Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

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

Reaction

3-ureidopropanoate
+
H2O
=
beta-Alanine
+
CO2
+
NH3

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 Hydrolases
         3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
             3.5.1 In linear amides
                3.5.1.6 beta-ureidopropionase

Crystallization

Crystallization on EC 3.5.1.6 - beta-ureidopropionase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystals of the recombinant enzyme from Drosophila melanogaster are obtained by the hanging-drop vapour-diffusion method
-
sitting drop vapor diffusion method, crystal structure is determined to 2.8 A resolution
-
T299C is crystallized by the hanging-drop vapor diffusion method at 20°C. The T299C mutant enzyme crystallizes in space group C2221 with one polypeptide chain per asymmetric unit. The structure is determined to 2.08 A by molecular replacement
crystal structures of wild-type beta-alanine synthase in complex with the reaction product beta-alanine, and of the mutant E159A with the substrate N-carbamyl-beta-alanine
overexpressed native and selenomethionine-substituted SkbetaAS, hanging drop vapor diffusion method
recombinant betaAS, X-ray analysis
-