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Information on EC 1.13.11.66 - hydroquinone 1,2-dioxygenase
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1.13.11.66 hydroquinone 1,2-dioxygenaseIUBMB Comments
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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Word Map
- 1.13.11.66
- semialdehyde
- sphingomonas
- para-nitrophenol
-
4-monooxygenase
- maleylacetate
-
fission
- methylhydroquinone
- heterotetramer
- chlorohydroquinone
- burkholderia
- 4-hydroxybenzoate
- 2-chloro-4-nitrophenol
- fluorescens
- p-benzoquinone
-
wastewater
-
catecholic
-
alkylphenols
-
sensu
-
cupin
-
ironii
-
monooxygenation
- sludge
- 1,4-benzoquinone
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
pnpcd, hydroquinone dioxygenase, hydroquinone 1,2-dioxygenase, two-subunit hydroquinone 1,2-dioxygenase, pnpc2, pnpc1, pdcde, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
HQDO
hydroquinone 1,2-dioxygenase
hydroquinone dioxygenase
mnpC
PnpC1
PnpC2
type II HQDO
YaiA
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
benzene-1,4-diol + O2 = (2Z,4E)-4-hydroxy-6-oxohexa-2,4-dienoate
-
-
-
-
benzene-1,4-diol + O2 = (2Z,4E)-4-hydroxy-6-oxohexa-2,4-dienoate
catalytic mechanism, overview
benzene-1,4-diol + O2 = (2Z,4E)-4-hydroxy-6-oxohexa-2,4-dienoate
catalytic mechanism, overview
-
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PATHWAY SOURCE
PATHWAYS
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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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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
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-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-methoxyhydroquinone + O2
?
59% 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
-
?
chlorohydroquinone + O2
?
-
70% of the activity with hydroquinone
-
?
methoxyhydroquinone + O2
?
-
50% of the activity with hydroquinone
-
?
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
-
?
2-methylhydroquinone + O2
?
139% 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
-
?
benzene-1,4-diol + O2
(2Z,4E)-4-hydroxy-6-oxohexa-2,4-dienoate
-
-
-
?
benzene-1,4-diol + O2
(2Z,4E)-4-hydroxy-6-oxohexa-2,4-dienoate
C1I210; C1I209
-
-
?
benzene-1,4-diol + O2
(2Z,4E)-4-hydroxy-6-oxohexa-2,4-dienoate
-
-
?
benzene-1,4-diol + O2
(2Z,4E)-4-hydroxy-6-oxohexa-2,4-dienoate
-
-
?
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
consumption of an equimolar amount of molecular oxygen
-
?
hydroquinone + O2
gamma-hydroxymuconic acid semialdehyde
-
-
?
hydroquinone + O2
gamma-hydroxymuconic acid semialdehyde
-
-
?
methylhydroquinone + O2
?
-
120% of the activity with hydroquinone
-
?
methylhydroquinone + O2
?
substrate binding structure, overview
-
?
methylhydroquinone + O2
?
substrate binding structure, overview
-
?
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
?
-
-
YaiA is a hydroquinone dioxygenase that converts hydroquinone putatively to 4-hydroxymuconic semialdehyde in an oxygen-consuming reaction. Hydroquinone and methylhydroquinone are both substrates of YaiA
-
?
additional information
?
-
-
2-methylhydroquinone is a slightly better substrate than unsubstituted hydroquinone
-
?
additional information
?
-
-
YaiA is a hydroquinone dioxygenase that converts hydroquinone putatively to 4-hydroxymuconic semialdehyde in an oxygen-consuming reaction. Hydroquinone and methylhydroquinone are both substrates of YaiA
-
?
additional information
?
-
-
2-methylhydroquinone is a slightly better substrate than unsubstituted hydroquinone
-
?
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
?
-
hydroquinone 1,2-dioxygenase, a Fe(II) ring cleaving dioxygenase from Sphingomonas sp. strain TTNP3, oxidizes a wide range of hydroquinones to the corresponding 4-hydroxymuconic semialdehydes
-
?
additional information
?
-
-
hydroquinone 1,2-dioxygenase, a Fe(II) ring cleaving dioxygenase from Sphingomonas sp. strain TTNP3, oxidizes a wide range of hydroquinones to the corresponding 4-hydroxymuconic semialdehydes
-
?
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
?
-
hydroquinone 1,2-dioxygenase, a Fe(II) ring cleaving dioxygenase from Sphingomonas sp. strain TTNP3, oxidizes a wide range of hydroquinones to the corresponding 4-hydroxymuconic semialdehydes
-
?
