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Literature summary for 3.5.1.6 extracted from

  • Walsh, T.A.; Green, S.B.; Larrinua, I.M.; Schmitzer, P.R.
    Characterization of plant beta-ureidopropionase and functional overexpression in Escherichia coli (2001), Plant Physiol., 125, 1001-1011.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
cDNA truncated at the N-terminus by 14 residues, overexpression in Escherichia coli BL21 Arabidopsis sp.

General Stability

General Stability Organism
dithiothreitol and glycerol stabilize Arabidopsis sp.

Inhibitors

Inhibitors Comment Organism Structure
(R)-2-phenylpropionic acid IC50: 0.115 mM Zea mays
(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 Zea mays
(RS)-2-benzylpropionic acid IC50: 0.006 mM Zea mays
(S)-2-phenylpropionic acid IC50: 0.0057 mM Zea mays
1,10-phenanthroline 1 mM, 96% inhibition, activity can be partially restored by Zn2+ Zea mays
2,6-dipicolinic acid 1 mM, 33% inhibition Zea mays
2-methyl-N-carbamoyl-beta-alanine competitive inhibitor of the reaction with N-carbamoyl-beta-alanine Zea mays
3-Phenylpropionic acid IC50: 0.0056 mM Zea mays
8-hydroxyquinoline 1 mM, 29% inhibition Zea mays
Cu2+ 0.2 mM, complete inhibition Zea mays
cyclopropanecarboxylic acid IC50: 0.008 mM Zea mays
EDTA 1 mM, 56% inhibition Zea mays
iodoacetamide 1 mM, complete inhibition, completely prevented by addition of substrate, the sensitive thiol group is located at the active site Zea mays
isobutyric acid IC50: 0.018 mM Zea mays
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 Zea mays
n-butyric acid IC50: 0.055 mM Zea mays
p-chloromercuribenzenesulfonic acid complete inhibition Zea mays
propionic acid IC50: 0.025 mM Zea mays

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.006
-
2-methyl-N-carbamoyl-beta-alanine pH 7, 25°C Zea mays
0.011
-
N-Carbamoyl-beta-alanine pH 7, 25°C Zea mays

Localization

Localization Comment Organism GeneOntology No. Textmining
soluble recombinant beta-UP expressed in Escherichia coli BL21 Arabidopsis sp.
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ Zn2+-dependent enzyme, required as a catalytic cofactor Zea mays

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
43000
-
10 * 43000, recombinant beta-UP, at pH 7, SDS-PAGE, 10 * 43723, recombinant beta-UP, at pH 7, mass spectrometry, 10 * 43733, sequence calculation Arabidopsis sp.
43723
-
10 * 43000, recombinant beta-UP, at pH 7, SDS-PAGE, 10 * 43723, recombinant beta-UP, at pH 7, mass spectrometry, 10 * 43733, sequence calculation Arabidopsis sp.
43733
-
10 * 43000, recombinant beta-UP, at pH 7, SDS-PAGE, 10 * 43723, recombinant beta-UP, at pH 7, mass spectrometry, 10 * 43733, sequence calculation Arabidopsis sp.
90000
-
gel filtration at pH 5.6, in the absence of glycerol Arabidopsis sp.
400000
-
above, native state of beta-UP, gel filtration at pH 7.3, in the presence of 5% v/v glycerol Arabidopsis sp.
440000
-
native state of beta-UP, gel filtration Zea mays

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2-methyl-N-carbamoyl-beta-alanine + H2O Zea mays final enzyme of the catabolic pathway of pyrimidine bases, substrate derives from thymine 2-methyl-beta-alanine + CO2 + NH3
-
?
2-methyl-N-carbamoyl-beta-alanine + H2O Arabidopsis sp. final enzyme of the catabolic pathway of pyrimidine bases, substrate derives from thymine 2-methyl-beta-alanine + CO2 + NH3
-
?
N-carbamoyl-beta-alanine + H2O Zea mays final enzyme of the catabolic pathway of pyrimidine bases, substrate derives from uracil beta-alanine + CO2 + NH3
-
?
N-carbamoyl-beta-alanine + H2O Arabidopsis sp. final enzyme of the catabolic pathway of pyrimidine bases, substrate derives from uracil beta-alanine + CO2 + NH3
-
?

