Information on EC 3.5.1.6 - beta-ureidopropionase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
3.5.1.6
-
RECOMMENDED NAME
GeneOntology No.
beta-ureidopropionase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
3-ureidopropanoate + H2O = beta-alanine + CO2 + NH3
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of linear amides
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
alanine metabolism
-
-
beta-Alanine metabolism
-
-
Drug metabolism - other enzymes
-
-
Metabolic pathways
-
-
Pantothenate and CoA biosynthesis
-
-
pyrimidine metabolism
-
-
Pyrimidine metabolism
-
-
thymine degradation
-
-
uracil degradation I (reductive)
-
-
SYSTEMATIC NAME
IUBMB Comments
N-carbamoyl-beta-alanine amidohydrolase
The animal enzyme also acts on beta-ureidoisobutyrate.
CAS REGISTRY NUMBER
COMMENTARY hide
9027-27-4
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Blastobacter sp.
A17p-4
-
-
Manually annotated by BRENDA team
plant pathogen, opportunistic pathogen in humans, ATCC 25416
-
-
Manually annotated by BRENDA team
Clostridium uracilicum
Clostridium uracilicum M5-2
strain M5-2
-
-
Manually annotated by BRENDA team
E222c
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Pigeon
-
-
-
Manually annotated by BRENDA team
Sprague-Dawley rats, CD strain
-
-
Manually annotated by BRENDA team
facultative phototrophic bacterium, strain R10
-
-
Manually annotated by BRENDA team
heat-sensitive tomato variant, gene SlUPB1; heat-tolerant tomato variant CL5915-93D4-1-0-3, gene SlUPB1
-
-
Manually annotated by BRENDA team
heat-tolerant tomato variant CL5915-93D4-1-0-3, gene SlUPB1
-
-
Manually annotated by BRENDA team
heat-sensitive tomato variant, gene SlUPB1
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-amino-3-ureidopropionic acid + H2O
3-aminoalanine + CO2 + NH3
show the reaction diagram
2-methyl-3-ureidopropionic acid + H2O
3-amino-2-methylpropanoic acid + NH3 + CO2
show the reaction diagram
82% activity in comparison to 3-ureidopropionic acid
-
-
?
2-methyl-3-ureidopropionic acid + H2O
alpha-methyl-beta-alanine + CO2 + NH3
show the reaction diagram
2-methyl-N-carbamoyl-beta-alanine + H2O
2-methyl-beta-alanine + CO2 + NH3
show the reaction diagram
2-phenyl-3-ureidopropionic acid + H2O
3-amino-2-phenylpropanoic acid + CO2 + NH3
show the reaction diagram
2-ureidoethane phosphonic acid + H2O
ciliatine + CO2 + NH3
show the reaction diagram
2-ureidoethanesulfonic acid + H2O
taurine + CO2 + NH3
show the reaction diagram
-
-
-
-
?
3-methyl-3-ureidopropionic acid + H2O
beta-homoalanine + CO2 + NH3
show the reaction diagram
-
-
-
-
?
3-ureidobutyrate + H2O
2-methyl-beta-alanine + CO2 + NH3
show the reaction diagram
3-ureidopropanoate + H2O
beta-alanine + CO2 + NH3
show the reaction diagram
3-ureidopropionic acid + H2O
beta-alanine + CO2 + NH3
show the reaction diagram
4-amino-4-oxobutyric acid + H2O
?
show the reaction diagram
3% activity in comparison to 3-ureidopropionic acid
-
-
?
DL-beta-ureidobutyric acid + H2O
?
show the reaction diagram
-
-
-
-
?
gamma-ureido-n-butyric acid + H2O
4-aminobutanoate + CO2 + NH3
show the reaction diagram
-
-
-
-
?
N-acetyl-beta-alanine + H2O
?
show the reaction diagram
-
-
-
-
?
N-acetyl-DL-alanine + H2O
?
show the reaction diagram
-
-
-
-
?
N-acetyl-L-alanine + H2O
?
show the reaction diagram
-
-
-
-
?
N-acetyl-L-methionine + H2O
?
show the reaction diagram
-
-
-
-
?
