Information 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.
Specify your search results
Mark a special word or phrase in this record:
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


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

EC NUMBER
COMMENTARY
3.5.1.6
-
RECOMMENDED NAME
GeneOntology No.
beta-ureidopropionase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
N-carbamoyl-beta-alanine + H2O = beta-alanine + CO2 + NH3
show the reaction diagram
-
-
-
-
N-carbamoyl-beta-alanine + H2O = beta-alanine + CO2 + NH3
show the reaction diagram
the animal enzyme also acts on beta-ureidoisobutyrate
-
N-carbamoyl-beta-alanine + H2O = beta-alanine + CO2 + NH3
show the reaction diagram
detailed reaction mechanism, catalytic mechanism
-
N-carbamoyl-beta-alanine + H2O = beta-alanine + CO2 + NH3
show the reaction diagram
mechanism
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hydrolysis of linear amides
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
beta-Alanine metabolism
-
Drug metabolism - other enzymes
-
Metabolic pathways
-
Pantothenate and CoA biosynthesis
-
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.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3-ureidopropionase
Q19437
-
beta-Ala synthase
-
-
beta-alanine synthase
Q19437
-
beta-alanine synthase
Clostridium uracilicum
-
-
beta-alanine synthase
Clostridium uracilicum M5-2
-
-
-
beta-alanine synthase
-
-
beta-alanine synthase
-
-
beta-alanine synthase
-
-
beta-alanine synthase
-
-
beta-alanine synthase
-
-
beta-alanine synthase
-
-
beta-alanine synthase
-
-
beta-alanine synthase
-
-
beta-alanine synthase
-
-
beta-ureidopropionase
Q8H183
-
beta-ureidopropionate decarbamylase
Clostridium uracilicum
-
-
beta-ureidopropionate decarbamylase
Clostridium uracilicum M5-2
-
-
-
beta-ureidopropionate decarbamylase
-
-
betaUPase
-
-
BUP-1
-
-
human liver beta-ureidopropionase
-
-
N-carbamoyl-beta-Ala amidohydrolase
-
-
N-carbamoyl-beta-alanine amidohydrolase
-
-
-
-
N-carbamoyl-beta-alanine amidohydrolase
-
-
N-carbamoyl-beta-alanine amidohydrolase
-
-
N-carbamyl-beta-alanine decarbamylase
Clostridium uracilicum
-
-
N-carbamyl-beta-alanine decarbamylase
Clostridium uracilicum M5-2
-
-
-
NCbetaA
-
-
SkbetaAS
-
Saccharomyces kluyveri betaAS
CAS REGISTRY NUMBER
COMMENTARY
9027-27-4
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
strain C58, ATCC 33970
-
-
Manually annotated by BRENDA team
Blastobacter sp.
A17p-4
-
-
Manually annotated by BRENDA team
calf
-
-
Manually annotated by BRENDA team
plant pathogen, opportunistic pathogen in humans, ATCC 25416
-
-
Manually annotated by BRENDA team
Clostridium uracilicum
-
-
-
Manually annotated by BRENDA team
Clostridium uracilicum
strain M5-2
-
-
Manually annotated by BRENDA team
Clostridium uracilicum M5-2
strain M5-2
-
-
Manually annotated by BRENDA team
E222c
-
-
Manually annotated by BRENDA team
Comamonas sp. E222c
E222c
-
-
Manually annotated by BRENDA team
pyd3 mutations are viable and fertile as homozygotes and no morphological changes are evident in these flies
-
-
Manually annotated by BRENDA team
plant-like unicellular flagellate
-
-
Manually annotated by BRENDA team
gene UPB1
-
-
Manually annotated by BRENDA team
human
-
-
Manually annotated by BRENDA team
Pigeon
-
-
-
Manually annotated by BRENDA team
biotype B, strain ATCC 17536
-
-
Manually annotated by BRENDA team
rat; Sprague-Dawley rats, CD strain
-
-
Manually annotated by BRENDA team
Rattus rattus Cd
Sprague-Dawley rats, CD strain
-
-
Manually annotated by BRENDA team
facultative phototrophic bacterium, strain R10
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
metabolism
Q8H183
PYD3 is involved in the reductive pathway for the degradation of pyrimidine nucleotides, functional and mutational analysis of the catabolic pathway, overview
additional information
-
screening for genetic deficiency in betaUPase, GC/MS analysis of urine metabolome. Patients 1, 2, 3 and 4 are asymptomatic and patients 5 and 6 have autism and West syndrome, respectively. In the disorders in the first and second steps of pyrimidine degradation, the clinical presentation and disease severity varies considerably, even among patients in the same family
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
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
alpha-methyl-beta-alanine + CO2 + NH3
show the reaction diagram
-
-
-
-
?
