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2-amino-3-ureidopropionic acid + H2O
3-aminoalanine + CO2 + NH3
2-methyl-3-ureidopropionic acid + H2O
3-amino-2-methylpropanoic acid + NH3 + CO2
82% activity in comparison to 3-ureidopropionic acid
-
-
?
2-methyl-3-ureidopropionic acid + H2O
alpha-methyl-beta-alanine + CO2 + NH3
2-methyl-N-carbamoyl-beta-alanine + H2O
2-methyl-beta-alanine + CO2 + NH3
2-phenyl-3-ureidopropionic acid + H2O
3-amino-2-phenylpropanoic acid + CO2 + NH3
2-ureidoethane phosphonic acid + H2O
ciliatine + CO2 + NH3
2-ureidoethanesulfonic acid + H2O
taurine + CO2 + NH3
-
-
-
-
?
3-methyl-3-ureidopropionic acid + H2O
beta-homoalanine + CO2 + NH3
-
-
-
-
?
3-ureidobutyrate + H2O
2-methyl-beta-alanine + CO2 + NH3
-
-
-
?
3-ureidopropanoate + H2O
beta-alanine + CO2 + NH3
3-ureidopropionic acid + H2O
beta-alanine + CO2 + NH3
4-amino-4-oxobutyric acid + H2O
?
3% activity in comparison to 3-ureidopropionic acid
-
-
?
DL-beta-ureidobutyric acid + H2O
?
-
-
-
-
?
gamma-ureido-n-butyric acid + H2O
4-aminobutanoate + CO2 + NH3
-
-
-
-
?
N-acetyl-beta-alanine + H2O
?
-
-
-
-
?
N-acetyl-DL-alanine + H2O
?
-
-
-
-
?
N-acetyl-L-alanine + H2O
?
-
-
-
-
?
N-acetyl-L-methionine + H2O
?
-
-
-
-
?
N-carbamoyl-5-aminopentanoate + H2O
5-aminopentanoate + CO2 + NH3
-
-
-
-
?
N-carbamoyl-alpha-amino-beta-alanine + H2O
2,3-diaminopropanoate + CO2 + NH3
-
-
-
-
?
N-carbamoyl-alpha-methyl-beta-alanine + H2O
3-amino-2-methylpropanoic acid + CO2 + NH3
-
-
-
-
?
N-carbamoyl-alpha-phenyl-beta-alanine + H2O
3-amino-2-phenylpropanoic acid + CO2 + NH3
-
-
-
-
?
N-carbamoyl-beta-alanine + H2O
?
N-carbamoyl-beta-alanine + H2O
beta-alanine + CO2 + NH3
N-carbamoyl-beta-alanine + H2O
beta-alanine + NH3 + CO2
-
-
-
-
?
N-carbamoyl-beta-aminoisobutyrate + H2O
beta-aminoisobutyrate + CO2 + NH3
N-carbamoyl-beta-aminoisobutyric acid + H2O
beta-aminoisobutyric acid + NH3 + CO2
-
-
-
-
?
N-carbamoyl-beta-homoalanine + H2O
beta-homoalanine + CO2 + NH3
-
-
-
-
?
N-carbamoyl-ciliatine + H2O
ciliatine + CO2 + NH3
-
-
-
-
?
N-carbamoyl-D-ornithine + H2O
D-ornithine + CO2 + NH3
-
-
-
-
?
N-carbamoyl-DL-2-aminovaleric acid + H2O
2-aminopentanoate + CO2 + NH3
-
-
-
-
?
N-carbamoyl-DL-alanine + H2O
DL-alanine + CO2 + NH3
-
poor substrate, relative enzyme activity 4%
-
-
?
N-carbamoyl-DL-beta-aminoisobutyrate + H2O
DL-beta-aminoisobutyrate + CO2 + NH3
N-carbamoyl-GABA + H2O
4-aminobutanoic acid + CO2 + NH3
-
-
-
-
?
N-carbamoyl-gamma-amino-beta-hydroxybutyric acid + H2O
?
-
-
-
-
?
N-carbamoyl-glycine + H2O
glycine + CO2 + NH3
N-carbamoyl-homoisoserine + H2O
homoisoserine + CO2 + NH3
-
-
-
-
?
N-carbamoyl-L-alanine + H2O
L-alanine + CO2 + NH3
N-carbamoyl-L-methionine + H2O
L-methionine + CO2 + NH3
N-carbamoyl-L-ornithine + H2O
L-ornithine + CO2 + NH3
-
-
-
-
?
N-carbamoyl-L-phenylalanine + H2O
L-phenylalanine + CO2 + NH3
N-carbamoyl-L-serine + H2O
L-serine + CO2 + NH3
-
-
-
-
?
N-carbamoyl-taurine + H2O
taurine + CO2 + NH3
-
-
-
-
?
N-carbamoylglycine + H2O
glycine + CO2 + NH3
N-carbamyl-beta-alanine + H2O
beta-alanine + CO2 + NH3
-
-
-
-
?
N-carbamyl-beta-aminoisobutyrate + H2O
beta-aminoisobutyrate + CO2 + NH3
-
-
-
-
?
N-formyl-DL-alanine + H2O
?
-
-
-
-
?
N-formyl-L-methionine + H2O
?
-
-
-
-
?
additional information
?
-
2-amino-3-ureidopropionic acid + H2O
3-aminoalanine + CO2 + NH3
-
-
-
-
?
2-amino-3-ureidopropionic acid + H2O
3-aminoalanine + CO2 + NH3
-
-
-
-
?
