH 7.0, 23°C
0.021 - 0.26
O2
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.61
2,6-dibromohydroquinone
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pH 7.0, 23°C
2.1
2,6-dichloro-p-hydroquinone
pH 6.7, 22°C
3.05
2,6-dichlorohydroquinone
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pH 7.0, 23°C
1.25
2,6-dimethylhydroquinone
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pH 7.0, 23°C
2.41
2-chloro-6-methylhydroquinone
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pH 7.0, 23°C
2.1 - 13.5
hydroquinone
1.4 - 4.8
O2
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1200
2,6-dibromohydroquinone
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pH 7.0, 23°C
1000
2,6-dichlorohydroquinone
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pH 7.0, 23°C
23
2,6-dimethylhydroquinone
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pH 7.0, 23°C
540
2-chloro-6-methylhydroquinone
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pH 7.0, 23°C
6136
hydroquinone
pH 7.0, 25°C; pH 7.0, 25°C
0.7 - 26
O2
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.014
4-hydroxybenzoate
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pH 7.0, 25°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.27
crude extract, substrate hydroquinone, pH 7.0, 37°C
0.88
crude extract, substrate 2-chlorohydroquinone, pH 7.0, 37°C
3.1
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pH 7.4, temperature not specified in the publication
5.89
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pH 7.0, 25°C
6.1
pH 7.0, 25°C; pH 7.0, 25°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.7
optimal in 20 mM potassium phosphate buffer
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3 - 10
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7
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20% of maximum activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 70
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-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
17800
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2 * 17800, alpha-subunit, + 2 * 38300, beta-subunit
18000
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SDS-PAGE
34000
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x * 34000, SDS-PAGE
36000
x * 36000, SDS-PAGE
36522
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x * 36522, electrospray LC-MS
38300
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2 * 17800, alpha-subunit, + 2 * 38300, beta-subunit
112000
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gel filtration
120000
gel filtration; gel filtration
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
generation of a homology model, based on zinc protein PDB entry 1ZSW, which predicts that the tertiary structure of the enzyme differs significantly from that of the extradiol dioxygenases, and that the residues ligating the Fe(II) are H11, H227, and E276
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3
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20% activity after 30 min at pH 3.0
719179
10
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60% activity after 30 min at pH 10.0
719179
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
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the purified enzyme retains 35% activity after 20 min at 60°C
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 50% glycerol, 48% residual activity after 30 days
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-70°C, 50% glycerol, 77% residual activity after 30 days
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fairly stable for several hours on ice and retains approximately 80% of activity after 72 h
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ligandation with 4-hydroxybenzoate prevents the enzyme from irreversible inactivation
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using Ni-NTA chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli as His-tagged fusion proteins
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expression in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
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LITERATURE
E276A
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less than 6% of wild-type activity
H11A
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less than 6% of wild-type activity
H159A
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67% of wild-type activity
H227A
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less than 6% of wild-type activity
Y266F
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about 6% of wild-type activity
E278A
mutation in putative Fe(II)-binding site, complete loss of activity
H162A
mutation in putative Fe(II)-binding site, complete loss of activity
H229A
mutation in putative Fe(II)-binding site, complete loss of activity
additional information
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LINKS TO OTHER DATABASES (specific for EC-Number 1.13.11.66)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)