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
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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
ECTree
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Activating Compound
Activating Compound on EC 3.5.2.3 - dihydroorotase
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increases the catalytic efficiency on the ring cyclization reaction, but not on the ring hydrolysis
Dimethylsulfoxide
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increases the catalytic efficiency on the ring cyclization reaction, but not on the ring hydrolysis
pressure-induced activation of dihydroorotase, overview
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additional information
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pressure-induced activation of dihydroorotase, overview
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additional information
reversible activation of latent dihydroorotase from Aquifex aeolicus by moderate hydrostatic pressure. Moderate hydrostatic pressure applied to the isolated DHO subunit mimics the complex formation and reversibly activates the isolated subunit in the absence of ATC, suggesting that the loop has been displaced from the active site. This effect of pressure is explained by the negative volume change associated with the disruption of ionic interactions and exposure of ionized amino acids to the solvent (electrostriction). The isolated DHO protein, a 45-kDa monomer, lacks catalytic activity but becomes active upon formation of a dodecameric complex with aspartate transcarbamoylase (ATC, EC 2.1.3.2)
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additional information
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reversible activation of latent dihydroorotase from Aquifex aeolicus by moderate hydrostatic pressure. Moderate hydrostatic pressure applied to the isolated DHO subunit mimics the complex formation and reversibly activates the isolated subunit in the absence of ATC, suggesting that the loop has been displaced from the active site. This effect of pressure is explained by the negative volume change associated with the disruption of ionic interactions and exposure of ionized amino acids to the solvent (electrostriction). The isolated DHO protein, a 45-kDa monomer, lacks catalytic activity but becomes active upon formation of a dodecameric complex with aspartate transcarbamoylase (ATC, EC 2.1.3.2)
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additional information
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following pyrimidine limitation of orotidine 5'-monophosphate decarboxylase mutant strain cells, dihydroorotase and dihydroorotate dehydrogenase activities double while aspartate transcarbamoylase and orotate phosphoribosyltransferase activities are slightly elevated compared to their activities in the mutant strain cells grown on excess uracil
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