2-methyl-3-ureidopropionic acid + H2O
alpha-methyl-beta-alanine + CO2 + NH3
-
-
-
-
?
2-methyl-3-ureidopropionic acid + H2O
alpha-methyl-beta-alanine + CO2 + NH3
-
-
-
-
?
2-methyl-N-carbamoyl-beta-alanine + H2O
2-methyl-beta-alanine + CO2 + NH3
-
-
-
-
?
2-methyl-N-carbamoyl-beta-alanine + H2O
2-methyl-beta-alanine + CO2 + NH3
-
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
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
catalytic mechanism, substrate-binding residues
-
-
?
2-methyl-N-carbamoyl-beta-alanine + H2O
2-methyl-beta-alanine + CO2 + NH3
-
-
-
-
?
2-methyl-N-carbamoyl-beta-alanine + H2O
2-methyl-beta-alanine + CO2 + NH3
-
completes the catabolism of the pyrimidine bases uracil and thymine
-
-
?
2-methyl-N-carbamoyl-beta-alanine + H2O
2-methyl-beta-alanine + CO2 + NH3
-
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
-
only one enantiomer of the racemic substrate is hydrolyzed
-
-
?
2-phenyl-3-ureidopropionic acid + H2O
3-amino-2-phenylpropanoic acid + CO2 + NH3
-
-
-
-
?
2-phenyl-3-ureidopropionic acid + H2O
3-amino-2-phenylpropanoic acid + CO2 + NH3
-
-
-
-
?
2-ureidoethane phosphonic acid + H2O
ciliatine + CO2 + NH3
-
-
-
-
?
2-ureidoethane phosphonic acid + H2O
ciliatine + CO2 + NH3
-
-
-
-
?
3-ureidopropanoate + H2O
beta-alanine + CO2 + NH3
-
-
-
?
3-ureidopropanoate + H2O
beta-alanine + CO2 + NH3
3-ureidopropanoate i.e. N-carbamoyl-beta-alanine
-
-
?
3-ureidopropionic acid + H2O
beta-alanine + CO2 + NH3
-
-
-
-
?
3-ureidopropionic acid + H2O
beta-alanine + CO2 + NH3
-
-
-
?
N-carbamoyl-beta-alanine + H2O
?
-
-
-
-
?
N-carbamoyl-beta-alanine + H2O
?
-
-
-
-
?
N-carbamoyl-beta-alanine + H2O
?
-
-
-
-
?
N-carbamoyl-beta-alanine + H2O
?
Blastobacter sp.
-
-
-
-
?
N-carbamoyl-beta-alanine + H2O
?
-
-
-
-
?
N-carbamoyl-beta-alanine + H2O
?
-
-
-
-
?
N-carbamoyl-beta-alanine + H2O
?
-
-
-
-
?
N-carbamoyl-beta-alanine + H2O
?
Clostridium uracilicum
-
-
-
-
?
N-carbamoyl-beta-alanine + H2O
?
Clostridium uracilicum M5-2
-
-
-
-
?
N-carbamoyl-beta-alanine + H2O
?
-
-
-
-
?
N-carbamoyl-beta-alanine + H2O
?
-
-
-
-
?
N-carbamoyl-beta-alanine + H2O
?
-
-
-
-
?
N-carbamoyl-beta-alanine + H2O
?
-
-
-
-
?
N-carbamoyl-beta-alanine + H2O
?
-
-
-
-
?
N-carbamoyl-beta-alanine + H2O
?
-
-
-
?
N-carbamoyl-beta-alanine + H2O
?
-
-
-
-
?
N-carbamoyl-beta-alanine + H2O
?
-
-
-
-
?
N-carbamoyl-beta-alanine + H2O
?
Pigeon
-
-
-
-
?
N-carbamoyl-beta-alanine + H2O
?
-
-
-
-
?
N-carbamoyl-beta-alanine + H2O
?
-
-
172056, 172057, 172058, 172059, 172060, 172061, 172062, 172063, 172064, 172065, 172066, 172068, 172069 -
-
?
N-carbamoyl-beta-alanine + H2O
?
-
-
-
-
?
N-carbamoyl-beta-alanine + H2O
?
-
-
-
-
?
N-carbamoyl-beta-alanine + H2O
beta-alanine + CO2 + NH3
-
L enantiomer specific hydrolysis
-
-
ir
N-carbamoyl-beta-alanine + H2O
beta-alanine + CO2 + NH3
-
-
-
-
?
N-carbamoyl-beta-alanine + H2O
beta-alanine + CO2 + NH3
-
-
-
-
?
N-carbamoyl-beta-alanine + H2O
beta-alanine + CO2 + NH3
-
-
-
-
?
N-carbamoyl-beta-alanine + H2O
beta-alanine + CO2 + NH3
-
final enzyme of the catabolic pathway of pyrimidine bases, substrate derives from uracil
-
-
?
N-carbamoyl-beta-alanine + H2O
beta-alanine + CO2 + NH3
-
-
-
-
?
N-carbamoyl-beta-alanine + H2O
beta-alanine + CO2 + NH3
-
-
-
?
N-carbamoyl-beta-alanine + H2O
beta-alanine + CO2 + NH3
-
L enantiomer specific hydrolysis
-
-
ir
N-carbamoyl-beta-alanine + H2O
beta-alanine + CO2 + NH3
-
L enantiomer specific hydrolysis
-
-
ir
N-carbamoyl-beta-alanine + H2O
beta-alanine + CO2 + NH3
Blastobacter sp.
-
N-carbamoyl-D-amino acid hydrolyzing activity
-
-
ir
N-carbamoyl-beta-alanine + H2O
beta-alanine + CO2 + NH3
-
-
-
-
?
