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
3.5.1.6 beta-ureidopropionaseAdvanced search results
results (
results (Subunits
Subunits on EC 3.5.1.6 - beta-ureidopropionase
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SUBUNIT 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
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
-
3 * 42000, inactive trimer in the presence of the product, SDS-PAGE
decamer
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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
hexamer
-
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
