1.13.11.66: hydroquinone 1,2-dioxygenase
This is an abbreviated version!
For detailed information about hydroquinone 1,2-dioxygenase, go to the full flat file.
Word Map on EC 1.13.11.66
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1.13.11.66
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semialdehyde
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sphingomonas
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para-nitrophenol
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4-monooxygenase
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methylhydroquinone
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fission
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maleylacetate
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heterotetramer
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monooxygenation
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catecholic
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alkylphenols
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p-benzoquinone
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burkholderia
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wastewater
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chlorohydroquinone
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fluorescens
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1,4-benzoquinone
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4-hydroxybenzoate
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sludge
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ironii
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sensu
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cupin
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2-chloro-4-nitrophenol
- 1.13.11.66
- semialdehyde
- sphingomonas
- para-nitrophenol
-
4-monooxygenase
- methylhydroquinone
-
fission
- maleylacetate
- heterotetramer
-
monooxygenation
-
catecholic
-
alkylphenols
- p-benzoquinone
- burkholderia
-
wastewater
- chlorohydroquinone
- fluorescens
- 1,4-benzoquinone
- 4-hydroxybenzoate
- sludge
-
ironii
-
sensu
-
cupin
- 2-chloro-4-nitrophenol
Reaction
Synonyms
HQDO, hydroquinone 1,2-dioxygenase, hydroquinone dioxygenase, LinE, mnpC, PcpA, PdcDE, PnpC1, PnpC2, PnpCD, ring-cleavage hydroquinone 1,2-dioxygenase, two-subunit hydroquinone 1,2-dioxygenase, type II HQDO, YaiA
ECTree
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Subunits
Subunits on EC 1.13.11.66 - hydroquinone 1,2-dioxygenase
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heterotetramer
tetramer
additional information
C1I210; C1I209
2 * 38300, subunit alpha, + 2 * 18000, subunit beta
heterotetramer
2 * 19000, subunit alpha, + 2 * 38000, subunit beta
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
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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
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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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