BRENDA - Enzyme Database show
show all sequences of 5.1.1.4

Identification and characterization of bifunctional proline racemase/hydroxyproline epimerase from archaea: discrimination of substrates and molecular evolution

Watanabe, S.; Tanimoto, Y.; Nishiwaki, H.; Watanabe, Y.; PLoS One 10, e0120349 (2015)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expression in Escherichia coli
Clostridioides difficile
expression in Escherichia coli
Ferroplasma acidarmanus
expression in Escherichia coli
Haloarcula japonica
expression in Escherichia coli
Thermococcus litoralis
Engineering
Amino acid exchange
Commentary
Organism
R240W
mutant enzyme shows similar kinetic constants for proline and hydroxyproline as compared to the wild-type enzyme
Ferroplasma acidarmanus
W241F the mutant enzyme
shows 5.3fold, 430fold, and 5.8fold lower kcat/Km values for trans-4-hydroxy-L-proline, trans-3-hydroxy-L-proline, and cis-4-hydroxy-D-proline respectively, mainly due to a marked decrease in kcat values, whereas no significant effects are found in the kinetic constants of proline, suggesting that this (hydrophobic and bulky) tryptophan residue plays an importance role in the recognition of hydroxyproline (more hydrophilic and bulky than proline)
Thermococcus litoralis
Inhibitors
Inhibitors
Commentary
Organism
Structure
pyrrole-2-carboxylate
-
Clostridioides difficile
pyrrole-2-carboxylate
-
Ferroplasma acidarmanus
pyrrole-2-carboxylate
-
Haloarcula japonica
pyrrole-2-carboxylate
-
Thermococcus litoralis
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.092
-
D-proline
pH 8.0, 50C, wild-type enzyme
Thermococcus litoralis
0.156
-
D-proline
pH 8.0, 50C, mutant enzyme F62V
Thermococcus litoralis
0.194
-
D-proline
pH 8.0, 50C, mutant enzyme W241F
Thermococcus litoralis
0.612
-
D-proline
pH 8.0, 50C, wild-type enzyme
Clostridioides difficile
1.17
-
D-proline
pH 8.0, 50C, wild-type enzyme
Ferroplasma acidarmanus
1.21
-
L-proline
pH 8.0, 50C, wild-type enzyme
Thermococcus litoralis
1.29
-
L-proline
pH 8.0, 50C, mutant enzyme W241F
Thermococcus litoralis
1.93
-
L-proline
pH 8.0, 50C, mutant enzyme F62V
Thermococcus litoralis
2.54
-
D-proline
pH 8.0, 50C, mutant enzyme L221H
Thermococcus litoralis
4
-
D-proline
pH 8.0, 50C, mutant enzyme F62S
Thermococcus litoralis
8.53
-
L-proline
pH 8.0, 50C, wild-type enzyme
Clostridioides difficile
20.5
-
L-proline
pH 8.0, 50C, mutant enzyme L221H
Thermococcus litoralis
31.6
-
L-proline
pH 8.0, 50C, wild-type enzyme
Ferroplasma acidarmanus
53
-
L-proline
pH 8.0, 50C, mutant enzyme F240W
Ferroplasma acidarmanus
154
-
L-proline
pH 8.0, 50C, mutant enzyme F62S
Thermococcus litoralis
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
40000
-
x * 40000, SDS-PAGE
Clostridioides difficile
40000
-
x * 40000, SDS-PAGE
Ferroplasma acidarmanus
40000
-
x * 40000, SDS-PAGE
Thermococcus litoralis
42000
-
x * 42000, SDS-PAGE
Haloarcula japonica
80000
-
gel filtration
Clostridioides difficile
80000
-
gel filtration
Ferroplasma acidarmanus
80000
-
gel filtration
Haloarcula japonica
80000
-
gel filtration
Thermococcus litoralis
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Clostridioides difficile
Q17ZY4
-
-
Ferroplasma acidarmanus
S0APF4
-
-
Haloarcula japonica
M0LMI3
-
-
Haloarcula japonica DSM 6131
M0LMI3
-
-
Thermococcus litoralis
H3ZMH5
-
-
Thermococcus litoralis DSM 5473
H3ZMH5
-
-
Purification (Commentary)
Commentary
Organism
-
Clostridioides difficile
-
Ferroplasma acidarmanus
-
Haloarcula japonica
-
Thermococcus litoralis
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-proline
the reaction is completely bi-directional, and the reverse reactions. The specific activity with D-proline is 130% compared to the L-enantiomer. The bifunctional enzyme reversibly catalyzes the racemization of proline and the epimerization of 4-hydroxyproline and 3-hydroxyproline with similar kinetic constants. Catalysis is based on the same 1,1-proton transfer mechanism using two general acidic/basic cysteine residues located on opposite faces of the active site
730678
Thermococcus litoralis
L-proline
-
-
-
?