2-methyl-3-ureidopropionic acid + H2O
3-amino-2-methylpropanoic acid + NH3 + CO2
show the reaction diagram
-, Q19437
82% activity in comparison to 3-ureidopropionic acid
-
-
?
2-methyl-N-carbamoyl-beta-alanine + H2O
2-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-methyl-N-carbamoyl-beta-alanine + H2O
2-methyl-beta-alanine + CO2 + NH3
show the reaction diagram
Q96W94
betaAS is the final enzyme of the reductive pyrimidine catabolic pathway, which is responsible for the breakdown of the pyrimidine bases uracil and thymine
-
-
?
2-methyl-N-carbamoyl-beta-alanine + H2O
2-methyl-beta-alanine + CO2 + NH3
show the reaction diagram
-
completes the catabolism of the pyrimidine bases uracil and thymine
-
-
?
2-methyl-N-carbamoyl-beta-alanine + H2O
2-methyl-beta-alanine + CO2 + NH3
show the reaction diagram
-
final enzyme of the catabolic pathway of pyrimidine bases, substrate derives from thymine
-
-
?
2-methyl-N-carbamoyl-beta-alanine + H2O
2-methyl-beta-alanine + CO2 + NH3
show the reaction diagram
Q96W94
catalytic mechanism, substrate-binding residues
-
-
?
2-methyl-N-carbamoyl-beta-alanine + H2O
2-methyl-beta-alanine + CO2 + NH3
show the reaction diagram
-
only one enantiomer of the racemic substrate is hydrolyzed
-
-
?
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-ureidopropionic acid + H2O
beta-alanine + CO2 + NH3
show the reaction diagram
-
-
-
-
?
3-ureidopropionic acid + H2O
beta-alanine + CO2 + NH3
show the reaction diagram
-, Q19437
-
-
-
?
4-amino-4-oxobutyric acid + H2O
?
show the reaction diagram
-, Q19437
3% activity in comparison to 3-ureidopropionic acid
-
-
?
DL-beta-ureidobutyric acid + H2O
?
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
beta-alanine + CO2 + NH3
show the reaction diagram
-
-
-
-
?
N-carbamoyl-beta-alanine + H2O
beta-alanine + CO2 + NH3
show the reaction diagram
-
-
-
-
ir
N-carbamoyl-beta-alanine + H2O
beta-alanine + CO2 + NH3
show the reaction diagram
-
-
-
-
?
N-carbamoyl-beta-alanine + H2O
beta-alanine + CO2 + NH3
show the reaction diagram
-
-
-
-
?
N-carbamoyl-beta-alanine + H2O
beta-alanine + CO2 + NH3
show the reaction diagram
-
-
-
-
?
N-carbamoyl-beta-alanine + H2O
beta-alanine + CO2 + NH3
show the reaction diagram
-
-
-
-
?
N-carbamoyl-beta-alanine + H2O
beta-alanine + CO2 + NH3
show the reaction diagram
-
-
-
-
?
N-carbamoyl-beta-alanine + H2O
beta-alanine + CO2 + NH3
show the reaction diagram
-
-
-
-
?
N-carbamoyl-beta-alanine + H2O
beta-alanine + CO2 + NH3
show the reaction diagram
-
-
-
-
ir
N-carbamoyl-beta-alanine + H2O
beta-alanine + CO2 + NH3
show the reaction diagram
-
-
-
-
ir
N-carbamoyl-beta-alanine + H2O
beta-alanine + CO2 + NH3
show the reaction diagram
-
-
-
-
?
N-carbamoyl-beta-alanine + H2O
beta-alanine + CO2 + NH3
show the reaction diagram
Q8H183
-
-
-
?
N-carbamoyl-beta-alanine + H2O
beta-alanine + CO2 + NH3
show the reaction diagram
Comamonas sp., Blastobacter sp.