N-carbamoyl-5-aminopentanoate + H2O
5-aminopentanoate + CO2 + NH3
show the reaction diagram
-
-
-
-
?
N-carbamoyl-alpha-amino-beta-alanine + H2O
2,3-diaminopropanoate + CO2 + NH3
show the reaction diagram
-
-
-
-
?
N-carbamoyl-alpha-methyl-beta-alanine + H2O
3-amino-2-methylpropanoic acid + CO2 + NH3
show the reaction diagram
-
-
-
-
?
N-carbamoyl-alpha-phenyl-beta-alanine + H2O
3-amino-2-phenylpropanoic acid + CO2 + NH3
show the reaction diagram
-
-
-
-
?
N-carbamoyl-beta-alanine + H2O
?
show the reaction diagram
N-carbamoyl-beta-alanine + H2O
beta-alanine + CO2 + NH3
show the reaction diagram
N-carbamoyl-beta-alanine + H2O
beta-alanine + NH3 + CO2
show the reaction diagram
-
-
-
-
?
N-carbamoyl-beta-aminoisobutyrate + H2O
beta-aminoisobutyrate + CO2 + NH3
show the reaction diagram
N-carbamoyl-beta-aminoisobutyric acid + H2O
beta-aminoisobutyric acid + NH3 + CO2
show the reaction diagram
-
-
-
-
?
N-carbamoyl-beta-homoalanine + H2O
beta-homoalanine + CO2 + NH3
show the reaction diagram
-
-
-
-
?
N-carbamoyl-ciliatine + H2O
ciliatine + CO2 + NH3
show the reaction diagram
-
-
-
-
?
N-carbamoyl-D-ornithine + H2O
D-ornithine + CO2 + NH3
show the reaction diagram
-
-
-
-
?
N-carbamoyl-DL-2-aminovaleric acid + H2O
2-aminopentanoate + CO2 + NH3
show the reaction diagram
-
-
-
-
?
N-carbamoyl-DL-alanine + H2O
DL-alanine + CO2 + NH3
show the reaction diagram
-
poor substrate, relative enzyme activity 4%
-
-
?
N-carbamoyl-DL-beta-aminoisobutyrate + H2O
DL-beta-aminoisobutyrate + CO2 + NH3
show the reaction diagram
N-carbamoyl-GABA + H2O
4-aminobutanoic acid + CO2 + NH3
show the reaction diagram
-
-
-
-
?
N-carbamoyl-gamma-amino-beta-hydroxybutyric acid + H2O
?
show the reaction diagram
-
-
-
-
?
N-carbamoyl-glycine + H2O
glycine + CO2 + NH3
show the reaction diagram
N-carbamoyl-homoisoserine + H2O
homoisoserine + CO2 + NH3
show the reaction diagram
-
-
-
-
?
N-carbamoyl-L-alanine + H2O
L-alanine + CO2 + NH3
show the reaction diagram
N-carbamoyl-L-methionine + H2O
L-methionine + CO2 + NH3
show the reaction diagram
N-carbamoyl-L-ornithine + H2O
L-ornithine + CO2 + NH3
show the reaction diagram
-
-
-
-
?
N-carbamoyl-L-phenylalanine + H2O
L-phenylalanine + CO2 + NH3
show the reaction diagram
N-carbamoyl-L-serine + H2O
L-serine + CO2 + NH3
show the reaction diagram
-
-
-
-
?
N-carbamoyl-taurine + H2O
taurine + CO2 + NH3
show the reaction diagram
-
-
-
-
?
N-carbamoylglycine + H2O
glycine + CO2 + NH3
show the reaction diagram
N-carbamyl-beta-alanine + H2O
beta-alanine + CO2 + NH3
show the reaction diagram
-
-
-
-
?
N-carbamyl-beta-aminoisobutyrate + H2O
beta-aminoisobutyrate + CO2 + NH3
show the reaction diagram
-
-
-
-
?
N-formyl-DL-alanine + H2O
?
show the reaction diagram
-
-
-
-
?
