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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Reaction
Reaction on EC 1.3.5.2 - dihydroorotate dehydrogenase (quinone)
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(S)-dihydroorotate + a quinone = orotate + a quinol
existence of 3 families differing in their selectivity for oxidizing substrates: 1A are soluble, containing FMN and use fumarate, 1B are soluble, one subunit contains an iron-sulfur center, FAD and reduces NAD+, family 2 enzymes are membrane-bound, contain FMN and are oxidized by ubiquinone. Mechanism consists of 3 reaction phases. Different binding-mechanisms for enzyme the reaction-steps are suggested
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(S)-dihydroorotate + a quinone = orotate + a quinol
different binding sites for dihydroorotate and the electron acceptor, two-site ping-pong mechanism. Cleavage site at R182 is conserved between the two major families of dihydroorotate dehydrogenases, it is positioned in a loop, which is crucial for catalysis but irrelevant for protein stability
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(S)-dihydroorotate + a quinone = orotate + a quinol
68% identity with type A enzyme of Lactococcus lactis, two-site non-classical ping-pong kinetic mechanism
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(S)-dihydroorotate + a quinone = orotate + a quinol
one-site ping-pong mechanism, residues 129-137 form a flexible loop, responsible for substrate binding
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(S)-dihydroorotate + a quinone = orotate + a quinol
fourth step in biosynthesis of pyrimidines. Two domains: alpha/beta-barrel domain containing the active site, one alpha-helical domain that forms the opening of a tunnel leading to active site
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(S)-dihydroorotate + a quinone = orotate + a quinol
in liver, myocardium and skeletal muscle tissues the activity intensities vary from animal to animal, but are similar in ileum, colon and kidney cortex. Cardiac enzyme expresses a pronounced oxidase activity
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(S)-dihydroorotate + a quinone = orotate + a quinol
in liver, myocardium and skeletal muscle tissues the activity intensities vary from animal to animal, but are similar in ileum, colon and kidney cortex. Cardiac enzyme expresses a pronounced oxidase activity
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(S)-dihydroorotate + a quinone = orotate + a quinol
in liver, myocardium and skeletal muscle tissues the activity intensities vary from animal to animal, but are similar in ileum, colon and kidney cortex. Cardiac enzyme expresses a pronounced oxidase activity
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(S)-dihydroorotate + a quinone = orotate + a quinol
in liver, myocardium and skeletal muscle tissues the activity intensities vary from animal to animal, but are similar in ileum, colon and kidney cortex. Cardiac enzyme expresses a pronounced oxidase activity
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(S)-dihydroorotate + a quinone = orotate + a quinol
in liver, myocardium and skeletal muscle tissues the activity intensities vary from animal to animal, but are similar in ileum, colon and kidney cortex. Cardiac enzyme expresses a pronounced oxidase activity
-
(S)-dihydroorotate + a quinone = orotate + a quinol
in liver, myocardium and skeletal muscle tissues the activity intensities vary from animal to animal, but are similar in ileum, colon and kidney cortex. Cardiac enzyme expresses a pronounced oxidase activity
(S)-dihydroorotate + a quinone = orotate + a quinol
soluble quinones as second substrate
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(S)-dihydroorotate + a quinone = orotate + a quinol
two-site ping-pong mechanism
(S)-dihydroorotate + a quinone = orotate + a quinol
enzyme uses a stepwise mechanism for dihydroorotate oxidation
(S)-dihydroorotate + a quinone = orotate + a quinol
the active base S175 and the hydrogen bonding network including residues T178 and F115 work together for efficient deprotonation of dihydroorotate
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