-
N-carbamoyl-D-amino acid hydrolyzing activity
-
-
ir
N-carbamoyl-beta-alanine + H2O
beta-alanine + CO2 + NH3
show the reaction diagram
-
L enantiomer specific hydrolysis
-
-
ir
N-carbamoyl-beta-alanine + H2O
beta-alanine + CO2 + NH3
show the reaction diagram
-
L enantiomer specific hydrolysis
-
-
ir
N-carbamoyl-beta-alanine + H2O
beta-alanine + CO2 + NH3
show the reaction diagram
-
L enantiomer specific hydrolysis
-
-
ir
N-carbamoyl-beta-alanine + H2O
beta-alanine + CO2 + NH3
show the reaction diagram
-
L enantiomer specific hydrolysis
-
-
ir
N-carbamoyl-beta-alanine + H2O
beta-alanine + CO2 + NH3
show the reaction diagram
-
L enantiomer specific hydrolysis
-
-
ir
N-carbamoyl-beta-alanine + H2O
beta-alanine + CO2 + NH3
show the reaction diagram
-
L enantiomer specific hydrolysis
-
-
ir
N-carbamoyl-beta-alanine + H2O
beta-alanine + CO2 + NH3
show the reaction diagram
-
L enantiomer specific hydrolysis
-
-
ir
N-carbamoyl-beta-alanine + H2O
beta-alanine + CO2 + NH3
show the reaction diagram
Pigeon
-
L enantiomer specific hydrolysis
-
-
ir
N-carbamoyl-beta-alanine + H2O
beta-alanine + CO2 + NH3
show the reaction diagram
-
L enantiomer specific hydrolysis
-
-
ir
N-carbamoyl-beta-alanine + H2O
beta-alanine + CO2 + NH3
show the reaction diagram
-
L enantiomer specific hydrolysis
-
-
ir
N-carbamoyl-beta-alanine + H2O
beta-alanine + CO2 + NH3
show the reaction diagram
-
L enantiomer specific hydrolysis
-
-
ir
N-carbamoyl-beta-alanine + H2O
beta-alanine + CO2 + NH3
show the reaction diagram
-
L enantiomer specific hydrolysis
-
-
ir
N-carbamoyl-beta-alanine + H2O
beta-alanine + CO2 + NH3
show the reaction diagram
-
L enantiomer specific hydrolysis
-
-
ir
N-carbamoyl-beta-alanine + H2O
beta-alanine + CO2 + NH3
show the reaction diagram
-
L enantiomer specific hydrolysis
-
-
ir
N-carbamoyl-beta-alanine + H2O
beta-alanine + CO2 + NH3
show the reaction diagram
Clostridium uracilicum
-
L enantiomer specific hydrolysis
-
-
ir
N-carbamoyl-beta-alanine + H2O
beta-alanine + CO2 + NH3
show the reaction diagram
Q96W94
betaAS is the final enzyme of the reductive pyrimidine catabolic pathway, which is responsible for the breakdown of the pyrimidine bases uracil and thymine
-
-
?
N-carbamoyl-beta-alanine + H2O
beta-alanine + CO2 + NH3
show the reaction diagram
-
completes the catabolism of the pyrimidine bases uracil and thymine
-
-
?
N-carbamoyl-beta-alanine + H2O
beta-alanine + CO2 + NH3
show the reaction diagram
-
final enzyme of the catabolic pathway of pyrimidine bases, substrate derives from uracil
-
-
?
N-carbamoyl-beta-alanine + H2O
beta-alanine + CO2 + NH3
show the reaction diagram
Q96W94
catalytic mechanism, substrate-binding residues
-
-
?
N-carbamoyl-beta-alanine + H2O
beta-alanine + CO2 + NH3
show the reaction diagram
Rattus rattus Cd
-
L enantiomer specific hydrolysis
-
-
ir
N-carbamoyl-beta-alanine + H2O
beta-alanine + CO2 + NH3
show the reaction diagram
Clostridium uracilicum M5-2
-
L enantiomer specific hydrolysis
-
-
ir
N-carbamoyl-beta-alanine + H2O
beta-alanine + CO2 + NH3
show the reaction diagram
Comamonas sp. E222c
-
N-carbamoyl-D-amino acid hydrolyzing activity
-
-
ir
N-carbamoyl-beta-alanine + H2O
?
show the reaction diagram
-
-
-
-
-
N-carbamoyl-beta-alanine + H2O
?
show the reaction diagram
-
-
-
-
-
N-carbamoyl-beta-alanine + H2O
?
show the reaction diagram
-
-
-
-
-
N-carbamoyl-beta-alanine + H2O
?
show the reaction diagram
Q9UBR1
-
-
-
-
N-carbamoyl-beta-alanine + H2O
?
show the reaction diagram
-
-
-
-
-
N-carbamoyl-beta-alanine + H2O
?
show the reaction diagram
-
-
-
-
-
N-carbamoyl-beta-alanine + H2O
?
show the reaction diagram
-
-
-
-
-
N-carbamoyl-beta-alanine + H2O
?
show the reaction diagram
-
-
-
-
-
N-carbamoyl-beta-alanine + H2O
?
