1.3.5.2: dihydroorotate dehydrogenase (quinone)
This is an abbreviated version!
For detailed information about dihydroorotate dehydrogenase (quinone), go to the full flat file.
Word Map on EC 1.3.5.2
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1.3.5.2
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pyrimidine
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falciparum
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plasmodium
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leflunomide
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brequinar
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uridine
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malaria
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arthritis
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antimalarial
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rheumatoid
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dihydroorotase
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salvage
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teriflunomide
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dhods
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autoimmune
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orotidine
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ump
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atovaquone
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triazolopyrimidine
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flavoenzyme
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medicine
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phosphoribosyltransferase
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antirheumatic
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coq
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drug development
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decylubiquinone
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dmards
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synthesis
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species-selective
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pyre
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pharmacology
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isoxazole
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transcarbamoylase
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5-fluoroorotate
- 1.3.5.2
- pyrimidine
- falciparum
- plasmodium
- leflunomide
- brequinar
- uridine
- malaria
- arthritis
-
antimalarial
-
rheumatoid
- dihydroorotase
-
salvage
- teriflunomide
-
dhods
- autoimmune
- orotidine
- ump
- atovaquone
- triazolopyrimidine
-
flavoenzyme
- medicine
-
phosphoribosyltransferase
-
antirheumatic
- coq
- drug development
- decylubiquinone
-
dmards
- synthesis
-
species-selective
-
pyre
- pharmacology
-
isoxazole
-
transcarbamoylase
- 5-fluoroorotate
Reaction
Synonyms
class 2 dihydroorotate dehydrogenases, DHO-DH, DHOD, DHODase, DHODH, dihydroorotate dehydrogenase, EC 1.3.99.11, ETH_00004975, hDHODH, HsDHODH, L-5,6-dihydroorotate:ubiquinone exidoreductase, PfDHODH
ECTree
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Localization
Localization on EC 1.3.5.2 - dihydroorotate dehydrogenase (quinone)
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electron spin resonance spectra show that the N-terminal binds to membranes and experiences a somewhat high flexibility that could be related to the role of this region as a molecular lid controlling the entrance of the enzyme's active site and thus allowing the enzyme to give access to quinones that are dispersed in the membrane and that are necessary for the catalysis
cardiolipin enhances the interaction of truncated DHODH with lipid bilayers, but the presence of the transmembrane domain in human DHODH is necessary for stable binding to and securing its location at the outer surface of the inner mitochondrial membrane