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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
benzene-1,4-diol + O2
(2Z,4E)-4-hydroxy-6-oxohexa-2,4-dienoate
-
-
-
-
?
benzene-1,4-diol + O2
(2Z,4E)-4-hydroxy-6-oxohexa-2,4-dienoate
C1I210; C1I209
-
-
-
?
benzene-1,4-diol + O2
(2Z,4E)-4-hydroxy-6-oxohexa-2,4-dienoate
-
-
-
?
benzene-1,4-diol + O2
(2Z,4E)-4-hydroxy-6-oxohexa-2,4-dienoate
-
-
-
?
additional information
?
-
-
YaiA is a hydroquinone dioxygenase that converts hydroquinone putatively to 4-hydroxymuconic semialdehyde in an oxygen-consuming reaction. Hydroquinone and methylhydroquinone are both substrates of YaiA
-
-
?
additional information
?
-
-
YaiA is a hydroquinone dioxygenase that converts hydroquinone putatively to 4-hydroxymuconic semialdehyde in an oxygen-consuming reaction. Hydroquinone and methylhydroquinone are both substrates of YaiA
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
Iron
Manganese
-
preincubation in presence of 0.1 mM Fe2+ and 1 mM Mn2+ increases activity by 10fold
additional information
Fe2+
C1I210; C1I209
a Fe2+-dependent dioxygenase, selectively utilizes Fe2+for its catalytic reaction. Four residues of enzyme PnpD, His256, Asn258, Glu262, and His303, coordinate the iron ion
Fe2+
required for catalysis, each of the four beta subunits in the asymmetric unit of the enzyme crystal binds one Fe(II) ion. The iron ion in each beta subunit is coordinated to three protein residues, His258, Glu264, and His305 and a water molecule
Iron
-
preincubation in presence of 0.1 mM Fe2+ and 1 mM Mn2+ increases activity by 10fold
Iron
-
10fold activation by Fe2+, each subunit binds one molecule of 4-hydroxybenzoate and one molecule of iron
Iron
the residues ligating the Fe(II) are H11, H227, and E276
additional information
C1I210; C1I209
Fe3+, Mn2+, Co2+, Ni2+, Cu2+, and Cd2+ cannot substitute for Fe2+
additional information
-
Fe3+, Mn2+, Cu+, Cu2+ do not support enzyme activity
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3,4-dihydroxybenzoate
0.2 mM, 94% inhibition; 0.2 mM, 94% inhibition
4-coumaric acid
0.2 mM, 97% inhibition; 0.2 mM, 97% inhibition
Vanillyl alcohol
0.2 mM, 62% inhibition; 0.2 mM, 62% inhibition
4-hydroxybenzoate
0.2 mM, 46% inhibition; 0.2 mM, 46% inhibition
additional information
-
4-hydrobenzoate, the competitive inhibitor of the heterotetrameric HapCD hydroquinone dioxygenase of Pseudomonas fluorescens ACB, stabilizes the enzyme
-
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
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
ligandation with 4-hydroxybenzoate prevents the enzyme from irreversible inactivation
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.255
hydroquinone
-
pH 7.4, temperature not specified in the publication
0.021
O2
cosubstrate 2-chloro-6-methylhydroquinone, 1,2-cleavage, pH 7.0, 23°C
0.07
O2
cosubstrate 2,6-dimethylhydroquinone, pH 7.0, 23°C
0.12
O2
cosubstrate 2,6-dibromohydroquinone, pH 7.0, 23°C
0.19
O2
cosubstrate 2,6-dichlorohydroquinone, pH 7.0, 23°C
0.26
O2
cosubstrate 2-chloro-6-methylhydroquinone, 1,6-cleavage, pH 7.0, 23°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.4
O2
cosubstrate 2,6-dimethylhydroquinone, pH 7.0, 23°C
1.6
O2
cosubstrate 2-chloro-6-methylhydroquinone, 1,2-cleavage, pH 7.0, 23°C
1.8
O2
cosubstrate 2-chloro-6-methylhydroquinone, 1,6-cleavage, pH 7.0, 23°C
4.8
O2
cosubstrate 2,6-dichlorohydroquinone, pH 7.0, 23°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.7
O2
cosubstrate 2-chloro-6-methylhydroquinone, 1,6-cleavage, pH 7.0, 23°C
7
O2
cosubstrate 2-chloro-6-methylhydroquinone, 1,2-cleavage, pH 7.0, 23°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.88
crude extract, substrate 2-chlorohydroquinone, pH 7.0, 37°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
subunit C1, part of the PnpC1C2 multi-component protein complex
UniProt
brenda
subunit C2, part of the PnpC1C2 multi-component protein complex
UniProt
brenda
subunit C1, part of the PnpC1C2 multi-component protein complex
UniProt
brenda
subunit C2, part of the PnpC1C2 multi-component protein complex
UniProt
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
C1I210; C1I209
the two-subunit hydroquinone 1,2-dioxygenase PnpCD is the ring cleavage enzyme in para-nitrophenol catabolism
physiological function
additional information
physiological function
C1I210; C1I209
hydroquinone 1,2-dioxygenase PnpCD is the key enzyme in the hydroquinone pathway of para-nitrophenol degradation, catalyzes the ring cleavage of hydroquinone to gamma-hydroxymuconic semialdehyde
physiological function
-
