1.3.1.14: dihydroorotate dehydrogenase (NAD+)
This is an abbreviated version!
For detailed information about dihydroorotate dehydrogenase (NAD+), go to the full flat file.
Word Map on EC 1.3.1.14
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1.3.1.14
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pyrimidine
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flavin
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brequinar
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medicine
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l-dihydroorotate
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fmn
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lactis
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o2-sensitive
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mononucleotide
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photons
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bifidobacterium
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bifidum
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berghei
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ubiquinone
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carbamyl
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half-reaction
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nutrition
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pharmacology
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1.3.3.1
- 1.3.1.14
- pyrimidine
- flavin
- brequinar
- medicine
- l-dihydroorotate
- fmn
- lactis
-
o2-sensitive
- mononucleotide
-
photons
- bifidobacterium
- bifidum
- berghei
- ubiquinone
-
carbamyl
-
half-reaction
- nutrition
- pharmacology
-
1.3.3.1
Reaction
Synonyms
b-type dihydroorotate dehydrogenase, DHO dehydrogenase, DHODase, DHOdehase A, dihydro-orotic dehydrogenase, dihydroorotate dehydrogenase, dihydrorotate dehydrogenase B, L-5,6-dihydro-orotate:NAD oxidoreductase, More, orotate reductase, reductase, orotate
ECTree
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Cofactor
Cofactor on EC 1.3.1.14 - dihydroorotate dehydrogenase (NAD+)
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4Fe-4S-center
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two [2Fe-2S] clusters as cofactors, tightly bound to the beta subunit and located in the interface of the two dimers centered between the FMN and FAD group, Cys-226, Cys-231, Cys-234 and Cys-249 binds the iron-sulfur cluster
4Fe-4S-center
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cofactor content: 4 non-heme iron and 4 labile sulfur atoms per heterotetramer
4Fe-4S-center
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cofactor content: 4 non-heme iron and 4 labile sulfur atoms per heterotetramer
4Fe-4S-center
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cofactor content: 4 non-heme iron and 4 labile sulfur atoms per heterotetramer
4Fe-4S-center
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cofactor content: 4 non-heme iron and 4 labile sulfur atoms per heterotetramer
FAD
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two tightly bound FAD per heterotetrameric enzyme, FAD is necessary for ability to use NAD+ as electron acceptor, detailed way of binding
flavin
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flavoprotein with two different flavins, probably FAD and FMN
flavin
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interaction of flavin and dihydroorotate is completely dependent on cysteine
FMN
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two tightly bound FMN per heterotetrameric enzyme, detailed way of binding
FMN
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PyrDI is an FMN-containing iron-sulfur flavoprotein, 1 FMN molecule per PyrDI molecule
FMN
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key charge-stabilizing role for Lys-48 of subunit D during reduction of FMN by dihydroorotate or by electron transfer from the 2Fe-2S center