3.5.2.3: dihydroorotase
This is an abbreviated version!
For detailed information about dihydroorotase, go to the full flat file.
Word Map on EC 3.5.2.3
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3.5.2.3
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pyrimidine
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transcarbamoylase
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carbamoyl-phosphate
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phosphoribosyltransferase
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atcase
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orotidine
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carbamoyltransferase
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glutamine-dependent
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l-dihydroorotate
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2.1.3.2
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cpsase
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pyre
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dihydropyrimidinase
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hydantoinase
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dihydro-ouabain
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n-phosphonacetyl-l-aspartate
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n-carbamyl-l-aspartate
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allantoinase
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imidase
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synthesis
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succinate-grown
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amidohydrolases
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6.3.5.5
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drug development
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medicine
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5-fluoroorotate
- 3.5.2.3
- pyrimidine
-
transcarbamoylase
- carbamoyl-phosphate
- phosphoribosyltransferase
- atcase
- orotidine
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carbamoyltransferase
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glutamine-dependent
- l-dihydroorotate
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2.1.3.2
- cpsase
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pyre
- dihydropyrimidinase
- hydantoinase
- dihydro-ouabain
- n-phosphonacetyl-l-aspartate
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n-carbamyl-l-aspartate
- allantoinase
- imidase
- synthesis
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succinate-grown
-
amidohydrolases
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6.3.5.5
- drug development
- medicine
- 5-fluoroorotate
Reaction
Synonyms
amidohydrolase family protein, BcDHOase, CAD, carbamoylaspartic dehydrase, Class I DHOase, DHO, DHOase, dihydroorotase, dihydroorotase domain, dihydroorotate dehydrolase, hDHOase, huDHOase, human DHOase domain, LdDHOase, More, pyrC, type I DHOase, type II DHO, VcDHO, YpDHO
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Subunits
Subunits on EC 3.5.2.3 - dihydroorotase
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dimer
hexamer
homodimer
homotetramer
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temperature-dependent conversion to homodimer, crystallization data
monomer
multimer
additional information
?
x * 43900, about, sequence calculation, x* 48000, recombinant His6-tagged enzyme, SDS-PAGE
?
Leishmania donovani BHU 1081
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x * 43900, about, sequence calculation, x* 48000, recombinant His6-tagged enzyme, SDS-PAGE
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?
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x * 47503-48104, sequence calculation, mass spectrometry, and SDS-PAGE
?
Methanocaldococcus jannaschii ATCC 624773
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x * 47503-48104, sequence calculation, mass spectrometry, and SDS-PAGE
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homodimer
crystallization data, asymmetry between active sites, with N-carbamyl-L-aspartate bound to one site and dihydroorotate bound to the other
homodimer
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temperature-dependent conversion to homotetramer, crystallization data
monomer
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1 * 40000, gel filtration, 75% of the total activity is associated with the monomeric form
multimer
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multi-enzyme complex, carbamoyl phosphate synthetase, aspartate transcarbamylase and dihydroorotase, 129000 + 39000 + 44000, SDS-PAGE
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recombinant protein lacks catalytic activity, activity is acquired by forming a complex with aspartate transcarbamoylase, complex may be a heterohexamer or dodecamer
additional information
enzymes DHO-ATC complex structure, analysis of the quaternary structural organization and interactions between the subunits in the Aquifex aeolicus complex, overview
additional information
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enzymes DHO-ATC complex structure, analysis of the quaternary structural organization and interactions between the subunits in the Aquifex aeolicus complex, overview
additional information
replacement of the flexible loop weakens the dimerization of huDHOase
additional information
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replacement of the flexible loop weakens the dimerization of huDHOase
additional information
the His-SUMO tag does not interfere with SaPyrC dimerization
additional information
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the His-SUMO tag does not interfere with SaPyrC dimerization
additional information
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the His-SUMO tag does not interfere with SaPyrC dimerization
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additional information
direct intermolecular interactions between carbamoylphosphate synthetase II, aspartate transcarbamoylase, and dihydroorotase, which catalyze the first 3 reaction steps of the de novo pyrimidine biosynthetic pathway
additional information
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direct intermolecular interactions between carbamoylphosphate synthetase II, aspartate transcarbamoylase, and dihydroorotase, which catalyze the first 3 reaction steps of the de novo pyrimidine biosynthetic pathway
additional information
three-dimensional structure of DHO from Vibrio cholerae, structure analysis and comparison, overview
additional information
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three-dimensional structure of DHO from Vibrio cholerae, structure analysis and comparison, overview
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additional information
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three-dimensional structure of DHO from Vibrio cholerae, structure analysis and comparison, overview
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additional information
three-dimensional structure of DHO from Yersinia pestis, structure analysis and comparison, overview. Each subunit has a structure based on the (beta/alpha)8-barrel (TIM-barrel) fold, a characteristic of the amidohydrolase superfamily
additional information
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three-dimensional structure of DHO from Yersinia pestis, structure analysis and comparison, overview. Each subunit has a structure based on the (beta/alpha)8-barrel (TIM-barrel) fold, a characteristic of the amidohydrolase superfamily