N-formyl-L-methionine + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2-methyl-N-carbamoyl-beta-alanine + H2O
2-methyl-beta-alanine + CO2 + NH3
show the reaction diagram
3-ureidobutyrate + H2O
2-methyl-beta-alanine + CO2 + NH3
show the reaction diagram
3-ureidopropanoate + H2O
beta-alanine + CO2 + NH3
show the reaction diagram
N-carbamoyl-beta-alanine + H2O
?
show the reaction diagram
N-carbamoyl-beta-alanine + H2O
beta-alanine + CO2 + NH3
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(R)-2-phenylpropionic acid
-
IC50: 0.115 mM
(RS)-2-(2,6-dinitrophenoxy)-propionate
-
most potent inhibitor of aryl propionates, IC50: 500 nM, completely reversible by passing the enzyme-inhibitor complex over a gel filtration column
-
(RS)-2-benzylpropionic acid
-
IC50: 0.006 mM
-
(S)-2-phenylpropionic acid
-
IC50: 0.0057 mM
1,10-phenanthroline
-
1 mM, 96% inhibition, activity can be partially restored by Zn2+
2,2'-dipyridyl
-
2 mM 70% inhibition
2,6-dipicolinic acid
-
1 mM, 33% inhibition
2-methyl-beta-alanine
-
product inhibition, the presence of product leads to dissociation of hexamers to inactive trimers
2-methyl-N-carbamoyl-beta-alanine
-
competitive inhibitor of the reaction with N-carbamoyl-beta-alanine
-
3-Phenylpropionic acid
-
IC50: 0.0056 mM
4-ureidobutyrate
-
-
5,5'-dithiobis-(2-nitrobenzoic acid)
-
-
8-hydroxyquinoline
8-Hydroxyquinoline-5-sulfonic acid
-
-
acetate
-
competitive inhibition
Alpha-fluoroacetate
-
competitive inhibition
beta-Alanine
Beta-ureidoisobutyric acid
-
competitive inhibition
beta-ureidopropionate
-
competitive inhibition
Chloramphenicol
cyclopropanecarboxylic acid
-
IC50: 0.008 mM
ethylendiaminetetraacetate
-
2 mM 100% inhibition
gamma-aminobutyrate
glutarate monoamide
-
-
iodoacetamide
-
1 mM, complete inhibition, completely prevented by addition of substrate, the sensitive thiol group is located at the active site
Isobutyrate
isobutyric acid
-
IC50: 0.018 mM
N-Amidino-beta-alanine
-
-
n-butyric acid
-
IC50: 0.055 mM
N-carbamoyl-D-alanine
-
-
N-carbamoyl-L-leucine
-
-
N-Carbamoylglycine
-
-
N-ethylmaleimide
-
-
o-phenanthroline
-
2 mM 93% inhibition
p-chloromercuribenzenesulfonic acid
-
complete inhibition
p-chloromercuribenzoic acid
-
-
phenylhydrazine
-
49% inhibition
Propionate
Propionic acid
-
IC50: 0.025 mM
Semicarbazide
-
78% inhibition
sodium propionate
additional information
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.07
2-amino-3-ureidopropionic acid
-
-
6.59
2-methyl-3-ureidopropionic acid
-
-
0.006
2-methyl-N-carbamoyl-beta-alanine
84.37
2-phenyl-3-ureidopropionic acid
-
-
20.15
2-ureidoethane phosphonic acid
-
-
10.58
2-ureidoethanesulfonic acid
-
-
3.44
3-methyl-3-ureidopropionic acid
-
-
0.147 - 2.14
3-ureidopropionic acid
0.018
Beta-ureidoisobutyric acid
-
-
0.038 - 3.74
beta-ureidopropionic acid
4.52
DL-beta-ureidobutyric acid
-
-
11.6
gamma-ureido-n-butyrate
-
-
169.2
N-Acetyl-beta-alanine
-
pH 8.0, 30C
8.78
N-acetyl-DL-alanine
-
-
2.96
N-acetyl-L-alanine
-
pH 8.0, 30C
0.84
N-acetyl-L-methionine
-
pH 8.0, 30C
1.69
N-carbamoyl-5-aminopentanoate
-
pH 8.0, 30C
0.07
N-carbamoyl-alpha-amino-beta-alanine
-
pH 8.0, 30C
6.5
N-carbamoyl-alpha-methyl-beta-alanine
-
pH 8.0, 30C
84.38
N-carbamoyl-alpha-phenyl-beta-alanine
-
pH 8.0, 30C
0.0065 - 60
N-Carbamoyl-beta-alanine
1 - 2.81
N-carbamoyl-beta-aminoisobutyric acid
