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
1.3.98.1 dihydroorotate dehydrogenase (fumarate)Advanced search results
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results (Engineering
Engineering on EC 1.3.98.1 - dihydroorotate dehydrogenase (fumarate)
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
S175A
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low activity with dihydroorotate, increasing activity above pH 8.0 with dihydrooxonate
Q7L
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single nucleotide polymorphism due to missense polymorphism 19C>A, leading to amino acid substitution in the cationic N-terminal region of the polypeptide
C130A
C130S
E206/K296E
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conversion of intermolecular salt bridge, mutant is fully active in concentrated solutions and dissociates into monomers upon dilution like wild-type enzyme
E206A
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disturbance of intermolecular salt bridge, mutant retains almost complete activity
E206K
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disturbance of intermolecular salt bridge, mutant activity is severely impaired
K296A
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disturbance of intermolecular salt bridge, mutant retains almost complete activity
K296E
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disturbance of intermolecular salt bridge, mutant activity is severely impaired
L71F
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reaction is somehow slower than for wild-type, binding of dihydroorotate is much tighter than with wild-type
L71F/C130S/V133T
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addition of the two residues comprising the conserved proton-transfer network of Class 2 dihydroorotate dehydrogenase from Escherichia coli to the C130S Class 1A enzyme of Lactococcus lacits. Mutation does not did not restore the function of the active site base or rapid flavin reduction. Kd for dihydroorotate is about three times tighter than the wild-type
L71F/V133T
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reaction is drastically slower forwith wild-type, Kd for dihydroorotate is iabout eight-fold tighter than the wild-type
V133T
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reaction is somehow slower than for wild-type, binding of dihydroorotate is much weaker than with wild-type
H185A
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4fold increase in KM-value of CoQD, 50% increase in KM-value of L-dihydroorotate
R265A
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2fold increase in KM-value of CoQD, 15% increase in KM-value of L-dihydroorotate
additional information
C130A
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low activity with dihydroorotate, increasing activity above pH 8.0 with dihydrooxonate
C130A
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the mutant enzyme exhibits binding affinities for dihydroorotate similar to that of the wild type enzyme, reduction is extremely slow compared to that of the wild type, the rate of reduction increases with pH showing no sign of a plateau
C130A
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the mutant forms charge-transfer complexes upon binding 3,4-dihydroxybenzoate, but the maximum of the broad charge-transfer bands is shifted to 590 nm
C130S
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the mutant enzyme exhibits binding affinities for dihydroorotate similar to that of the wild type enzyme, reduction is extremely slow compared to that of the wild type, the rate of reduction increases with pH showing no sign of a plateau
C130S
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the mutant forms charge-transfer complexes upon binding 3,4-dihydroxybenzoate, but the maximum of the broad charge-transfer bands is shifted to 610 nm
additional information
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deletions of N-terminal residues from 2 down to 40 result in generally unstable proteins with apo protein quickly precipitating and FMN remaining in solution. A truncated protein lacking residues 2 to 30 is sufficiently stable, has near to wild-type activity using molecular oxygen and 20fold lower activity using 2,6-dichlorophenolindophenol as electron acceptor
additional information
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DHOD-knockout Trypanosoma cruzi do not express the enzyme protein and can not survive even in the presence of pyrimidine nucleosides, suggesting a vital role of fumarate reductase activity in the regulation of cellular redox balance