N-carbamoyl-beta-alanine + H2O
beta-alanine + CO2 + NH3
-
L enantiomer specific hydrolysis
-
-
ir
N-carbamoyl-beta-alanine + H2O
beta-alanine + CO2 + NH3
-
L enantiomer specific hydrolysis
-
-
ir
N-carbamoyl-beta-alanine + H2O
beta-alanine + CO2 + NH3
-
L enantiomer specific hydrolysis
-
-
ir
N-carbamoyl-beta-alanine + H2O
beta-alanine + CO2 + NH3
Clostridium uracilicum
-
L enantiomer specific hydrolysis
-
-
ir
N-carbamoyl-beta-alanine + H2O
beta-alanine + CO2 + NH3
Clostridium uracilicum M5-2
-
L enantiomer specific hydrolysis
-
-
ir
N-carbamoyl-beta-alanine + H2O
beta-alanine + CO2 + NH3
-
-
-
-
ir
N-carbamoyl-beta-alanine + H2O
beta-alanine + CO2 + NH3
-
N-carbamoyl-D-amino acid hydrolyzing activity
-
-
ir
N-carbamoyl-beta-alanine + H2O
beta-alanine + CO2 + NH3
-
N-carbamoyl-D-amino acid hydrolyzing activity
-
-
ir
N-carbamoyl-beta-alanine + H2O
beta-alanine + CO2 + NH3
-
-
-
-
?
N-carbamoyl-beta-alanine + H2O
beta-alanine + CO2 + NH3
-
-
-
-
?
N-carbamoyl-beta-alanine + H2O
beta-alanine + CO2 + NH3
-
L enantiomer specific hydrolysis
-
-
ir
N-carbamoyl-beta-alanine + H2O
beta-alanine + CO2 + NH3
-
-
-
-
?
N-carbamoyl-beta-alanine + H2O
beta-alanine + CO2 + NH3
-
L enantiomer specific hydrolysis
-
-
ir
N-carbamoyl-beta-alanine + H2O
beta-alanine + CO2 + NH3
-
-
-
-
?
N-carbamoyl-beta-alanine + H2O
beta-alanine + CO2 + NH3
-
-
-
-
ir
N-carbamoyl-beta-alanine + H2O
beta-alanine + CO2 + NH3
-
L enantiomer specific hydrolysis
-
-
ir
N-carbamoyl-beta-alanine + H2O
beta-alanine + CO2 + NH3
-
-
-
-
?
N-carbamoyl-beta-alanine + H2O
beta-alanine + CO2 + NH3
-
-
-
?
N-carbamoyl-beta-alanine + H2O
beta-alanine + CO2 + NH3
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
catalytic mechanism, substrate-binding residues
-
-
?
N-carbamoyl-beta-alanine + H2O
beta-alanine + CO2 + NH3
-
L enantiomer specific hydrolysis
-
-
ir
N-carbamoyl-beta-alanine + H2O
beta-alanine + CO2 + NH3
-
L enantiomer specific hydrolysis
-
-
ir
N-carbamoyl-beta-alanine + H2O
beta-alanine + CO2 + NH3
Pigeon
-
L enantiomer specific hydrolysis
-
-
ir
N-carbamoyl-beta-alanine + H2O
beta-alanine + CO2 + NH3
-
-
-
-
?
N-carbamoyl-beta-alanine + H2O
beta-alanine + CO2 + NH3
-
L enantiomer specific hydrolysis
-
-
ir
N-carbamoyl-beta-alanine + H2O
beta-alanine + CO2 + NH3
-
-
-
-
?
N-carbamoyl-beta-alanine + H2O
beta-alanine + CO2 + NH3
-
completes the catabolism of the pyrimidine bases uracil and thymine
-
-
?
N-carbamoyl-beta-alanine + H2O
beta-alanine + CO2 + NH3
-
-
-
-
ir
N-carbamoyl-beta-alanine + H2O
beta-alanine + CO2 + NH3
-
L enantiomer specific hydrolysis
172056, 172057, 172058, 172059, 172060, 172061, 172062, 172063, 172064, 172065, 172066 -
-
ir
N-carbamoyl-beta-alanine + H2O
beta-alanine + CO2 + NH3
-
L enantiomer specific hydrolysis
-
-
ir
N-carbamoyl-beta-alanine + H2O
beta-alanine + CO2 + NH3
-
L enantiomer specific hydrolysis
-
-
ir
N-carbamoyl-beta-alanine + H2O
beta-alanine + CO2 + NH3
-
-
-
-
?
N-carbamoyl-beta-alanine + H2O
beta-alanine + CO2 + NH3
-
final enzyme of the catabolic pathway of pyrimidine bases, substrate derives from uracil
-
-
?
N-carbamoyl-beta-aminoisobutyrate + H2O
beta-aminoisobutyrate + CO2 + NH3
-
-
-
-
?
N-carbamoyl-beta-aminoisobutyrate + H2O
beta-aminoisobutyrate + CO2 + NH3
-
-
-
-
?
N-carbamoyl-beta-aminoisobutyrate + H2O
beta-aminoisobutyrate + CO2 + NH3
-
-
-
-
?
N-carbamoyl-beta-aminoisobutyrate + H2O
beta-aminoisobutyrate + CO2 + NH3
-
-
-
-
?
N-carbamoyl-beta-aminoisobutyrate + H2O
beta-aminoisobutyrate + CO2 + NH3
-
-
-
-
?
N-carbamoyl-beta-aminoisobutyrate + H2O
beta-aminoisobutyrate + CO2 + NH3
-
-
-
-
?
