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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

Engineering

Engineering on EC 3.5.1.6 - beta-ureidopropionase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
R291E
-
R291 is the key residue for recognition of the substrate carboxyl group
R291K
-
R291 is the key residue for recognition of the substrate carboxyl group
R291Q
-
R291 is the key residue for recognition of the substrate carboxyl group
R291E
Agrobacterium tumefaciens C58 / ATCC 33970
-
R291 is the key residue for recognition of the substrate carboxyl group
-
R291K
Agrobacterium tumefaciens C58 / ATCC 33970
-
R291 is the key residue for recognition of the substrate carboxyl group
-
R291Q
Agrobacterium tumefaciens C58 / ATCC 33970
-
R291 is the key residue for recognition of the substrate carboxyl group
-
A85E
-
expression of the A85E plasmid results in severely reduced BUP-1 enzyme activity, with only 2.7% activity relative to the wild-type UPB1 plasmid
C233A
inactive mutant enzyme
E137K
inactive mutant enzyme
G235R
naturally occuring mutation and site-directed mutagenesis, inactive mutant. Mutation G235R introduces a large amino acid side chain for which there is no space available at this location. The larger structural rearrangements in the active site cavity required to prevent clashes with surrounding residues are expected to lead to enzyme inactivity and misfolding and defects in oligomerization, inability to obtain significant expression of soluble protein for this mutant
G31G
a naturally occuring synonymous mutation c.93C>T
K132L
inactive mutant enzyme, the mutant enzyme is exclusively dimeric
R130D
inactive mutant enzyme
R130D/S208R
inactive mutant enzyme, the mutant enzyme is exclusively dimeric
R130I
inactive mutant enzyme, a significant monomer proportion is detected
R236W
naturally occuring mutation and site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
R326Q
S208A
inactive mutant enzyme, a significant monomer proportion is detected
S208C
inactive mutant enzyme, exclusively exists as dimer
S208R
inactive mutant enzyme, the mutant enzyme is exclusively dimeric
S264R
naturally occuring mutation and site-directed mutagenesis,mutation S264R abolishes the hydrogen bond to Y314, which may be important for structural fixation of a residue stretch that is involved in shaping the entrance to the active site, the mutant shows reduced activity compared to the wild-type enzyme
T299C
inactive mutant enzyme, exclusively exists as dimer
T359M
E159A
0.09% of the wild-type activity
E159D
0.09% of the wild-type activity
H226E
no activity
H262A
8.9% of the wild-type activity
H397N
7.2% of the wild-type activity
R322A
0.14% of the wild-type activity
additional information