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Literature summary 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)

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

General Stability

EC Number General Stability Organism
3.5.1.6 dithiothreitol and glycerol stabilize Arabidopsis sp.

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.5.1.6 (R)-2-phenylpropionic acid IC50: 0.115 mM Zea mays
3.5.1.6 (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
3.5.1.6 (RS)-2-benzylpropionic acid IC50: 0.006 mM Zea mays
3.5.1.6 (S)-2-phenylpropionic acid IC50: 0.0057 mM Zea mays
3.5.1.6 1,10-phenanthroline 1 mM, 96% inhibition, activity can be partially restored by Zn2+ Zea mays
3.5.1.6 2,6-dipicolinic acid 1 mM, 33% inhibition Zea mays
3.5.1.6 2-methyl-N-carbamoyl-beta-alanine competitive inhibitor of the reaction with N-carbamoyl-beta-alanine Zea mays
3.5.1.6 3-Phenylpropionic acid IC50: 0.0056 mM Zea mays
3.5.1.6 8-hydroxyquinoline 1 mM, 29% inhibition Zea mays
3.5.1.6 Cu2+ 0.2 mM, complete inhibition Zea mays
3.5.1.6 cyclopropanecarboxylic acid IC50: 0.008 mM Zea mays
3.5.1.6 EDTA 1 mM, 56% inhibition Zea mays
3.5.1.6 iodoacetamide 1 mM, complete inhibition, completely prevented by addition of substrate, the sensitive thiol group is located at the active site Zea mays
3.5.1.6 isobutyric acid IC50: 0.018 mM Zea mays
3.5.1.6 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
3.5.1.6 n-butyric acid IC50: 0.055 mM Zea mays
3.5.1.6 p-chloromercuribenzenesulfonic acid complete inhibition Zea mays
3.5.1.6 propionic acid IC50: 0.025 mM Zea mays

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.5.1.6 0.006
-
2-methyl-N-carbamoyl-beta-alanine pH 7, 25°C Zea mays
3.5.1.6 0.011
-
N-Carbamoyl-beta-alanine pH 7, 25°C Zea mays

Localization

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

Metals/Ions

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

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.5.1.6 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.
3.5.1.6 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.
3.5.1.6 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.
3.5.1.6 90000
-
gel filtration at pH 5.6, in the absence of glycerol Arabidopsis sp.
3.5.1.6 400000
-
above, native state of beta-UP, gel filtration at pH 7.3, in the presence of 5% v/v glycerol Arabidopsis sp.
3.5.1.6 440000
-
native state of beta-UP, gel filtration Zea mays

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.5.1.6 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
-
?
3.5.1.6 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
-
?
3.5.1.6 N-carbamoyl-beta-alanine + H2O Zea mays final enzyme of the catabolic pathway of pyrimidine bases, substrate derives from uracil beta-alanine + CO2 + NH3
-
?
3.5.1.6 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

EC Number Organism UniProt Comment Textmining
3.5.1.6 Arabidopsis sp.
-
-
-
3.5.1.6 Zea mays
-
-
-

Purification (Commentary)

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

Reaction

EC Number Reaction Comment Organism Reaction ID
3.5.1.6 3-ureidopropanoate + H2O = beta-alanine + CO2 + NH3 mechanism Zea mays

Source Tissue

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

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.5.1.6 0.03
-
recombinant beta-UP Arabidopsis sp.

Storage Stability

EC Number Storage Stability Organism
3.5.1.6 -70°C, partially purified beta-UP, in presence of 10% w/v glycerol, several months, stable Zea mays
3.5.1.6 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)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.1.6 2-methyl-N-carbamoyl-beta-alanine + H2O
-
Arabidopsis sp. 2-methyl-beta-alanine + CO2 + NH3
-
?
3.5.1.6 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
-
?
3.5.1.6 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
-
?
3.5.1.6 2-methyl-N-carbamoyl-beta-alanine + H2O only one enantiomer of the racemic substrate is hydrolyzed Zea mays 2-methyl-beta-alanine + CO2 + NH3
-
?
3.5.1.6 N-carbamoyl-beta-alanine + H2O
-
Zea mays beta-alanine + CO2 + NH3
-
?
3.5.1.6 N-carbamoyl-beta-alanine + H2O
-
Arabidopsis sp. beta-alanine + CO2 + NH3
-
?
3.5.1.6 N-carbamoyl-beta-alanine + H2O final enzyme of the catabolic pathway of pyrimidine bases, substrate derives from uracil Zea mays beta-alanine + CO2 + NH3
-
?
3.5.1.6 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

EC Number Subunits Comment Organism
3.5.1.6 decamer
-
Zea mays
3.5.1.6 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.
3.5.1.6 dimer recombinant beta-UP is dimeric at pH 5.6, in the absence of glycerol Arabidopsis sp.

Synonyms

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

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.5.1.6 25
-
assay at Zea mays

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.5.1.6 6 7.2 broad optimum at mildly acidic pH values Zea mays

pH Range

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

pI Value

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

IC50 Value

EC Number IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
3.5.1.6 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
3.5.1.6 0.0056
-
IC50: 0.0056 mM Zea mays 3-Phenylpropionic acid
3.5.1.6 0.0057
-
IC50: 0.0057 mM Zea mays (S)-2-phenylpropionic acid
3.5.1.6 0.006
-
IC50: 0.006 mM Zea mays (RS)-2-benzylpropionic acid
3.5.1.6 0.008
-
IC50: 0.008 mM Zea mays cyclopropanecarboxylic acid
3.5.1.6 0.018
-
IC50: 0.018 mM Zea mays isobutyric acid
3.5.1.6 0.025
-
IC50: 0.025 mM Zea mays propionic acid
3.5.1.6 0.055
-
IC50: 0.055 mM Zea mays n-butyric acid
3.5.1.6 0.115
-
IC50: 0.115 mM Zea mays (R)-2-phenylpropionic acid