N-carbamoyl-beta-aminoisobutyrate + H2O
beta-aminoisobutyrate + CO2 + NH3
-
-
-
-
?
N-carbamoyl-beta-aminoisobutyrate + H2O
beta-aminoisobutyrate + CO2 + NH3
-
-
-
-
?
N-carbamoyl-beta-aminoisobutyrate + H2O
beta-aminoisobutyrate + CO2 + NH3
-
-
-
-
?
N-carbamoyl-beta-aminoisobutyrate + H2O
beta-aminoisobutyrate + CO2 + NH3
-
-
-
-
?
N-carbamoyl-DL-beta-aminoisobutyrate + H2O
DL-beta-aminoisobutyrate + CO2 + NH3
Blastobacter sp.
-
-
-
-
?
N-carbamoyl-DL-beta-aminoisobutyrate + H2O
DL-beta-aminoisobutyrate + CO2 + NH3
-
-
-
-
?
N-carbamoyl-DL-beta-aminoisobutyrate + H2O
DL-beta-aminoisobutyrate + CO2 + NH3
-
-
-
-
?
N-carbamoyl-DL-beta-aminoisobutyrate + H2O
DL-beta-aminoisobutyrate + CO2 + NH3
-
-
-
-
?
N-carbamoyl-DL-beta-aminoisobutyrate + H2O
DL-beta-aminoisobutyrate + CO2 + NH3
-
-
-
-
?
N-carbamoyl-DL-beta-aminoisobutyrate + H2O
DL-beta-aminoisobutyrate + CO2 + NH3
Pigeon
-
-
-
-
?
N-carbamoyl-DL-beta-aminoisobutyrate + H2O
DL-beta-aminoisobutyrate + CO2 + NH3
-
-
-
-
?
N-carbamoyl-DL-beta-aminoisobutyrate + H2O
DL-beta-aminoisobutyrate + CO2 + NH3
-
-
-
-
?
N-carbamoyl-glycine + H2O
glycine + CO2 + NH3
-
-
-
-
?
N-carbamoyl-glycine + H2O
glycine + CO2 + NH3
-
-
-
-
?
N-carbamoyl-L-alanine + H2O
L-alanine + CO2 + NH3
-
-
-
-
?
N-carbamoyl-L-alanine + H2O
L-alanine + CO2 + NH3
-
-
-
-
?
N-carbamoyl-L-methionine + H2O
L-methionine + CO2 + NH3
-
-
-
-
?
N-carbamoyl-L-methionine + H2O
L-methionine + CO2 + NH3
-
-
-
-
?
N-carbamoyl-L-phenylalanine + H2O
L-phenylalanine + CO2 + NH3
-
-
-
-
?
N-carbamoyl-L-phenylalanine + H2O
L-phenylalanine + CO2 + NH3
-
-
-
-
?
N-carbamoylglycine + H2O
glycine + CO2 + NH3
-
-
-
-
?
N-carbamoylglycine + H2O
glycine + CO2 + NH3
-
-
-
-
?
N-carbamoylglycine + H2O
glycine + CO2 + NH3
-
poor substrate, relative enzyme activity 1%
-
-
?
additional information
?
-
-
the enzyme is involved in the pyrimidine catabolism
-
-
?
additional information
?
-
-
betaAS catalyzes the terminal reaction of the reductive pyrimidine catabolic pathway
-
-
?
additional information
?
-
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
?
-
-
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2-methyl-N-carbamoyl-beta-alanine + H2O
2-methyl-beta-alanine + CO2 + NH3
3-ureidobutyrate + H2O
2-methyl-beta-alanine + CO2 + NH3
-
-
-
?
3-ureidopropanoate + H2O
beta-alanine + CO2 + NH3
-
-
-
?
N-carbamoyl-beta-alanine + H2O
?
N-carbamoyl-beta-alanine + H2O
beta-alanine + CO2 + NH3
additional information
?
-
2-methyl-N-carbamoyl-beta-alanine + H2O
2-methyl-beta-alanine + CO2 + NH3
-
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
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
-
completes the catabolism of the pyrimidine bases uracil and thymine
-
-
?
2-methyl-N-carbamoyl-beta-alanine + H2O
2-methyl-beta-alanine + CO2 + NH3
-
final enzyme of the catabolic pathway of pyrimidine bases, substrate derives from thymine
-
-
?
N-carbamoyl-beta-alanine + H2O
?
-
-
-
-
?
N-carbamoyl-beta-alanine + H2O
?
-
-
-
-
?
N-carbamoyl-beta-alanine + H2O
?
-
-
-
-
?
N-carbamoyl-beta-alanine + H2O
?
Blastobacter sp.
-
-
-
-
?
N-carbamoyl-beta-alanine + H2O
?
-
-
-
-
?
N-carbamoyl-beta-alanine + H2O
?
-
-
-
-
?
N-carbamoyl-beta-alanine + H2O
?
-
-
-
-
?
N-carbamoyl-beta-alanine + H2O
?
Clostridium uracilicum
-
-
-
-
?
N-carbamoyl-beta-alanine + H2O
?
Clostridium uracilicum M5-2
-
-
-
-
?
N-carbamoyl-beta-alanine + H2O
?
-
-
-
-
?
N-carbamoyl-beta-alanine + H2O
?
-
-
-
-
?
N-carbamoyl-beta-alanine + H2O
?
-
-
-
-
?
N-carbamoyl-beta-alanine + H2O
?
-
-
-
-
?
N-carbamoyl-beta-alanine + H2O
?
-
-
-
-
?
N-carbamoyl-beta-alanine + H2O
?
