BRENDA - Enzyme Database show
show all sequences of 3.5.1.6

Characterization of plant beta-ureidopropionase and functional overexpression in Escherichia coli

Walsh, T.A.; Green, S.B.; Larrinua, I.M.; Schmitzer, P.R.; Plant Physiol. 125, 1001-1011 (2001)

Data extracted from this reference:

Cloned(Commentary)
Commentary
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
Commentary
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
Commentary
Organism
Structure
0.006
-
2-methyl-N-carbamoyl-beta-alanine
pH 7, 25C
Zea mays
0.011
-
N-Carbamoyl-beta-alanine
pH 7, 25C
Zea mays
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
soluble
recombinant beta-UP expressed in Escherichia coli BL21
Arabidopsis sp.
-
-
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Zn2+
Zn2+-dependent enzyme, required as a catalytic cofactor
Zea mays
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
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
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
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
Primary Accession No. (UniProt)
Commentary
Textmining
Arabidopsis sp.
-
-
-
Zea mays
-
-
-
Purification (Commentary)
Commentary
Organism
partial
Zea mays
recombinant beta-UP
Arabidopsis sp.
Reaction
Reaction
Commentary
Organism
3-ureidopropanoate + H2O = beta-alanine + CO2 + NH3
mechanism
Zea mays
Source Tissue
Source Tissue
Commentary
Organism
Textmining
shoot
of etiolated seedlings
Zea mays
-
Specific Activity [micromol/min/mg]
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
0.03
-
recombinant beta-UP
Arabidopsis sp.
Storage Stability
Storage Stability
Organism
-70C, partially purified beta-UP, in presence of 10% w/v glycerol, several months, stable
Zea mays
4C, partially purified beta-UP, in presence of Mg2+ and dithiothreitol, 7 days, about 10% loss of activity
Zea mays
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2-methyl-N-carbamoyl-beta-alanine + H2O
-
657030
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
657030
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
657030
Arabidopsis sp.
2-methyl-beta-alanine + CO2 + NH3
-
-
-
?
2-methyl-N-carbamoyl-beta-alanine + H2O
only one enantiomer of the racemic substrate is hydrolyzed
657030
Zea mays
2-methyl-beta-alanine + CO2 + NH3
-
-
-
?
N-carbamoyl-beta-alanine + H2O
-
657030
Zea mays
beta-alanine + CO2 + NH3
-
-
-
?
N-carbamoyl-beta-alanine + H2O
-
657030
Arabidopsis sp.
beta-alanine + CO2 + NH3
-
-
-
?
N-carbamoyl-beta-alanine + H2O
final enzyme of the catabolic pathway of pyrimidine bases, substrate derives from uracil
657030
Zea mays
beta-alanine + CO2 + NH3
-
-
-
?
N-carbamoyl-beta-alanine + H2O
final enzyme of the catabolic pathway of pyrimidine bases, substrate derives from uracil
657030
Arabidopsis sp.
beta-alanine + CO2 + NH3
-
-
-
?
Subunits
Subunits
Commentary
Organism
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.
decamer
-
Zea mays
dimer
recombinant beta-UP is dimeric at pH 5.6, in the absence of glycerol
Arabidopsis sp.
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
25
-
assay at
Zea mays
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6
7.2
broad optimum at mildly acidic pH values
Zea mays
pH Range
pH Minimum
pH Maximum
Commentary
Organism
additional information
-
activity declines at more alkaline pH values
Zea mays
pI Value
Organism
Commentary
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
Commentary
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
Cloned(Commentary) (protein specific)
Commentary
Organism
cDNA truncated at the N-terminus by 14 residues, overexpression in Escherichia coli BL21
Arabidopsis sp.
General Stability (protein specific)
General Stability
Organism
dithiothreitol and glycerol stabilize
Arabidopsis sp.
IC50 Value (protein specific)
IC50 Value
IC50 Value Maximum
Commentary
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
Inhibitors (protein specific)
Inhibitors
Commentary
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] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.006
-
2-methyl-N-carbamoyl-beta-alanine
pH 7, 25C
Zea mays
0.011
-
N-Carbamoyl-beta-alanine
pH 7, 25C
Zea mays
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
soluble
recombinant beta-UP expressed in Escherichia coli BL21
Arabidopsis sp.
-
-
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Zn2+
Zn2+-dependent enzyme, required as a catalytic cofactor
Zea mays
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
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) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
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
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
partial
Zea mays
recombinant beta-UP
Arabidopsis sp.
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
shoot
of etiolated seedlings
Zea mays
-
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
0.03
-
recombinant beta-UP
Arabidopsis sp.
Storage Stability (protein specific)
Storage Stability
Organism
-70C, partially purified beta-UP, in presence of 10% w/v glycerol, several months, stable
Zea mays
4C, partially purified beta-UP, in presence of Mg2+ and dithiothreitol, 7 days, about 10% loss of activity
Zea mays
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2-methyl-N-carbamoyl-beta-alanine + H2O
-
657030
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