show the reaction diagram
Pigeon
-
-
-
-
-
N-carbamoyl-beta-alanine + H2O
?
show the reaction diagram
-
-
-
-
-
N-carbamoyl-beta-alanine + H2O
?
show the reaction diagram
-
-
-
-
-
N-carbamoyl-beta-alanine + H2O
?
show the reaction diagram
-
-
-
-
-
N-carbamoyl-beta-alanine + H2O
?
show the reaction diagram
-
-
-
-
-
N-carbamoyl-beta-alanine + H2O
?
show the reaction diagram
-
-
-
-
-
N-carbamoyl-beta-alanine + H2O
?
show the reaction diagram
-
-
-
-
-
N-carbamoyl-beta-alanine + H2O
?
show the reaction diagram
Blastobacter sp.
-
-
-
-
-
N-carbamoyl-beta-alanine + H2O
?
show the reaction diagram
-
-
-
-
-
N-carbamoyl-beta-alanine + H2O
?
show the reaction diagram
Clostridium uracilicum
-
-
-
-
-
N-carbamoyl-beta-alanine + H2O
?
show the reaction diagram
Rattus rattus Cd
-
-
-
-
-
N-carbamoyl-beta-alanine + H2O
?
show the reaction diagram
Clostridium uracilicum M5-2
-
-
-
-
-
N-carbamoyl-beta-alanine + H2O
?
show the reaction diagram
Comamonas sp. E222c
-
-
-
-
-
N-carbamoyl-beta-alanine + H2O
beta-alanine + NH3 + CO2
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-DL-beta-aminoisobutyrate + H2O
DL-beta-aminoisobutyrate + CO2 + NH3
show the reaction diagram
-
-
-
-
?
N-carbamoyl-DL-beta-aminoisobutyrate + H2O
DL-beta-aminoisobutyrate + CO2 + NH3
show the reaction diagram
-
-
-
-
?
N-carbamoyl-DL-beta-aminoisobutyrate + H2O
DL-beta-aminoisobutyrate + CO2 + NH3
show the reaction diagram
-
-
-
-
?
N-carbamoyl-DL-beta-aminoisobutyrate + H2O
DL-beta-aminoisobutyrate + CO2 + NH3
show the reaction diagram
-
-
-
-
?
N-carbamoyl-DL-beta-aminoisobutyrate + H2O
DL-beta-aminoisobutyrate + CO2 + NH3
show the reaction diagram
Blastobacter sp.
-
-
-
-
?
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-carbamoylglycine + H2O
glycine + CO2 + NH3
show the reaction diagram
-
poor substrate, relative enzyme activity 1%
-
-
?
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
-
-
-
-
?
gamma-ureido-n-butyric acid + H2O
4-aminobutanoate + CO2 + NH3
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
betaAS catalyzes the terminal reaction of the reductive pyrimidine catabolic pathway
-
-
-
additional information
?
-
Q96W94
detailed enzyme/active site structure, a subunit 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, conformational changes occur during each catalytic cycle
-
-
-
additional information
?
-
-
enzyme shows cooperativity for the substrate and allosteric regulation
-
-
-
additional information
?
-
-
the enzyme is involved in the pyrimidine catabolism
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
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
Q96W94
betaAS is the final enzyme of the reductive pyrimidine catabolic pathway, which is responsible for the breakdown of the pyrimidine bases uracil and thymine
-
-
?
2-methyl-N-carbamoyl-beta-alanine + H2O
2-methyl-beta-alanine + CO2 + NH3
show the reaction diagram
-
completes the catabolism of the pyrimidine bases uracil and thymine
-
-
?
N-carbamoyl-beta-alanine + H2O
beta-alanine + CO2 + NH3
show the reaction diagram
Q8H183
-
-
-
?
N-carbamoyl-beta-alanine + H2O
beta-alanine + CO2 + NH3
show the reaction diagram
Q96W94
betaAS is the final enzyme of the reductive pyrimidine catabolic pathway, which is responsible for the breakdown of the pyrimidine bases uracil and thymine
-
-
?
N-carbamoyl-beta-alanine + H2O
beta-alanine + CO2 + NH3
show the reaction diagram
-
completes the catabolism of the pyrimidine bases uracil and thymine
-
-
?
N-carbamoyl-beta-alanine + H2O
beta-alanine + CO2 + NH3
show the reaction diagram
-
final enzyme of the catabolic pathway of pyrimidine bases, substrate derives from uracil
-
-
?