-
-
-
?
N-carbamoyl-beta-alanine + H2O
?
-
-
-
-
?
N-carbamoyl-beta-alanine + H2O
?
-
-
-
-
?
N-carbamoyl-beta-alanine + H2O
?
Pigeon
-
-
-
-
?
N-carbamoyl-beta-alanine + H2O
?
-
-
-
-
?
N-carbamoyl-beta-alanine + H2O
?
-
-
172056, 172057, 172058, 172059, 172060, 172061, 172062, 172063, 172064, 172065, 172066, 172068, 172069 -
-
?
N-carbamoyl-beta-alanine + H2O
?
-
-
-
-
?
N-carbamoyl-beta-alanine + H2O
?
-
-
-
-
?
N-carbamoyl-beta-alanine + H2O
beta-alanine + CO2 + NH3
-
final enzyme of the catabolic pathway of pyrimidine bases, substrate derives from uracil
-
-
?
N-carbamoyl-beta-alanine + H2O
beta-alanine + CO2 + NH3
-
-
-
?
N-carbamoyl-beta-alanine + H2O
beta-alanine + CO2 + NH3
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
-
completes the catabolism of the pyrimidine bases uracil and thymine
-
-
?
N-carbamoyl-beta-alanine + H2O
beta-alanine + CO2 + NH3
-
final enzyme of the catabolic pathway of pyrimidine bases, substrate derives from uracil
-
-
?
additional information
?
-
-
the enzyme is involved in the pyrimidine catabolism
-
-
?
additional information
?
-
-
betaAS catalyzes the terminal reaction of the reductive pyrimidine catabolic pathway
-
-
?
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beta-ureidopropionase deficiency
3-Ureidopropionate contributes to the neuropathology of 3-ureidopropionase deficiency and severe propionic aciduria: a hypothesis.
beta-ureidopropionase deficiency
Beta-ureidopropionase deficiency presenting with congenital anomalies of the urogenital and colorectal systems.
beta-ureidopropionase deficiency
beta-Ureidopropionase Deficiency Presenting with Febrile Status Epilepticus.
beta-ureidopropionase deficiency
beta-Ureidopropionase deficiency: a novel inborn error of metabolism discovered using NMR spectroscopy on urine.
beta-ureidopropionase deficiency
beta-Ureidopropionase deficiency: an inborn error of pyrimidine degradation associated with neurological abnormalities.
beta-ureidopropionase deficiency
Clinical Findings and a Therapeutic Trial in the First Patient with beta-Ureidopropionase Deficiency.
beta-ureidopropionase deficiency
Confirmation of the enzyme defect in the first case of beta-ureidopropionase deficiency. Beta-alanine deficiency.
beta-ureidopropionase deficiency
Detection of beta-ureidopropionase deficiency with HPLC-electrospray tandem mass spectrometry and confirmation of the defect at the enzyme level.
beta-ureidopropionase deficiency
Diagnosis and monitoring of inborn errors of metabolism using urease-pretreatment of urine, isotope dilution, and gas chromatography-mass spectrometry.
beta-ureidopropionase deficiency
Five cases of beta-ureidopropionase deficiency detected by GC/MS analysis of urine metabolome.
beta-ureidopropionase deficiency
Genetic analysis of the first 4 patients with beta-ureidopropionase deficiency.
beta-ureidopropionase deficiency
NMR-based urinalysis for rapid diagnosis of ?-ureidopropionase deficiency in a patient with Dravet syndrome.
beta-ureidopropionase deficiency
Noninvasive human metabolome analysis for differential diagnosis of inborn errors of metabolism.
beta-ureidopropionase deficiency
Screening and diagnosis of beta-ureidopropionase deficiency by gas chromatographic/mass spectrometric analysis of urine.
carbamoyl-phosphate synthase (ammonia) deficiency
Noninvasive human metabolome analysis for differential diagnosis of inborn errors of metabolism.
Hyperthyroidism
CTF1/NF1 binding site is important in beta myosin heavy chain antisense promoter regulation.
Muscle Hypotonia
Screening and diagnosis of beta-ureidopropionase deficiency by gas chromatographic/mass spectrometric analysis of urine.
Neuroblastoma
Diagnosis and monitoring of inborn errors of metabolism using urease-pretreatment of urine, isotope dilution, and gas chromatography-mass spectrometry.
ornithine carbamoyltransferase deficiency
Noninvasive human metabolome analysis for differential diagnosis of inborn errors of metabolism.
Ornithine Carbamoyltransferase Deficiency Disease
Noninvasive human metabolome analysis for differential diagnosis of inborn errors of metabolism.
Phenylketonurias
Noninvasive human metabolome analysis for differential diagnosis of inborn errors of metabolism.
Propionic Acidemia
3-Ureidopropionate contributes to the neuropathology of 3-ureidopropionase deficiency and severe propionic aciduria: a hypothesis.
Propionic Acidemia
Diagnosis and monitoring of inborn errors of metabolism using urease-pretreatment of urine, isotope dilution, and gas chromatography-mass spectrometry.
Protein Deficiency
Effect of dietary protein on pyrimidine-metabolizing enzymes in rats.
Status Epilepticus
beta-Ureidopropionase Deficiency Presenting with Febrile Status Epilepticus.
