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
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Application
Application on EC 1.3.5.2 - dihydroorotate dehydrogenase (quinone)
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drug development
medicine
pharmacology
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A77 1726 inhibits cell growth in multiple myeloma cell lines at clinically achievable concentrations by induction of apoptosis. Inhibition of cell growth is partly due to inhibition of multiple myeloma cell proliferation. A77 1726 shows synergistic and additive activity together with genotoxic agents melphalan, treosulfan, and doxorubicin
synthesis
expression of full-length and N-terminally trucated enzyme lacking 29 amino acids in an Escherichia coli system
additional information
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DHODH represents a potential target for anti-malarial therapy
drug development
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DHODH represents a potential target for anti-malarial therapy
drug development
DHODH represents a potential target for anti-malarial therapy
medicine
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enzyme inhibition is a mechanism of action that may be relevant for the therapeutic effects of leflunomide
medicine
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great interest in inhibitors as potential therapeutic agents for the treatment of diseases involving aberrant cell proliferation
medicine
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great interest in inhibitors as potential therapeutic agents for the treatment of diseases involving aberrant cell proliferation
medicine
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great interest in inhibitors as potential therapeutic agents for the treatment of diseases involving aberrant cell proliferation
medicine
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inhibition of pyrimidine biosynthesis by targeting enzyme activity, mechanism for antimicrobial intervention
medicine
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molecular target of the antiproliferative, immunosuppressive compound brequinar sodium
medicine
background for the development of antipyrimidines with high efficacy for decreasing in situ pyrimidine nucleotide pools in Candida albicans
medicine
PfDHODH is a promising target for chemotherapeutic intervention in prevention of malaria
medicine
promising new target for chemotherapeutic intervention in prevention of malaria, synthesized inhibitors prevent growth of cultured parasites at low micromolar concentrations, interaction of inhibitors with amino acid residues F188, H185, and R265
medicine
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promising new target for chemotherapeutic intervention in prevention of malaria, synthesized inhibitors show considerable lower affinity for the human DHODH enzyme relative to the Plasmodium DHODH enzyme
medicine
DHODH represents a potential target for anti-malarial therapy
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kinetic isotope effects on flavin reduction in anaerobic stopped-flow experiments, are about 3fold for DHO labeled at the 5-position, about 4fold for DHO labeled at the 6-position, and about 6-7fold for DHO labeled at both the 5- and 6-positions, at a pH value above the pKa controlling reduction, no isotope effect was observed for DHO deuterated at the 5-position, which is consistent with a stepwise reaction, above the kinetic pKa, the deprotonation of C5 is fast enough that it does not contribute to the observed rate constant and, therefore, is not isotopically sensitive
additional information
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kinetic isotope effects on flavin reduction in anaerobic stopped-flow experiments, pKa near 9.4 controlling reduction, similar to that previously reported for the Escherichia coli enzyme
additional information
three types of hydrogen bonding pathways, hydrogen bonding of the active base serine to a water molecule, which is hydrogen bonded to the substrate carboxylate group or a threonine residue, the threonine residue is positioned to enable proton transfer to another water molecule leading to the bulk solvent
additional information
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three types of hydrogen bonding pathways, hydrogen bonding of the active base serine to a water molecule, which is hydrogen bonded to the substrate carboxylate group or a threonine residue, the threonine residue is positioned to enable proton transfer to another water molecule leading to the bulk solvent