N-carbamoyl-beta-alanine + H2O
?
show the reaction diagram
-
-
-
-
-
N-carbamoyl-beta-alanine + H2O
?
show the reaction diagram
-
-
-
-
-
N-carbamoyl-beta-alanine + H2O
?
show the reaction diagram
-
-
-
-
-
N-carbamoyl-beta-alanine + H2O
?
show the reaction diagram
Q9UBR1
-
-
-
-
N-carbamoyl-beta-alanine + H2O
?
show the reaction diagram
-
-
-
-
-
N-carbamoyl-beta-alanine + H2O
?
show the reaction diagram
-
-
-
-
-
N-carbamoyl-beta-alanine + H2O
?
show the reaction diagram
-
-
-
-
-
N-carbamoyl-beta-alanine + H2O
?
show the reaction diagram
-
-
-
-
-
N-carbamoyl-beta-alanine + H2O
?
show the reaction diagram
Pigeon
-
-
-
-
-
N-carbamoyl-beta-alanine + H2O
?
show the reaction diagram
-
-
-
-
-
N-carbamoyl-beta-alanine + H2O
?
show the reaction diagram
-
-
-
-
-
N-carbamoyl-beta-alanine + H2O
?
show the reaction diagram
-
-
-
-
-
N-carbamoyl-beta-alanine + H2O
?
show the reaction diagram
-
-
-
-
-
N-carbamoyl-beta-alanine + H2O
?
show the reaction diagram
-
-
-
-
-
N-carbamoyl-beta-alanine + H2O
?
show the reaction diagram
-
-
-
-
-
N-carbamoyl-beta-alanine + H2O
?
show the reaction diagram
Blastobacter sp.
-
-
-
-
-
N-carbamoyl-beta-alanine + H2O
?
show the reaction diagram
-
-
-
-
-
N-carbamoyl-beta-alanine + H2O
?
show the reaction diagram
Clostridium uracilicum
-
-
-
-
-
N-carbamoyl-beta-alanine + H2O
?
show the reaction diagram
Rattus rattus Cd
-
-
-
-
-
N-carbamoyl-beta-alanine + H2O
?
show the reaction diagram
Clostridium uracilicum M5-2
-
-
-
-
-
N-carbamoyl-beta-alanine + H2O
?
show the reaction diagram
Comamonas sp. E222c
-
-
-
-
-
2-methyl-N-carbamoyl-beta-alanine + H2O
2-methyl-beta-alanine + CO2 + NH3
show the reaction diagram
-
final enzyme of the catabolic pathway of pyrimidine bases, substrate derives from thymine
-
-
?
additional information
?
-
-
betaAS catalyzes the terminal reaction of the reductive pyrimidine catabolic pathway
-
-
-
additional information
?
-
-
the enzyme is involved in the pyrimidine catabolism
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Zn2+
-
contains two Zn2+ per subunit, dizinc metal center in the catalytic domain of the subunit representing the active site of enzyme, binding mode
Zn2+
-
contains two tightly bound Zn2+, removal leads to loss of activity
Zn2+
-
Zn2+-dependent enzyme, required as a catalytic cofactor
Zn2+
-
two Zn2+ ions per subunit
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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
-
2 mM 100% inhibition
8-hydroxyquinoline
-
1 mM, 29% inhibition
8-Hydroxyquinoline-5-sulfonic acid
-
-
acetate
-
competitive inhibition
Alpha-fluoroacetate
-
competitive inhibition
beta-Alanine
-
product inhibition
beta-Alanine
-
product inhibition
beta-Alanine
-
product inhibition, the presence of product leads to dissociation of hexamers to inactive trimers
Beta-ureidoisobutyric acid
-
competitive inhibition
beta-ureidopropionate
-
competitive inhibition
Chloramphenicol
-
-
Chloramphenicol
-
1.6fold reduced activity in chloramphenicol-treated cells
Cu2+
-
0.2 mM, complete inhibition
Cu2+
-
strong inhibition
cyclopropanecarboxylic acid
-
IC50: 0.008 mM
EDTA
-
1 mM, 56% inhibition
ethylendiaminetetraacetate
-
2 mM 100% inhibition
gamma-aminobutyrate
-
product analog, product inhibition
gamma-aminobutyrate
-
-
glutarate monoamide
-
-
Hg2+
-
slight inhibition
iodoacetamide
-
1 mM, complete inhibition, completely prevented by addition of substrate, the sensitive thiol group is located at the active site
Isobutyrate
-
competitive inhibition
Isobutyrate
-
-
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
-
competitive inhibition
Propionic acid
-
IC50: 0.025 mM
Semicarbazide
-
78% inhibition
Zn2+
-
slight inhibition