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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
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
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
E159A
0.09% of the wild-type activity
E159D
0.09% of the wild-type 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
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
L13S
inactive mutant enzyme, the mutation is identified in beta-ureidopropionase-deficient patients
R326Q
naturally occuring mutation and site-directed mutagenesis, the mutation results in folding defects and oligomer assembly impairment, inactive mutant
R326Q
naturally occuring mutation causing enzyme deficiency, phenotype
R326Q
naturally occuring mutation in exon 9 affecting pre-mRNA splicing, analysis using a minigel approach
T359M
inactive mutant 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
additional information
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
additional information
-
screening for genetic deficiency in betaUPase, genotyping and phenotypes, overview
additional information
missense mutations and intronic mutations that lead to aberrant splicing, overview
additional information
disruption of dimer-dimer interfaces by site-directed mutagenesis generated dimeric, inactive enzyme variants
additional information
-
transgenic overexpression of SlUPB1 in tomato, upregulation of gene SlUPB1 in heat-sensitive variant L4783 and downregulation of gene SlUPB1 in heat-tolerant variant CL5915. Pollen germination rates of transgenics overexpressing SlUPB1 are higher than germination rates of the background tomato L4783. Germination rates of transgenics downregulating SlUPB1 are significantly lower than germination rates of background tomato CL5915
additional information
-
transgenic overexpression of SlUPB1 in tomato, upregulatiopn of gene SlUPB1 in heat-sensitive variant L4783 and downregulation of gene SlUPB1 in heat-tolerant variant CL5915. Pollen germination rates of transgenics overexpressing SlUPB1 are higher than germination rates of the background tomato L4783. Germination rates of transgenics downregulating SlUPB1 are significantly lower than germination rates of background tomato CL5915
additional information
-
transgenic overexpression of SlUPB1 in tomato, upregulation of gene SlUPB1 in heat-sensitive variant L4783 and downregulation of gene SlUPB1 in heat-tolerant variant CL5915. Pollen germination rates of transgenics overexpressing SlUPB1 are higher than germination rates of the background tomato L4783. Germination rates of transgenics downregulating SlUPB1 are significantly lower than germination rates of background tomato CL5915
-
additional information
-
transgenic overexpression of SlUPB1 in tomato, upregulatiopn of gene SlUPB1 in heat-sensitive variant L4783 and downregulation of gene SlUPB1 in heat-tolerant variant CL5915. Pollen germination rates of transgenics overexpressing SlUPB1 are higher than germination rates of the background tomato L4783. Germination rates of transgenics downregulating SlUPB1 are significantly lower than germination rates of background tomato CL5915
-
additional information
-
transgenic overexpression of SlUPB1 in tomato, upregulation of gene SlUPB1 in heat-sensitive variant L4783 and downregulation of gene SlUPB1 in heat-tolerant variant CL5915. Pollen germination rates of transgenics overexpressing SlUPB1 are higher than germination rates of the background tomato L4783. Germination rates of transgenics downregulating SlUPB1 are significantly lower than germination rates of background tomato CL5915
-
additional information
-
transgenic overexpression of SlUPB1 in tomato, upregulatiopn of gene SlUPB1 in heat-sensitive variant L4783 and downregulation of gene SlUPB1 in heat-tolerant variant CL5915. Pollen germination rates of transgenics overexpressing SlUPB1 are higher than germination rates of the background tomato L4783. Germination rates of transgenics downregulating SlUPB1 are significantly lower than germination rates of background tomato CL5915
-
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Tamaki, N.; Mizutani, N.; Kikugawa, M.; Fujimoto, S.; Mizota, C.
Purification and properties of beta-ureidopropionase from the rat liver
Eur. J. Biochem.
169
21-26
1987
Rattus rattus
brenda
Matthews, M.M.; Traut, T.W.
Regulation of N-carbamoyl-beta-alanine amidohydrolase, the terminal enzyme in pyrimidine catabolism, by ligand-induced change in polymerization
J. Biol. Chem.
262
7232-7237
1987
Clostridium uracilicum, Euglena gracilis, Homo sapiens, Mus musculus, Rattus rattus, Clostridium uracilicum M5-2
brenda
Traut, T.W.; Loechel, S.
Pyrimidine catabolism: individual characterization of the three sequential enzymes with a new assay
Biochemistry
23
2533-2539
1984
Escherichia coli, Euglena gracilis, Mus musculus, Rattus rattus
brenda
Hardiman, M.K.; Alfant, M.; Wakelin, V.P.; Tremblay, G.C.
Capacity of rat liver for pyrimidine synthesis and catabolism during fetal and neonatal development
Arch. Biochem. Biophys.
224
326-331
1983
Rattus rattus, Rattus rattus Cd
brenda
Kaspari, H.
Repression of beta-ureidopropionase by ammonia in Rhodopseudomonas capsulata
J. Gen. Microbiol.
122
95-100
1981
Clostridium uracilicum, Euglena gracilis, Rattus rattus, Rhodobacter capsulatus, Clostridium uracilicum M5-2
-
brenda
Wasternack, C.; Lippmann, G.; Reinbotte, H.
Pyrimidine-degrading enzymes purification and properties of beta-ureidopropionase of Euglena gracilis
Biochim. Biophys. Acta
570
341-351
1979
Clostridium uracilicum, Euglena gracilis, Mus musculus, Rattus rattus, Clostridium uracilicum M5-2
brenda
Campbell, L.L.
Reductive degradation of pyrimidines. V. Enzymatic conversion of N-carbamyl-beta-alanine to beta-alanine, carbon dioxide and ammonia
J. Biol. Chem.
235
2375-2379
1960
Canis lupus familiaris, Clostridium uracilicum, Oryctolagus cuniculus, Pigeon, Rattus rattus, Clostridium uracilicum M5-2
brenda
Caravaca, J.; Grisolia, S.