3.44
N-carbamoyl-beta-homoalanine
-
pH 8.0, 30C
20.15
N-carbamoyl-ciliatine
-
pH 8.0, 30C
9.09
N-carbamoyl-D-ornithine
-
pH 8.0, 30C
42.3
N-carbamoyl-DL-2-aminovaleric acid
-
-
5.17
N-carbamoyl-GABA
-
pH 8.0, 30C
6.94
N-carbamoyl-gamma-amino-beta-hydroxybutyric acid
-
pH 8.0, 30C
4.75
N-Carbamoyl-glycine
-
pH 8.0, 30C
6.55
N-carbamoyl-homoisoserine
-
pH 8.0, 30C
0.26
N-carbamoyl-L-alanine
-
pH 8.0, 30C
0.11
N-carbamoyl-L-methionine
-
pH 8.0, 30C
9.47
N-carbamoyl-L-ornithine
-
pH 8.0, 30C
0.89
N-carbamoyl-L-phenylalanine
-
pH 8.0, 30C
75.1
N-carbamoyl-L-serine
-
-
10.58
N-carbamoyl-taurine
-
pH 8.0, 30C
0.68
N-Carbamoylglycine
-
-
7.71
N-formyl-DL-alanine
-
-
6.01
N-formyl-L-methionine
-
pH 8.0, 30C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.15
2-amino-3-ureidopropionic acid
Agrobacterium tumefaciens
-
-
24.39
2-methyl-3-ureidopropionic acid
Agrobacterium tumefaciens
-
-
0.13
2-phenyl-3-ureidopropionic acid
Agrobacterium tumefaciens
-
-
0.23
2-ureidoethane phosphonic acid
Agrobacterium tumefaciens
-
-
5.84
2-ureidoethanesulfonic acid
Agrobacterium tumefaciens
-
-
0.2
3-methyl-3-ureidopropionic acid
Agrobacterium tumefaciens
-
-
25.71
3-ureidopropionic acid
Agrobacterium tumefaciens
-
-
3.93
N-Acetyl-beta-alanine
Agrobacterium tumefaciens
-
pH 8.0, 30C
0.89
N-acetyl-L-alanine
Agrobacterium tumefaciens
-
pH 8.0, 30C
0.15
N-acetyl-L-methionine
Agrobacterium tumefaciens
-
pH 8.0, 30C
2.28
N-carbamoyl-5-aminopentanoate
Agrobacterium tumefaciens
-
pH 8.0, 30C
0.15
N-carbamoyl-alpha-amino-beta-alanine
Agrobacterium tumefaciens
-
pH 8.0, 30C
24.39
N-carbamoyl-alpha-methyl-beta-alanine
Agrobacterium tumefaciens
-
pH 8.0, 30C
0.13
N-carbamoyl-alpha-phenyl-beta-alanine
Agrobacterium tumefaciens
-
pH 8.0, 30C
0.005 - 25.71
N-Carbamoyl-beta-alanine
0.21
N-carbamoyl-beta-homoalanine
Agrobacterium tumefaciens
-
pH 8.0, 30C
0.23
N-carbamoyl-ciliatine
Agrobacterium tumefaciens
-
pH 8.0, 30C
0.01
N-carbamoyl-D-ornithine
Agrobacterium tumefaciens
-
pH 8.0, 30C
24.03
N-carbamoyl-GABA
Agrobacterium tumefaciens
-
pH 8.0, 30C
1.95
N-carbamoyl-gamma-amino-beta-hydroxybutyric acid
Agrobacterium tumefaciens
-
pH 8.0, 30C
21.88
N-Carbamoyl-glycine
Agrobacterium tumefaciens
-
pH 8.0, 30C
4.27
N-carbamoyl-homoisoserine
Agrobacterium tumefaciens
-
pH 8.0, 30C
6.27
N-carbamoyl-L-alanine
Agrobacterium tumefaciens
-
pH 8.0, 30C
8.64
N-carbamoyl-L-methionine
Agrobacterium tumefaciens
-
pH 8.0, 30C
0.08
N-carbamoyl-L-ornithine
Agrobacterium tumefaciens
-
pH 8.0, 30C
5.81
N-carbamoyl-L-phenylalanine
Agrobacterium tumefaciens
-
pH 8.0, 30C
5.84
N-carbamoyl-taurine
Agrobacterium tumefaciens
-
pH 8.0, 30C
23.03
N-formyl-L-methionine
Agrobacterium tumefaciens
-
pH 8.0, 30C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.02
N-Acetyl-beta-alanine
Agrobacterium tumefaciens
-
pH 8.0, 30C
10716
0.3
N-acetyl-L-alanine
Agrobacterium tumefaciens
-
pH 8.0, 30C
2972
0.18
N-acetyl-L-methionine
Agrobacterium tumefaciens
-
pH 8.0, 30C
1165
1.35
N-carbamoyl-5-aminopentanoate
Agrobacterium tumefaciens
-
pH 8.0, 30C
42239
2.14
N-carbamoyl-alpha-amino-beta-alanine
Agrobacterium tumefaciens
-
pH 8.0, 30C
42231
3.7
N-carbamoyl-alpha-methyl-beta-alanine
Agrobacterium tumefaciens
-
pH 8.0, 30C
42232
0.00154
N-carbamoyl-alpha-phenyl-beta-alanine
Agrobacterium tumefaciens
-
pH 8.0, 30C
42233
12.01