the enzyme YaiA plays a key role in alleviating quinone/copper stress. The yahCD-yaiAB operon of Lactococcus lactis IL1403 provides resistance to combined copper/quinone stress. The operon is under the control of CopR, which also regulates expression of the copRZA copper resistance operon as well as other Lactococcus lactis genes. Expression of the yahCD-yaiAB operon is induced by copper but not by quinones. Copper induction of the yahCD-yaiAB operon offers protection to copper/quinone toxicity and can provide a growth advantage to Lactococcus lactis in some environments. Regulation of quinone degradation by CopR thus appears to be a hallmark of Lactococci. The conversion of hydroquinone to 4-hydroxymuconic semialdehyde by the YaiA dioxygenase appears to be too slow for acute detoxification, but probably serves as long-term remedy by degrading the hydroquinone pool, which constitutes a reservoir for the formation of toxic pbenzoquinones by spontaneous oxidation that is greatly accelerated by copper
physiological function
-
the enzyme YaiA plays a key role in alleviating quinone/copper stress. The yahCD-yaiAB operon of Lactococcus lactis IL1403 provides resistance to combined copper/quinone stress. The operon is under the control of CopR, which also regulates expression of the copRZA copper resistance operon as well as other Lactococcus lactis genes. Expression of the yahCD-yaiAB operon is induced by copper but not by quinones. Copper induction of the yahCD-yaiAB operon offers protection to copper/quinone toxicity and can provide a growth advantage to Lactococcus lactis in some environments. Regulation of quinone degradation by CopR thus appears to be a hallmark of Lactococci. The conversion of hydroquinone to 4-hydroxymuconic semialdehyde by the YaiA dioxygenase appears to be too slow for acute detoxification, but probably serves as long-term remedy by degrading the hydroquinone pool, which constitutes a reservoir for the formation of toxic pbenzoquinones by spontaneous oxidation that is greatly accelerated by copper
additional information
active site structure analysis, apo or with bound substrate methylhydroquinone, overview
additional information
-
active site structure analysis, apo or with bound substrate methylhydroquinone, overview
additional information
C1I210; C1I209
the PnpCD structure contains a pseudo cupin and a iron metallocenter in the catalytic PnpD, which adds to understanding of the ring cleavage mechanism of dioxygenases, structure analysis, overview
additional information
-
active site structure analysis, apo or with bound substrate methylhydroquinone, overview
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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). LINE_SPHJU
Sphingobium japonicum (strain DSM 16413 / CCM 7287 / MTCC 6362 / UT26 / NBRC 101211 / UT26S)
321
0
35958
Swiss-Prot
-
A0A1U9YWB6_9RHIZ
319
0
35414
TrEMBL
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
19000
38000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
heterotetramer
tetramer
additional information
heterotetramer
C1I210; C1I209
2 * 38300, subunit alpha, + 2 * 18000, subunit beta
heterotetramer
2 * 19000, subunit alpha, + 2 * 38000, subunit beta
additional information
C1I210; C1I209
the PnpCD structure contains a pseudo cupin and an iron metallocenter in the catalytic PnpD. Both the PnpC and the C-terminal domains of PnpD comprise a conserved cupin fold, whereas PnpC cannot form a competent metal binding pocket as can PnpD cupin, structure analysis, overview
additional information
both subunits alpha and beta fold as a cupin, but that of the small alpha subunit lacks a competent metal binding pocket. Two tetramers are present in the asymmetric unit of the enzyme crystals
additional information
-
both subunits alpha and beta fold as a cupin, but that of the small alpha subunit lacks a competent metal binding pocket. Two tetramers are present in the asymmetric unit of the enzyme crystals
additional information
-
both subunits alpha and beta fold as a cupin, but that of the small alpha subunit lacks a competent metal binding pocket. Two tetramers are present in the asymmetric unit of the enzyme crystals
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified full-length or proteolytically truncated PnpCD in apo form and in complex with Fe3+ or substrate analogue hydroxybenzonitrile and Cd2+, i.e. apo-PnpCD, PnpCD-Fe3+, and PnpCD-Cd2+-HBN, sitting-drop vapor diffusion method, 15-20 mg/ml protein in 10mM Tris-HCl, pH 8.0, and 100 mM NaCl, is mixed with reservoir solution containing 0.2 M sodium thiocyanate, 20% w/v PEG 3350, 20°C, method optimization, X-ray diffraction structure determination and analysis
C1I210; C1I209
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
