3.5.1.6: beta-ureidopropionase
This is an abbreviated version!
For detailed information about beta-ureidopropionase, go to the full flat file.
Word Map on EC 3.5.1.6
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3.5.1.6
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pyrimidine
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uracil
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dihydropyrimidinase
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thymine
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dihydrouracil
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kluyveri
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nitrilase
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amidohydrolases
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beta-aminoisobutyric
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beta-ureidoisobutyrate
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medicine
- 3.5.1.6
- pyrimidine
- uracil
- dihydropyrimidinase
- thymine
- dihydrouracil
- kluyveri
- nitrilase
-
amidohydrolases
-
beta-aminoisobutyric
- beta-ureidoisobutyrate
- medicine
Reaction
Synonyms
3-ureidopropionase, beta-Ala synthase, beta-alanine synthase, beta-UP, beta-ureidopropionase, beta-ureidopropionate decarbamylase, betaAS, betaUP, betaUPase, BUP-1, BUP1, human liver beta-ureidopropionase, N-carbamoyl-beta-Ala amidohydrolase, N-carbamoyl-beta-alanine amidohydrolase, N-carbamyl-beta-alanine decarbamylase, NCbetaA, PYD3, SkbetaAS, UPB1
ECTree
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Subunits
Subunits on EC 3.5.1.6 - beta-ureidopropionase
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decamer
dimer
dodecamer
hexamer
homodecamer
homodimer
homohexamer
oligomer
homodimer at pH 9, the enzyme increasingly associates to form octamers and larger oligomers with decreasing pH. Native PAGE analysis of wild-type enzyme indicates coexistence in at least five different oligomeric states, of which the smallest is most probably the dimer
tetramer
4 * 43158, sequence calculation, structure analysis by dynamic light scattering and circular dichroism spectroscopy, and modeling, overview
trimer
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3 * 42000, inactive trimer in the presence of the product, SDS-PAGE
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10 * 43000, recombinant beta-UP, at pH 7, SDS-PAGE, 10 * 43723, recombinant beta-UP, at pH 7, mass spectrometry, 10 * 43733, sequence calculation
dodecamer
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12 * 42000, active dodecamer in the presence of substrate, SDS-PAGE
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6 * 42000, the native enzyme is a hexamer, which readily associates to an active dodecamer in the presence of substrate and dissociates to an inactive trimer in the presence of the product, SDS-PAGE
homodimer
homodimer at pH 9, the enzyme increasingly associates to form octamers and larger oligomers with decreasing pH. Native PAGE analysis of wild-type enzyme indicates coexistence in at least five different oligomeric states, of which the smallest is most probably the dimer
homodimer
a subunit of the homodimer consists of two domains: a larger catalytic domain with a dizinc metal center, representing the active site, and a smaller domain mediating the majority of the intersubunit contacts, the dimeric state is essential for catalytic activity