657030
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
657030
Arabidopsis sp.
2-methyl-beta-alanine + CO2 + NH3
-
-
-
?
2-methyl-N-carbamoyl-beta-alanine + H2O
only one enantiomer of the racemic substrate is hydrolyzed
657030
Zea mays
2-methyl-beta-alanine + CO2 + NH3
-
-
-
?
N-carbamoyl-beta-alanine + H2O
-
657030
Zea mays
beta-alanine + CO2 + NH3
-
-
-
?
N-carbamoyl-beta-alanine + H2O
-
657030
Arabidopsis sp.
beta-alanine + CO2 + NH3
-
-
-
?
N-carbamoyl-beta-alanine + H2O
final enzyme of the catabolic pathway of pyrimidine bases, substrate derives from uracil
657030
Zea mays
beta-alanine + CO2 + NH3
-
-
-
?
N-carbamoyl-beta-alanine + H2O
final enzyme of the catabolic pathway of pyrimidine bases, substrate derives from uracil
657030
Arabidopsis sp.
beta-alanine + CO2 + NH3
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
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.
decamer
-
Zea mays
dimer
recombinant beta-UP is dimeric at pH 5.6, in the absence of glycerol
Arabidopsis sp.
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
25
-
assay at
Zea mays
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6
7.2
broad optimum at mildly acidic pH values
Zea mays
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
additional information
-
activity declines at more alkaline pH values
Zea mays
pI Value (protein specific)
Organism
Commentary
pI Value Maximum
pI Value
Arabidopsis sp.
recombinant beta-UP, isoelectric focusing
-
6
Arabidopsis sp.
recombinant beta-UP, sequence calculation
-
7.1
Other publictions for EC 3.5.1.6
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [C]
Temperature Range [C]
Temperature Stability [C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [C] (protein specific)
Temperature Range [C] (protein specific)
Temperature Stability [C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
733675
Lam
NMR-based urinalysis for rapid ...
Homo sapiens
Clin. Chim. Acta
440
201-204
2015
-
-
1
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
734810
Meijer
Publishers note. Identificatio ...
Homo sapiens
Nucleosides Nucleotides Nucleic Acids
33
639-645
2014
-
-
1
-
3
-
-
-
-
-
-
2
-
1
-
-
-
-
-
2
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
3
-
-
-
-
-
-
-
-
2
-
-
-
-
-
2
-
-
2
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
734855
Shen
Expression of a gene encoding ...
Solanum lycopersicum, Solanum lycopersicum CL5915, Solanum lycopersicum L4783
Physiol. Plant.
150
425-435
2014
-
-
1
-
1
-
-
-
-
-
-
-
-
4
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
733382
Van Kuilenburg
beta-Ureidopropionase deficien ...
Homo sapiens
Biochim. Biophys. Acta
1822
1096-1108
2012
-
-
1
-
6
-
-
-
-
-
1
2
-
1
-
-
1
-
-
-
3
-
2
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
6
-
-
-
-
-
-
-
1
2
-
-
-
1
-
-
3
-
2
1
-
-
-
-
-
-
-
-
-
3
3
-
-
-
734844
Fidlerova
Contribution of the beta-ureid ...
Homo sapiens
Pharmacol. Rep.
64
1234-1242
2012
-
-
1
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
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Matthews
Regulation of N-carbamoyl-beta ...
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Traut
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Kaspari
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Wasternack
Pyrimidine-degrading enzymes p ...
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12
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
7
-
4
-
1
1
5
-
-
-
1
-
4
1
-
12
-
1
-
-
-
1
-
-
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172062
Campbell
Reductive degradation of pyrim ...
Canis lupus familiaris, Clostridium uracilicum, Clostridium uracilicum M5-2, Oryctolagus cuniculus, Pigeon, Rattus rattus
J. Biol. Chem.
235
2375-2379
1960
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-
-
-
-
-
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1
-
-
-
6
-
9
-
-
1
-
-
4
-
-
12
-
1
1
1
-
2
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
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1
-
-
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6
-
-
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1
-
4
-
-
12
-
1
1
1
-
2
1
-
-
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-
-
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-
172063
Caravaca
Enzymatic decarbamylation of c ...
Canis lupus familiaris, Oryctolagus cuniculus, Pigeon, Rattus rattus
J. Biol. Chem.
231
357-365
1958
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-
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2
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4
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4
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4
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4
4
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12
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-
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-
-
2
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-
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2
-
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4
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4
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4
4
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12
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2
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