purified enzyme free or in complex with substrate methylhydroquinone under anaerobic conditions, or with inhibitors 4-hydroxybenzoate and 4-nitrophenol, sitting drop vapor diffusion method, mixing of 0.001 ml of 8 mg/ml protein in 25 mM Tris, pH 7.0, 5 mM NaCl, and 0.5 mM ligand, with 0.001 ml of reservoir solution containing 14% PEG 3350, 0.35 M MgCl2, and 0.1 M MES, pH 6.5, 4°C, 1 day, the structure of the free enzyme is obtained by soaking the crystals in a stabilizing solution containing 16% PEG 3350, 0.35 M MgCl2, and 0.1 M MES, pH 6.5, for two days, changing the solution three times, in order to remove the ligands, X-ray diffraction structure determination and analysis at 1.90-2.40 resolution, molecular replacement using the coordinates of PnpCD structure from Pseudomonas sp. strain WBC-3, PDB ID 4ZXA as template, modeling
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E248Q
C1I210; C1I209
site-directed mutagenesis, the mutation results in complete loss of enzyme activity
F264A
C1I210; C1I209
site-directed mutagenesis, the mutation results in almost complete loss of enzyme activity
F79A
C1I210; C1I209
site-directed mutagenesis, the mutation results in almost complete loss of enzyme activity
L252A
C1I210; C1I209
site-directed mutagenesis, the mutation results in a 70% loss of enzyme activity
L313A
C1I210; C1I209
site-directed mutagenesis, the mutation results in almost complete loss of enzyme activity
V315A
C1I210; C1I209
site-directed mutagenesis, the mutation results in a 50% loss of enzyme activity
W230A
C1I210; C1I209
site-directed mutagenesis, the mutation results in a 70% loss of enzyme activity
W273a
C1I210; C1I209
site-directed mutagenesis, the mutation results in almost complete loss of enzyme activity
W76A
C1I210; C1I209
site-directed mutagenesis, the mutation results in almost complete loss of enzyme 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
additional information
expression of the hydroquinone dioxygenase PnpC1C2 multi-component protein complex in Escherichia coli results in conversion of hydroquinone to 4-hydroxymuconic semialdehyde
additional information
expression of the hydroquinone dioxygenase PnpC1C2 multi-component protein complex in Escherichia coli results in conversion of hydroquinone to 4-hydroxymuconic semialdehyde
additional information
-
expression of the hydroquinone dioxygenase PnpC1C2 multi-component protein complex in Escherichia coli results in conversion of hydroquinone to 4-hydroxymuconic semialdehyde
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
4-hydrobenzoate, the competitive inhibitor of the heterotetrameric HapCD hydroquinone dioxygenase of Pseudomonas fluorescens ACB, stabilizes the enzyme
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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
-
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
C1I210; C1I209
recombinant N-terminally His6-tagged enzyme from Escherichia coli by nickel affinity chromatography, tag removal by rTEV protease cleavage, over 95% purity. No enzyme activity can be detected with purified YaiA, even when it is purified in the presence of 4-hydrobenzoate
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
gene yaiA, encoded in the the yahCD-yaiAB operon, DNA and amino acid sequence determination and analysis, recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli. YaiA activity could be detected in crude Escherichia coli cytoplasmic extract overexpressing Lactcoccus lactis YaiA from a plasmid
-
genes pnpCD, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
C1I210; C1I209
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the the yahCD-yaiAB operon is induced by copper but not by quinones
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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 JMP 134-1
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
Ferraroni, M.; Da Vela, S.; Kolvenbach, B.A.; Corvini, P.F.; Scozzafava, A.
The crystal structures of native hydroquinone 1,2-dioxygenase from Sphingomonas sp. TTNP3 and of substrate and inhibitor complexes
Biochim. Biophys. Acta
1865
520-530
2017
Sphingomonas sp. (F8TW82 AND F8TW83), Sphingomonas sp., Sphingomonas sp. TTNP3 (F8TW82 AND F8TW83)
brenda
Liu, S.; Su, T.; Zhang, C.; Zhang, W.M.; Zhu, D.; Su, J.; Wei, T.; Wang, K.; Huang, Y.; Guo, L.; Xu, S.; Zhou, N.Y.; Gu, L.
Crystal structure of PnpCD, a two-subunit hydroquinone 1,2-dioxygenase, reveals a novel structural class of Fe2+-dependent dioxygenases
J. Biol. Chem.
290
24547-24560
2015
Pseudomonas sp. (C1I210 AND C1I209)
brenda
Mancini, S.; Abicht, H.K.; Gonskikh, Y.; Solioz, M.
A copper-induced quinone degradation pathway provides protection against combined copper/quinone stress in Lactococcus lactis IL1403
Mol. Microbiol.
95
645-659
2015
Lactococcus lactis, Lactococcus lactis IL1403
brenda
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