isobutyric acid
-
IC50: 0.018 mM
additional information
-
removal of the enzyme-bound zinc by chelators leads to loss of activity
-
additional information
-
not inhibited by hydroxyurea, acetohydroxamic acid, benzenesulfonamide, 4-carboxybenzenesulfonamide, 4-nitrobenzenesulfonamide, all up to 1 mM, substrate analogs, such as alpha-ureidopropionate, alpha-ureidoisobutyrate, alpha-ureido-n-butyrate, N-carbamoyl-Asp, or product beta-alanine, all up to 2 mM
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.07
-
2-amino-3-ureidopropionic acid
-
-
6.59
-
2-methyl-3-ureidopropionic acid
-
-
0.006
-
2-methyl-N-carbamoyl-beta-alanine
-
-
-
0.006
-
2-methyl-N-carbamoyl-beta-alanine
-
pH 7, 25C
-
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
-
3-ureidopropionic acid
-, Q19437
pH 7.5, 30C
2.14
-
3-ureidopropionic acid
-
-
0.018
-
Beta-ureidoisobutyric acid
-
-
0.038
-
beta-ureidopropionic acid
-
-
0.5
-
beta-ureidopropionic acid
-
-
0.63
-
beta-ureidopropionic acid
Clostridium uracilicum
-
-
3.5
-
beta-ureidopropionic acid
-
-
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
-
N-Carbamoyl-beta-alanine
-
pH 6.8
0.008
-
N-Carbamoyl-beta-alanine
-
-
0.008
-
N-Carbamoyl-beta-alanine
-
-
0.011
-
N-Carbamoyl-beta-alanine
-
pH 7, 25C
0.011
-
N-Carbamoyl-beta-alanine
-
-
0.0155
-
N-Carbamoyl-beta-alanine
-
-
0.0174
-
N-Carbamoyl-beta-alanine
-
pH 7.4
0.022
-
N-Carbamoyl-beta-alanine
-
-
0.0235
0.5
N-Carbamoyl-beta-alanine
-
pH dependent
0.0235
-
N-Carbamoyl-beta-alanine
-
-
0.032
-
N-Carbamoyl-beta-alanine
-
pH 8.1
0.038
-
N-Carbamoyl-beta-alanine
-
-
0.634
-
N-Carbamoyl-beta-alanine
Clostridium uracilicum
-
-
1.56
-
N-Carbamoyl-beta-alanine
-
-
2.14
-
N-Carbamoyl-beta-alanine
-
pH 8.0, 30C
4
-
N-Carbamoyl-beta-alanine
-
-
50
-
N-Carbamoyl-beta-alanine
-
value above 50 mM
60
-
N-Carbamoyl-beta-alanine
-
wild-type enzyme
1
-
N-carbamoyl-beta-aminoisobutyric acid
-
-
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]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.15
-
2-amino-3-ureidopropionic acid
-
-
24.39
-
2-methyl-3-ureidopropionic acid
-
-
0.13
-
2-phenyl-3-ureidopropionic acid
-
-
0.23
-
2-ureidoethane phosphonic acid
-
-
5.84
-
2-ureidoethanesulfonic acid
-
-
0.2
-
3-methyl-3-ureidopropionic acid
-
-
25.71
-
3-ureidopropionic acid
-
-
3.93
-
N-Acetyl-beta-alanine
-
pH 8.0, 30C
0.89
-
N-acetyl-L-alanine
-
pH 8.0, 30C
0.15
-
N-acetyl-L-methionine
-
pH 8.0, 30C
2.28
-
N-carbamoyl-5-aminopentanoate
-
pH 8.0, 30C
-
0.15
-
N-carbamoyl-alpha-amino-beta-alanine
-
pH 8.0, 30C
-
24.39
-
N-carbamoyl-alpha-methyl-beta-alanine
-
pH 8.0, 30C
-
0.13
-
N-carbamoyl-alpha-phenyl-beta-alanine
-
pH 8.0, 30C
-
0.005
-
N-Carbamoyl-beta-alanine
-
mutant enzyme E159A; mutant enzyme E159D
0.0077
-
N-Carbamoyl-beta-alanine
-
mutant enzyme R322A
0.38
-
N-Carbamoyl-beta-alanine
-
mutant enzyme H397N
0.47
-
N-Carbamoyl-beta-alanine
-
mutant enzyme H262A
0.6
-
N-Carbamoyl-beta-alanine
-
-
5.3
-
N-Carbamoyl-beta-alanine
-
wild-type enzyme
25.71
-
N-Carbamoyl-beta-alanine
-
pH 8.0, 30C
0.21
-
N-carbamoyl-beta-homoalanine
-
pH 8.0, 30C
-
0.23
-
N-carbamoyl-ciliatine
-
pH 8.0, 30C
-
0.01
-
N-carbamoyl-D-ornithine
-
pH 8.0, 30C
-
24.03
-
N-carbamoyl-GABA
-
pH 8.0, 30C
-
1.95
-
N-carbamoyl-gamma-amino-beta-hydroxybutyric acid
-
pH 8.0, 30C
-
21.88
-
N-Carbamoyl-glycine
-
pH 8.0, 30C
4.27
-
N-carbamoyl-homoisoserine
-
pH 8.0, 30C
-
6.27
-
N-carbamoyl-L-alanine
-
pH 8.0, 30C
8.64
-
N-carbamoyl-L-methionine
-
pH 8.0, 30C
0.08
-
N-carbamoyl-L-ornithine
-
pH 8.0, 30C
5.81
-
N-carbamoyl-L-phenylalanine
-
pH 8.0, 30C
5.84
-
N-carbamoyl-taurine
-
pH 8.0, 30C
-
23.03
-
N-formyl-L-methionine
-
pH 8.0, 30C
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.02
