1.3.98.1: dihydroorotate dehydrogenase (fumarate)
This is an abbreviated version!
For detailed information about dihydroorotate dehydrogenase (fumarate), go to the full flat file.
Word Map on EC 1.3.98.1
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1.3.98.1
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pyrimidine
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leflunomide
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brequinar
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uridine
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plasmodium
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falciparum
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ubiquinone
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teriflunomide
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dhods
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1.3.3.1
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ump
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dihydro-orotate
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triazolopyrimidine
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atovaquone
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1.3.99.11
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dysostosis
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analysis
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medicine
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acrofacial
- 1.3.98.1
- pyrimidine
- leflunomide
- brequinar
- uridine
- plasmodium
- falciparum
- ubiquinone
- teriflunomide
-
dhods
-
1.3.3.1
- ump
-
dihydro-orotate
- triazolopyrimidine
- atovaquone
-
1.3.99.11
- dysostosis
- analysis
- medicine
-
acrofacial
Reaction
Synonyms
(DHO) dehydrogenase, 4,5-L-dihydroorotate:oxygen oxidoreductase, ACT/DHOD, class 1A DHOD, class 1A DHODH, class 1A dihydroorotate dehydrogenase, DHOD, DHOD1, DHOD2, DHOD3, DHODA, DHOdehase, DHODH, DHODH-1A, dihydroorotate dehydrogenase, dihydroorotate dehydrogenase class 1A, Dihydroorotate oxidase, EC 1.3.3.1, LmDHODH, More, oxidase, dihydroorotate, TcDHOD
ECTree
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Reaction
Reaction on EC 1.3.98.1 - dihydroorotate dehydrogenase (fumarate)
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(S)-dihydroorotate + fumarate = orotate + succinate
light sensitivity seems to result in a conformational change and a partial loss of enzymatic activity
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(S)-dihydroorotate + fumarate = orotate + succinate
A flavoprotein (FAD, FMN). Ferricyanide can act as accetor
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(S)-dihydroorotate + fumarate = orotate + succinate
mechanism, pyrimidine biosynthetic pathways
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(S)-dihydroorotate + fumarate = orotate + succinate
cysteine and serine are active site base residues. One-site ping-pong mechanism with fumarate as electron acceptor
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(S)-dihydroorotate + fumarate = orotate + succinate
cysteine and serine are active site base residues. One-site ping-pong mechanism with fumarate as electron acceptor
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(S)-dihydroorotate + fumarate = orotate + succinate
sulfhydryl groups suggested to be located near the active site, suggested that enzyme produces superoxide free radicals upon reaction with oxygen
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(S)-dihydroorotate + fumarate = orotate + succinate
the active site contains a water filled cavity buried beneath a highly conserved and flexible loop. Orotate is bound by four conserved asparagine side chains. Implications for differences in substrate binding and in the catalytic mechanism between the different enzyme families are given
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(S)-dihydroorotate + fumarate = orotate + succinate
ping-pong bi-bi mechanism
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(S)-dihydroorotate + fumarate = orotate + succinate
two-site ping-pong mechanism, catalytic base is serine
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