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Information on EC 1.3.98.1 - dihydroorotate dehydrogenase (fumarate) and Organism(s) Homo sapiens and UniProt Accession Q02127

for references in articles please use BRENDA:EC1.3.98.1

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IUBMB Comments

Binds FMN. The reaction, which takes place in the cytosol, is the only redox reaction in the de novo biosynthesis of pyrimidine nucleotides. Molecular oxygen can replace fumarate in vitro. Other class 1 dihydroorotate dehydrogenases use either NAD+ (EC 1.3.1.14) or NADP+ (EC 1.3.1.15) as electron acceptor. The membrane bound class 2 dihydroorotate dehydrogenase (EC 1.3.5.2) uses quinone as electron acceptor.

The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms

Synonyms
dhodh, dhodehase, dhoda, lmdhodh, dihydroorotate oxidase, tcdhod, (dho) dehydrogenase, class 1a dhod, class 1a dhodh, dhod1, more

SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
(DHO) dehydrogenase
-
-
-
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4,5-L-dihydroorotate:oxygen oxidoreductase
-
-
-
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DHOdehase
-
-
-
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DHODH
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Dihydroorotate oxidase
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-
-
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oxidase, dihydroorotate
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-
-
-
additional information
-
class 2 DHODH family enzyme
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
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oxidation
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-
-
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reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
MetaCyc
UMP biosynthesis II
SYSTEMATIC NAME
IUBMB Comments
(S)-dihydroorotate:fumarate oxidoreductase
Binds FMN. The reaction, which takes place in the cytosol, is the only redox reaction in the de novo biosynthesis of pyrimidine nucleotides. Molecular oxygen can replace fumarate in vitro. Other class 1 dihydroorotate dehydrogenases use either NAD+ (EC 1.3.1.14) or NADP+ (EC 1.3.1.15) as electron acceptor. The membrane bound class 2 dihydroorotate dehydrogenase (EC 1.3.5.2) uses quinone as electron acceptor.
CAS REGISTRY NUMBER
COMMENTARY hide
9029-03-2
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY hide
Reversibility
r=reversible
ir=irreversible
?=not specified
L-dihydroorotate + fumarate
orotate + succinate
show the reaction diagram
-
Substrates: -
Products: -
?
additional information
?
-
-
Substrates: three-dimensional active site structure, profile of interactions for molecular recognition, interaction of DHODH with orotate via residues Asn212, Asn284, Ser215, Phe149, Lys100, Gly148, Asn217, Asn145, and Thr285, overview
Products: -
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY hide
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-dihydroorotate + fumarate
orotate + succinate
show the reaction diagram
-
Substrates: -
Products: -
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,5-dihydrofuro[3,4-d]pyrimidine-2,4,7-trione
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2,3-dihydrotriazolo[4,5-d]pyrimidine-5,7-dione
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2,6-dioxo-1,2,3,6-tetrahydropyrimidine-4-carboxylic acid
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4,6-dioxo-1,4,5,6-tetrahydro-1,3,5-triazine-2-carboxylic acid
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5-amino-2,6-dioxo-1,2,3,6-tetrahydropyrimidine-4-carboxylic acid
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5-fluoro-2,6-dioxo-1,2,3,6-tetrahydropyrimidine-4-carboxylic acid
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5-nitro-2,6-dioxo-1,2,3,6-tetrahydropyrimidine-4-carboxylic acid
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5-[(dimethylamino)methyl]-2,6-dioxo-1,2,3,6-tetrahydropyrimidine-4-carboxylic acid
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7,9-dihydro-3H-purine-2,6,8-trione
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butyl 2,6-dioxo-1,2,3,6-tetrahydropyrimidine-4-carboxylate
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additional information
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inhibitor virtual screening, overview
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
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assay at
top print hide Go to Localization Search
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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anchored
Manually annotated by BRENDA team
Highest Expressing Human Cell Lines
Cell Line Links Gene Links
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
structure comparisons of enzymes from Trypanosoma cruzi, Leishmania major, and Homo sapiens, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme in complex with orotate, crystal structure analysis, overview
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
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in patients with rheumatoid arthritis treated with leflunomide, the frequency of remission is increased in patients carrying the C allele of single nucleotide polymorphism 19C>A compared with patients carrying the A allele
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Pawlik, A.; Herczynska, M.; Kurzawski, M.; Safranow, K.; Dziedziejko, V.; Drozdzik, M.
The effect of exon (19C>A) dihydroorotate dehydrogenase gene polymorphism on rheumatoid arthritis treatment with leflunomide
Pharmacogenomics
10
303-309
2009
Homo sapiens
Manually annotated by BRENDA team