N-Carbamoyl-beta-alanine
Agrobacterium tumefaciens
-
pH 8.0, 30C
1829
0.06
N-carbamoyl-beta-homoalanine
Agrobacterium tumefaciens
-
pH 8.0, 30C
42230
0.01
N-carbamoyl-ciliatine
Agrobacterium tumefaciens
-
pH 8.0, 30C
42235
0.00882
N-carbamoyl-D-ornithine
Agrobacterium tumefaciens
-
pH 8.0, 30C
42240
4.65
N-carbamoyl-GABA
Agrobacterium tumefaciens
-
pH 8.0, 30C
42236
0.28
N-carbamoyl-gamma-amino-beta-hydroxybutyric acid
Agrobacterium tumefaciens
-
pH 8.0, 30C
42237
4.61
N-Carbamoyl-glycine
Agrobacterium tumefaciens
-
pH 8.0, 30C
15862
0.65
N-carbamoyl-homoisoserine
Agrobacterium tumefaciens
-
pH 8.0, 30C
42238
24.12
N-carbamoyl-L-alanine
Agrobacterium tumefaciens
-
pH 8.0, 30C
8412
78.55
N-carbamoyl-L-methionine
Agrobacterium tumefaciens
-
pH 8.0, 30C
4105
0.0017
N-carbamoyl-L-ornithine
Agrobacterium tumefaciens
-
pH 8.0, 30C
24602
6.53
N-carbamoyl-L-phenylalanine
Agrobacterium tumefaciens
-
pH 8.0, 30C
9551
0.55
N-carbamoyl-taurine
Agrobacterium tumefaciens
-
pH 8.0, 30C
42234
3.83
N-formyl-L-methionine
Agrobacterium tumefaciens
-
pH 8.0, 30C
4839
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.9
2-methyl-beta-alanine
-
-
0.0016
4-ureidobutyrate
-
-
1.1
beta-Alanine
-
-
1.6
gamma-aminobutyrate
-
-
0.63
glutarate monoamide
-
-
0.09 - 0.24
Propionate
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.115
(R)-2-phenylpropionic acid
Zea mays
-
IC50: 0.115 mM
0.0005
(RS)-2-(2,6-dinitrophenoxy)-propionate
Zea mays
-
most potent inhibitor of aryl propionates, IC50: 500 nM, completely reversible by passing the enzyme-inhibitor complex over a gel filtration column
-
0.006
(RS)-2-benzylpropionic acid
Zea mays
-
IC50: 0.006 mM
-
0.0057
(S)-2-phenylpropionic acid
Zea mays
-
IC50: 0.0057 mM
0.0056
3-Phenylpropionic acid
Zea mays
-
IC50: 0.0056 mM
0.008
cyclopropanecarboxylic acid
Zea mays
-
IC50: 0.008 mM
0.018
isobutyric acid
Zea mays
-
IC50: 0.018 mM
0.055
n-butyric acid
Zea mays
-
IC50: 0.055 mM
0.025
Propionic acid
Zea mays
-
IC50: 0.025 mM
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00000006
-
nitrogen source ammonium sulfate, carbon source succinate
0.00000008
-
nitrogen source ammonium sulfate, carbon source glucose
0.00000032
-
nitrogen source beta-alanine, carbon source glucose
0.00000062
-
nitrogen source aminoisobutyric acid, carbon source glucose
0.00000208
-
nitrogen source uracil, carbon source glucose
0.00000252
-
nitrogen source dihydrouracil, carbon source glucose
0.00000312
-
-
0.00000333
-
nitrogen source cytosine, carbon source glucose
0.00000412
-
nitrogen source 5-methylcytosine, carbon source glucose
0.00000867
-
nitrogen source thymine, carbon source glucose
0.0000155
Blastobacter sp.
-
-
0.0009
-
0.1 M Tris-HCl buffer (pH 7.5), 10 mM MgCl2, at 30C
0.005
-
nitrogen source 6 mM NH4Cl
0.0167
-
purified recombinant detagged mutant L13S, pH and temperature not specified in the publication
0.03
-
recombinant beta-UP
0.041
-
nitrogen source 1 mM NH4Cl
0.048
-
nitrogen source 3 mM uracil
0.0558
-
purified recombinant detagged mutant S264R, pH and temperature not specified in the publication
0.084
Pigeon
-
-
0.282
-
purified recombinant detagged wild-type enzyme, pH and temperature not specified in the publication
0.88
-
N-carbamoyl-beta-alanine as substrate
1.84
-
purified enzyme at pH 7, 38C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 7.2