Enzymatic decarbamylation of carbamyl beta-alanine and carbamyl beta-aminoisobutyric acid
J. Biol. Chem.
231
357-365
1958
Canis lupus familiaris, Oryctolagus cuniculus, Pigeon, Rattus rattus
brenda
Waldmann, G.; Podschun, B.
Assay for beta-ureidopropionase by high-performance liquid chromatography
Anal. Biochem.
188
233-236
1990
Bos taurus, Clostridium uracilicum, Euglena gracilis, Mus musculus, Rattus rattus
brenda
Ogawa, J.; Shimizu, S.
beta-Ureidopropionase with N-carbamoyl-alpha-L-amino acid amidohydrolase activity from an aerobic bacterium, Pseudomonas putida IFO 12996
Eur. J. Biochem.
223
625-630
1994
Clostridium uracilicum, Comamonas sp., Euglena gracilis, Mus musculus, Pseudomonas putida, Rattus rattus
brenda
Ogawa, J.; Kaimura, T.; Yamada, H.; Shimizu, S.
Evaluation of pyrimidine- and hydantoin-degrading enzyme activities in aerobic bacteria
FEMS Microbiol. Lett.
122
55-60
1994
Agrobacterium sp., Arthrobacter sp., Bacillus sp. (in: Bacteria), Blastobacter sp., Comamonas sp., Pseudomonas putida, Comamonas sp. E222c
-
brenda
West, T.P.
Reductive catabolism of uracil and thymine by Burkholderia cepacia
Arch. Microbiol.
168
237-239
1997
Burkholderia cepacia
-
brenda
Van Kuilenburg, A.B.P.; Van Lenthe, H.; Van Gennip, A.H.
A radiochemical assay for beta-ureidopropionase using radiolabeled N-carbamyl-beta-alanine obtained via hydrolysis of [2-14C]5,6-dihydrouracil
Anal. Biochem.
272
250-253
1999
Homo sapiens, Rattus rattus
brenda
Vreken, P.; van Kuilenburg, A.B.P.; Hamajima, N.; Meinsma, R.; van Lenthe, H.; Goehlich-Ratmann, G.; Assmann, B.E.; Wevers, R.A.; van Gennip, A.H.
cDNA cloning, genomic structure and chromosomal localization of the human BUP-1 gene encoding beta-ureidopropionase
Biochim. Biophys. Acta
1447
251-257
1999
Rattus rattus, Homo sapiens (Q9UBR1), Homo sapiens
brenda
Dobritzsch, D.; Gojkovic, Z.; Andersen, B.; Piskur, J.
Crystallization and preliminary X-ray analysis of beta-alanine synthase from the yeast Saccharomyces kluyveri
Acta Crystallogr. Sect. D
59
1267-1269
2003
Lachancea kluyveri
brenda
Lundgren, S.; Gojkovic, Z.; Piskur, J.; Dobritzsch, D.
Yeast beta-alanine synthase shares a structural scaffold and origin with dizinc-dependent exopeptidases
J. Biol. Chem.
278
51851-51862
2003
Lachancea kluyveri (Q96W94), Lachancea kluyveri
brenda
Traut, T.W.
beta-Alanine synthase, an enzyme involved in catabolism of uracil and thymine
Methods Enzymol.
324
399-410
2000
Rattus norvegicus
brenda
Walsh, T.A.; Green, S.B.; Larrinua, I.M.; Schmitzer, P.R.
Characterization of plant beta-ureidopropionase and functional overexpression in Escherichia coli
Plant Physiol.
125
1001-1011
2001
Arabidopsis sp., Zea mays
brenda
Rawls, J.M.
Analysis of pyrimidine catabolism in Drosophila melanogaster using epistatic interactions with mutations of pyrimidine biosynthesis and beta-alanine metabolism
Genetics
172
1665-1674
2006
Drosophila melanogaster
brenda
West, T.P.
Pyrimidine base catabolism in Pseudomonas putida biotype B
Antonie van Leeuwenhoek
80
163-167
2001
Pseudomonas putida
brenda
Lundgren, S.; Andersen, B.; Piskur, J.; Dobritzsch, D.
Crystallization and preliminary X-ray data analysis of beta-alanine synthase from Drosophila melanogaster
Acta Crystallogr. Sect. F
63
874-877
2007
Drosophila melanogaster
brenda
Schnackerz, K.D.; Dobritzsch, D.
Amidohydrolases of the reductive pyrimidine catabolic pathway: Purification, characterization, structure, reaction mechanisms and enzyme deficiency
Biochim. Biophys. Acta
1784
431-444
2008
Arabidopsis thaliana, Bos taurus, Caenorhabditis elegans, Dictyostelium discoideum, Drosophila melanogaster, Euglena gracilis, Homo sapiens, Pseudomonas putida, Rattus norvegicus, Zea mays, Lachancea kluyveri
brenda
Lundgren, S.; Andersen, B.; Piskur, J.; Dobritzsch, D.
Crystal structures of yeast beta-alanine synthase complexes reveal the mode of substrate binding and large scale domain closure movements
J. Biol. Chem.
282
36037-36047
2007
Lachancea kluyveri (Q96W94), Lachancea kluyveri
brenda
Lundgren, S.; Lohkamp, B.; Andersen, B.; Piskur, J.; Dobritzsch, D.
The crystal structure of beta-alanine synthase from Drosophila melanogaster reveals a homooctameric helical turn-like assembly
J. Mol. Biol.
377
1544-1559
2008
Drosophila melanogaster
brenda
van Kuilenburg, A.B.; van Lenthe, H.; van Gennip, A.H.