-
N-Acetyl-beta-alanine
-
pH 8.0, 30C
13478
0.3
-
N-acetyl-L-alanine
-
pH 8.0, 30C
13547
0.18
-
N-acetyl-L-methionine
-
pH 8.0, 30C
13566
1.35
-
N-carbamoyl-5-aminopentanoate
-
pH 8.0, 30C
0
2.14
-
N-carbamoyl-alpha-amino-beta-alanine
-
pH 8.0, 30C
0
3.7
-
N-carbamoyl-alpha-methyl-beta-alanine
-
pH 8.0, 30C
0
0.00154
-
N-carbamoyl-alpha-phenyl-beta-alanine
-
pH 8.0, 30C
0
12.01
-
N-Carbamoyl-beta-alanine
-
pH 8.0, 30C
13814
0.06
-
N-carbamoyl-beta-homoalanine
-
pH 8.0, 30C
0
0.01
-
N-carbamoyl-ciliatine
-
pH 8.0, 30C
0
0.00882
-
N-carbamoyl-D-ornithine
-
pH 8.0, 30C
0
4.65
-
N-carbamoyl-GABA
-
pH 8.0, 30C
0
0.28
-
N-carbamoyl-gamma-amino-beta-hydroxybutyric acid
-
pH 8.0, 30C
0
4.61
-
N-Carbamoyl-glycine
-
pH 8.0, 30C
13819
0.65
-
N-carbamoyl-homoisoserine
-
pH 8.0, 30C
0
24.12
-
N-carbamoyl-L-alanine
-
pH 8.0, 30C
86369
78.55
-
N-carbamoyl-L-methionine
-
pH 8.0, 30C
86374
0.0017
-
N-carbamoyl-L-ornithine
-
pH 8.0, 30C
244864
6.53
-
N-carbamoyl-L-phenylalanine
-
pH 8.0, 30C
86375
0.55
-
N-carbamoyl-taurine
-
pH 8.0, 30C
0
3.83
-
N-formyl-L-methionine
-
pH 8.0, 30C
13888
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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
-
Propionate
-
-
0.24
-
Propionate
-
-
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.115
-
(R)-2-phenylpropionic acid
-
IC50: 0.115 mM
0.0005
-
(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
-
0.006
-
(RS)-2-benzylpropionic acid
-
IC50: 0.006 mM
-
0.0057
-
(S)-2-phenylpropionic acid
-
IC50: 0.0057 mM
0.0056
-
3-Phenylpropionic acid
-
IC50: 0.0056 mM
0.008
-
cyclopropanecarboxylic acid
-
IC50: 0.008 mM
0.018
-
isobutyric acid
-
IC50: 0.018 mM
0.055
-
n-butyric acid
-
IC50: 0.055 mM
0.025
-
Propionic acid
-
IC50: 0.025 mM
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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
0.03
-
-
recombinant beta-UP
0.041
-
-
nitrogen source 1 mM NH4Cl
0.048
-
-
nitrogen source 3 mM uracil
0.084
-
Pigeon
-
-
0.88
-
-
N-carbamoyl-beta-alanine as substrate
1.1
-
-, Q19437
pH 7.5, 30C
1.59
-
-
-
1.84
-
-
purified enzyme at pH 7, 38C
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
7.2
-
broad optimum at mildly acidic pH values
6.8
-
-
N-carbamoyl-beta-aminoisobutyric acid as substrate
7
7.5
-
-
7
8
-, Q19437
broad optimum
7
-
-
carbamoyl-beta-alanine as substrate
7.4
7.8
Clostridium uracilicum
-
-
7.4
-
-
-
7.5
8
Clostridium uracilicum
-
-
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.3
8.3
-
-
6
10.5
Clostridium uracilicum
-
-
additional information
-
-
activity declines at more alkaline pH values
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
-
-
assay at
30
35
Clostridium uracilicum
-
-
40
-
-, Q19437
unstable, 65 s half-life
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
20
50
Clostridium uracilicum
-
-
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
-
-
recombinant beta-UP, isoelectric focusing
7.1
-
-
recombinant beta-UP, sequence calculation
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
recombinant beta-UP expressed in Escherichia coli BL21
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
43160
-
Q9UBR1
amino acid sequence calculation
44040
-
-
amino acid sequence calculation
90000
-
-
gel filtration at pH 5.6, in the absence of glycerol
90000
-
-
gel filtration
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
-
-, Q19437
gel filtration, blue native PAGE
1500000
2000000
-
gel filtration
additional information
-
-
native oligomerization state: 1.5 - 2 MDa
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
decamer
-
10 * 43000, recombinant beta-UP, at pH 7, SDS-PAGE, 10 * 43723, recombinant beta-UP, at pH 7, mass spectrometry, 10 * 43733, sequence calculation
