3.5.2.1: barbiturase
This is an abbreviated version!
For detailed information about barbiturase, go to the full flat file.
Word Map on EC 3.5.2.1
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3.5.2.1
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pyrimidine
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dihydrouracil
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hydantoinase
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5-fluorouracil
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5,6-dihydrouracil
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5,6-dihydrothymine
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dihydropyrimidine
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dihydroorotase
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hydantoin
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3.5.2.2
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dihydrothymine
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dihydropyrimidinuria
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allantoinase
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beta-amino
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dhpase
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imidase
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5,6-dihydropyrimidine
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fluoropyrimidine
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collapsin
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cyanuric
- 3.5.2.1
- pyrimidine
- dihydrouracil
- hydantoinase
- 5-fluorouracil
- 5,6-dihydrouracil
- 5,6-dihydrothymine
-
dihydropyrimidine
- dihydroorotase
- hydantoin
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3.5.2.2
- dihydrothymine
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dihydropyrimidinuria
- allantoinase
-
beta-amino
- dhpase
- imidase
- 5,6-dihydropyrimidine
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fluoropyrimidine
-
collapsin
-
cyanuric
Reaction
ECTree
3.5.2.1 barbituraseAdvanced search results
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General Information on EC 3.5.2.1 - barbiturase
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GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
evolution
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the enzyme belongs to a protein family that consists of only cyanuric acid hydrolase (CAH) and barbiturase. CAH and barbiturase enzymes act on structurally analogous 6-membered ring substrates, yet each enzyme is specific and does not react with the other's substrate. While most organisms utilize a reductive pyrimidine degradation pathway, some actinobacteria use barbiturase in an oxidative catabolic pathway. Unlike barbiturase, cyanuric acid hydrolases are more broadly distributed throughout bacteria and fungi. The CAH/barbiturase family includes 169 different sequences of Actinobacteria, phylogenetic analysis and tree, overview
metabolism
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barbiturase participating in pyrimidine catabolism by some actinobacterial species. Barbiturase catalyzes the second step in the oxidative pyrimidine degradation pathway