Activity of pyrimidine degradation enzymes in normal tissues
Nucleosides Nucleotides Nucleic Acids
25
1211-1214
2006
Homo sapiens
brenda
Thomas, H.R.; Ezzeldin, H.H.; Guarcello, V.; Mattison, L.K.; Fridley, B.L.; Diasio, R.B.
Genetic regulation of beta-ureidopropionase and its possible implication in altered uracil catabolism
Pharmacogenet. Genomics
18
25-35
2008
Homo sapiens
brenda
Martinez-Gomez, A.I.; Martinez-Rodriguez, S.; Pozo-Dengra, J.; Tessaro, D.; Servi, S.; Clemente-Jimenez, J.M.; Rodriguez-Vico, F.; Las Heras-Vazquez, F.J.
Potential application of N-carbamoyl-beta-alanine amidohydrolase from Agrobacterium tumefaciens C58 for beta-amino acid production
Appl. Environ. Microbiol.
75
514-520
2009
Agrobacterium tumefaciens, Agrobacterium tumefaciens C58 / ATCC 33970
brenda
Zrenner, R.; Riegler, H.; Marquard, C.R.; Lange, P.R.; Geserick, C.; Bartosz, C.E.; Chen, C.T.; Slocum, R.D.
A functional analysis of the pyrimidine catabolic pathway in Arabidopsis
New Phytol.
183
117-132
2009
Arabidopsis thaliana (Q8H183)
brenda
Kuhara, T.; Ohse, M.; Inoue, Y.; Shinka, T.
Five cases of beta-ureidopropionase deficiency detected by GC/MS analysis of urine metabolome
J. Mass Spectrom.
44
214-221
2009
Homo sapiens
brenda
Janowitz, T.; Ajonina, I.; Perbandt, M.; Woltersdorf, C.; Hertel, P.; Liebau, E.; Gigengack, U.
The 3-ureidopropionase of Caenorhabditis elegans, an enzyme involved in pyrimidine degradation
FEBS J.
277
4100-4109
2010
Caenorhabditis elegans (Q19437), Caenorhabditis elegans
brenda
Martinez-Gomez, A.I.; Andujar-Sanchez, M.; Clemente-Jimenez, J.M.; Neira, J.L.; Rodriguez-Vico, F.; Martinez-Rodriguez, S.; Las Heras-Vazquez, F.J.
N-Carbamoyl-beta-alanine amidohydrolase from Agrobacterium tumefaciens C58: a promiscuous enzyme for the production of amino acids
J. Chromatogr. B
879
3277-3282
2011
Agrobacterium tumefaciens, Agrobacterium tumefaciens C58 / ATCC 33970
brenda
Van Kuilenburg, A.; Dobritzsch, D.; Meijer, J.; Krumpel, M.; Selim, L.; Rashed, M.; Assmann, B.; Meinsma, R.; Lohkamp, B.; Ito, T.; Abeling, N.; Saito, K.; Eto, K.; Smitka, M.; Engvall, M.; Zhang, C.; Xu, W.; Zoetekouw, L.; Hennekam, R.
beta-Ureidopropionase deficiency: phenotype, genotype and protein structural consequences in 16 patients
Biochim. Biophys. Acta
1822
1096-1108
2012
Homo sapiens (Q9UBR1)
brenda
Lam, C.W.; Law, C.Y.; Leung, K.F.; Lai, C.K.; Pak-lam Chen, S.; Chan, B.; Chan, K.Y.; Yuen, Y.P.; Mak, C.M.; Yan-wo Chan, A.
NMR-based urinalysis for rapid diagnosis of beta-ureidopropionase deficiency in a patient with Dravet syndrome
Clin. Chim. Acta
440
201-204
2015
Homo sapiens (Q9UBR1), Homo sapiens
brenda
Meijer, J.; Nakajima, Y.; Zhang, C.; Meinsma, R.; Ito, T.; Van Kuilenburg, A.B.
Publishers note. Identification of a novel synonymous mutation in the human beta-ureidopropionase gene UPB1 affecting pre-mRNA splicing
Nucleosides Nucleotides Nucleic Acids
33
639-645
2014
Homo sapiens (Q9UBR1)
brenda
Fidlerova, J.; Kleiblova, P.; Kormunda, S.; Novotny, J.; Kleibl, Z.
Contribution of the beta-ureidopropionase (UPB1) gene alterations to the development of fluoropyrimidine-related toxicity
Pharmacol. Rep.
64
1234-1242
2012
Homo sapiens (Q9UBR1)
brenda
Shen, Y.; Chen, Y.; Liu, H.; Chiang, F.; Wang, Y.; Hou, L.; Lin, J.; Lin, C.; Lin, H.; Lai, H.; Jeng, S.
Expression of a gene encoding beta-ureidopropionase is critical for pollen germination in tomatoes
Physiol. Plant.
150
425-435
2014
Solanum lycopersicum, Solanum lycopersicum CL5915, Solanum lycopersicum L4783
brenda
Maurer, D.; Lohkamp, B.; Krumpel, M.; Widersten, M.; Dobritzsch, D.
Crystal structure and pH-dependent allosteric regulation of human beta-ureidopropionase, an enzyme involved in anticancer drug metabolism
Biochem. J.
475
2395-2416
2018
Homo sapiens (Q9UBR1)
brenda
Kummer, D.; Froehlich, T.K.; Joerger, M.; Aebi, S.; Sistonen, J.; Amstutz, U.; Largiader, C.R.
Dihydropyrimidinase and beta-ureidopropionase gene variation and severe fluoropyrimidine-related toxicity
Pharmacogenomics
16
1367-1377
2015
Homo sapiens (Q9UBR1)
brenda