decamer
-
-
dimer
-
2 * 45000, SDS-PAGE
dimer
-
in solution
dimer
-
recombinant beta-UP is dimeric at pH 5.6, in the absence of glycerol
dimer
-
2 * 45000 Da
dodecamer
-
12 * 42000, active dodecamer in the presence of substrate, SDS-PAGE
dodecamer
-, Q19437
12 * 43200
hexamer
-
6 * 54000, hexamer is composed of 3 dimers of 115000, SDS-PAGE
hexamer
-
6 * 42000, 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
homodecamer
-
10 * 45500
homodecamer
-
10 * 44000
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
homodimer
-
-
homodimer
-
2 * 50000
homodimer
-
2 * 45000, SDS-PAGE
homohexamer
-
6 * 40000 Da
polymer
-
1500000-2000000, no subunit molecular weight reported
trimer
-
3 * 42000, inactive trimer in the presence of the product, SDS-PAGE
homohexamer
-
6 * 42000 Da
additional information
-
subunit: 44000 Da
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.1
10.7
-
-
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
45
-
Clostridium uracilicum
-
rapid inactivation above
45
-
-
after 60 min 20% activity
65
-
-
80% activity lost at 70C
additional information
-
-
heating destabilizes
additional information
-
-
Tm = 326.23 K, unfolding temperature of wild type holoenzyme (determination by circular dichroism)
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
dithiothreitol and glycerol stabilize
-
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
-
stored in 50% glycerol without gross denaturation
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
4C, buffer without stabilizing detergents and reducing thiols, 26 days, almost complete loss of activity
-
-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
-
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
-
-70C, partially purified beta-UP, in presence of 10% w/v glycerol, several months, stable
-
4C, partially purified beta-UP, in presence of Mg2+ and dithiothreitol, 7 days, about 10% loss of activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
immobilized metal ion affinity chromatography, gel filtration
-
recombinant beta-UP
-
immobilized metal ion affinity chromatography (Ni2+)
-, Q19437
partially
Clostridium uracilicum
-
partially
-
recombinant betaAS
-
recombinant SkbetaAS
-
partially
-
purified 1000fold
-
partial
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
His-tagged version expressed in Escherichia coli
-
cDNA truncated at the N-terminus by 14 residues, overexpression in Escherichia coli BL21
-
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
Q8H183
hexahistidine fusion protein expressed in Escherichia coli BL21-CodonPlus (DE3)-RIL
-, Q19437
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
Q9UBR1
gene UPB1, genotyping
-
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
-
expression in Escherichia coli B843(DE3)
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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
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
R291Q
-
R291 is the key residue for recognition of the substrate carboxyl group
additional information
Q8H183
construction of a T-DNA knockout mutant of gene PYD3, the mutant exhibits no obvious phenotype under optimal growing conditions, but the pyd3 mutant is unable to catabolize [2-14C]-uracil or to grow on uracil as the sole nitrogen source
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
additional information
-
screening for genetic deficiency in betaUPase, genotyping and phenotypes, overview
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
medicine
-
analysis of putative enzyme defects in patients with neurological disfunctions
medicine
Q9UBR1
mutation analysis in patients with cloned genes