-
broad optimum at mildly acidic pH values
7 - 8
broad optimum
7 - 7.5
-
-
7.4 - 7.8
Clostridium uracilicum
-
-
7.5 - 8
Clostridium uracilicum
-
-
7.5 - 8.2
-
-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.3 - 8.3
-
-
6 - 10.5
Clostridium uracilicum
-
-
additional information
-
activity declines at more alkaline pH values
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
assay at
30 - 35
Clostridium uracilicum
-
-
40
unstable, 65 s half-life
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 50
Clostridium uracilicum
-
-
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
-
recombinant beta-UP, isoelectric focusing
7.1
-
recombinant beta-UP, sequence calculation
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
expression anaylsis, overview
Manually annotated by BRENDA team
-
of etiolated seedlings
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
recombinant beta-UP expressed in Escherichia coli BL21
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
43160
amino acid sequence calculation
44040
-
amino acid sequence calculation
95000
-
gel filtration
234000
-
gel filtration
235000
-
gel filtration, native enzyme in absence of ligands
240000
-
gel filtration
323000
-
sucrose density gradient centrifugation
327000
-
gel filtration
340000
-
gel filtration
400000
-
above, native state of beta-UP, gel filtration at pH 7.3, in the presence of 5% v/v glycerol
440000
-
native state of beta-UP, gel filtration
472000
gel filtration, blue native PAGE
1500000 - 2000000
-
gel filtration
additional information
-
native oligomerization state: 1.5 - 2 MDa
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decamer
dodecamer
hexamer
homodecamer
homodimer
homohexamer
polymer
-
1500000-2000000, no subunit molecular weight reported
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
additional information
-
subunit: 44000 Da
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
-
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
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.1 - 10.7
-
-
172065
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
65
-
80% activity lost at 70C
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
dithiothreitol and glycerol stabilize
-
stored in 50% glycerol without gross denaturation
-
the hexamer is a stable enzyme species, detergents, e.g. 3% v/v CHAPSO or CHAPS, and reducing thiols stabilize purified enzyme in solution, 1 mM dithiothreitol stabilizes
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-25C 50% decrease in specific activity within a few days 4C, 50% glycerol solution 20% decrease in activity at 1 month, 50% decrease at 2 months of storage
-
-70C, partially purified beta-UP, in presence of 10% w/v glycerol, several months, stable
-
4C, 50 mM Tris buffer with 10% glycerol + 10 mM 2-mercaptoethanol or 2 mM dithiothreitol enzyme loses less than 20% activity when maintained for 3 days
-
4C, buffer without stabilizing detergents and reducing thiols, 26 days, almost complete loss of activity
-
4C, partially purified beta-UP, in presence of Mg2+ and dithiothreitol, 7 days, about 10% loss of activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
immobilized metal ion affinity chromatography (Ni2+)
immobilized metal ion affinity chromatography, gel filtration
-
partial
-
partially