Organism

Organism UniProt Comment Textmining
Arabidopsis sp.
-
-
-
Zea mays
-
-
-

Purification (Commentary)

Purification (Comment) Organism
partial Zea mays
recombinant beta-UP Arabidopsis sp.

Reaction

Reaction Comment Organism Reaction ID
3-ureidopropanoate + H2O = beta-alanine + CO2 + NH3 mechanism Zea mays

Source Tissue

Source Tissue Comment Organism Textmining
shoot of etiolated seedlings Zea mays
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.03
-
recombinant beta-UP Arabidopsis sp.

Storage Stability

Storage Stability Organism
-70°C, partially purified beta-UP, in presence of 10% w/v glycerol, several months, stable Zea mays
4°C, partially purified beta-UP, in presence of Mg2+ and dithiothreitol, 7 days, about 10% loss of activity Zea mays

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-methyl-N-carbamoyl-beta-alanine + H2O
-
Arabidopsis sp. 2-methyl-beta-alanine + CO2 + NH3
-
?
2-methyl-N-carbamoyl-beta-alanine + H2O final enzyme of the catabolic pathway of pyrimidine bases, substrate derives from thymine Zea mays 2-methyl-beta-alanine + CO2 + NH3
-
?
2-methyl-N-carbamoyl-beta-alanine + H2O final enzyme of the catabolic pathway of pyrimidine bases, substrate derives from thymine Arabidopsis sp. 2-methyl-beta-alanine + CO2 + NH3
-
?
2-methyl-N-carbamoyl-beta-alanine + H2O only one enantiomer of the racemic substrate is hydrolyzed Zea mays 2-methyl-beta-alanine + CO2 + NH3
-
?
N-carbamoyl-beta-alanine + H2O
-
Zea mays beta-alanine + CO2 + NH3
-
?
N-carbamoyl-beta-alanine + H2O
-
Arabidopsis sp. beta-alanine + CO2 + NH3
-
?
N-carbamoyl-beta-alanine + H2O final enzyme of the catabolic pathway of pyrimidine bases, substrate derives from uracil Zea mays beta-alanine + CO2 + NH3
-
?
N-carbamoyl-beta-alanine + H2O final enzyme of the catabolic pathway of pyrimidine bases, substrate derives from uracil Arabidopsis sp. beta-alanine + CO2 + NH3
-
?

Subunits

Subunits Comment Organism
decamer
-
Zea mays
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 Arabidopsis sp.
dimer recombinant beta-UP is dimeric at pH 5.6, in the absence of glycerol Arabidopsis sp.

Synonyms

Synonyms Comment Organism
beta-Ala synthase
-
Zea mays
beta-UP
-
Zea mays
beta-UP
-
Arabidopsis sp.
N-carbamoyl-beta-Ala amidohydrolase
-
Zea mays

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Zea mays

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6 7.2 broad optimum at mildly acidic pH values Zea mays

pH Range

pH Minimum pH Maximum Comment Organism
additional information
-
activity declines at more alkaline pH values Zea mays

pI Value

Organism Comment pI Value Maximum pI Value
Arabidopsis sp. recombinant beta-UP, isoelectric focusing
-
6
Arabidopsis sp. recombinant beta-UP, sequence calculation
-
7.1

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
0.0005
-
most potent inhibitor of aryl propionates, IC50: 500 nM, completely reversible by passing the enzyme-inhibitor complex over a gel filtration column Zea mays (RS)-2-(2,6-dinitrophenoxy)-propionate
0.0056
-
IC50: 0.0056 mM Zea mays 3-Phenylpropionic acid
0.0057
-
IC50: 0.0057 mM Zea mays (S)-2-phenylpropionic acid
0.006
-
IC50: 0.006 mM Zea mays (RS)-2-benzylpropionic acid
0.008
-
IC50: 0.008 mM Zea mays cyclopropanecarboxylic acid
0.018
-
IC50: 0.018 mM Zea mays isobutyric acid
0.025
-
IC50: 0.025 mM Zea mays propionic acid
0.055
-
IC50: 0.055 mM Zea mays n-butyric acid
0.115
-
IC50: 0.115 mM Zea mays (R)-2-phenylpropionic acid