purified 1000fold
-
recombinant beta-UP
-
recombinant betaAS
-
recombinant SkbetaAS
-
recombinant wild-type and mutant enzymes from Escherichia coli strain C41(DE3)pRARE2 by nickel affinity chromatography, desalting gel filtration, and cleavage of the tag by His-tagged 3C protease, followed by gel filtration and anion exchange chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cDNA encoding human beta-ureidopropionase gene, BUP-1 cloned, plasmid yc28d10.r1 sequenced and expressed in Escherichia coli BL21, eukaryotic expression vector pCR3 transfected to COS-7-cells
cDNA truncated at the N-terminus by 14 residues, overexpression in Escherichia coli BL21
-
expression in Escherichia coli B843(DE3)
-
expression of GFP-tagged PYD3 in Arabdiopsis thaliana via Agrobacterium-mediated transformation using the floral dip method. Quantitative real-time RT-PCR analysis of PYD expression in wild-type and pyd mutants, overview
gene SIUPB1, cloning, transgenic overexpression, and expression analysis; gene SIUPB1, cloning, transgenic overexpression by Agrobacterium tumefaciens-mediated transformation, and expression analysis
-
gene UPB1
-
gene UPB1, DNA and amino acid sequence determination and analysis, genotyping, reverse transcription and quantitative real-time PCR enzyme expression analysis, overview
-
gene UPB1, genotyping
-
gene UPB1, located on chromosome 22q11.2, DNA and amino acid sequence determination and analysis, expression of wild-type and mutant enzymes in HEK293 cells
-
gene UPB1, located on chromosome 22q11.2, DNA and amino acid sequence determination and analysis, sequence comparisons and genomic organization analysis, genotyping of beta-ureidopropionase deficient patients as well as the analysis of the mutations in a three-dimensional framework, PCR enzyme expression analysis, overview. Recombinant heterologous expression of wild-type and mutant enzymes in Escherichia coli strain C41(DE3)pRARE2, all mutations yield mutant beta-ureidopropionase proteins with significantly decreased activity
-
hexahistidine fusion protein expressed in Escherichia coli BL21-CodonPlus (DE3)-RIL
His-tagged version expressed in Escherichia coli
-
mutation A85E is introduced into the wild-type UPB1 plasmid using site-directed mutagenesis. The mutated plasmid is then transfected into the RKO cell line
-
ENGINEERING
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
-
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
-
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
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
L13S
-
naturally occuring mutation and site-directed mutagenesis, the mutation results in folding defects and oligomer assembly impairment, the mutant shows reduced activity compared to the wild-type enzyme
R236W
-
naturally occuring mutation and site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
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
T359M
-
naturally occuring mutation and site-directed mutagenesis, the mutation results in folding defects and oligomer assembly impairment, the mutant shows highly reduced activity compared to the wild-type enzyme
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
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
Show AA Sequence (212 entries)
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