D-proline
the reaction is completely bi-directional, and the reverse reactions. The specific activity with D-proline is 130% compared to the L-enantiomer. The bifunctional enzyme reversibly catalyzes the racemization of proline and the epimerization of 4-hydroxyproline and 3-hydroxyproline with similar kinetic constants. Catalysis is based on the same 1,1-proton transfer mechanism using two general acidic/basic cysteine residues located on opposite faces of the active site
730678
Thermococcus litoralis DSM 5473
L-proline
-
-
-
?
L-azetidine-2-carboxylate
low activity
730678
Thermococcus litoralis
D-azetidine-2-carboxylate
-
-
-
?
L-azetidine-2-carboxylate
low activity
730678
Thermococcus litoralis DSM 5473
D-azetidine-2-carboxylate
-
-
-
?
L-pipecolate
low activity
730678
Thermococcus litoralis
D-pipecolate
-
-
-
?
L-pipecolate
low activity
730678
Thermococcus litoralis DSM 5473
D-pipecolate
-
-
-
?
L-proline
-
730678
Clostridioides difficile
D-proline
-
-
-
r
L-proline
kcat/Km value for trans-4-hydroxy-L-proline is about 3fold lower than that for L-proline, which is attributed to a 17fold lower kcat value. The kinetic parameters of the epimerization of cis-4-hydroxy-D-proline can not be determined
730678
Ferroplasma acidarmanus
D-proline
-
-
-
r
L-proline
the enzyme can utilize both proline and hydroxyprolines as substrate
730678
Haloarcula japonica
D-proline
-
-
-
r
L-proline
the reaction is completely bi-directional, and the reverse reactions. The specific activity with D-proline is 130% compared to the L-enantiomer. The bifunctional enzyme reversibly catalyzes the racemization of proline and the epimerization of 4-hydroxyproline and 3-hydroxyproline with similar kinetic constants. Catalysis is based on the same 1,1-proton transfer mechanism using two general acidic/basic cysteine residues located on opposite faces of the active site
730678
Thermococcus litoralis
D-proline
-
-
-
r
L-proline
the reaction is completely bi-directional, and the reverse reactions. The specific activity with D-proline is 130% compared to the L-enantiomer. The bifunctional enzyme reversibly catalyzes the racemization of proline and the epimerization of 4-hydroxyproline and 3-hydroxyproline with similar kinetic constants. Catalysis is based on the same 1,1-proton transfer mechanism using two general acidic/basic cysteine residues located on opposite faces of the active site
730678
Thermococcus litoralis DSM 5473
D-proline
-
-
-
r
L-proline
the enzyme can utilize both proline and hydroxyprolines as substrate
730678
Haloarcula japonica DSM 6131
D-proline
-
-
-
r
Subunits
Subunits
Commentary
Organism
?
x * 40000, SDS-PAGE
Clostridioides difficile
?
x * 40000, SDS-PAGE
Ferroplasma acidarmanus
?
x * 42000, SDS-PAGE
Haloarcula japonica
?
x * 40000, SDS-PAGE
Thermococcus litoralis
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
50
-
assay at
Clostridioides difficile
50
-
assay at
Ferroplasma acidarmanus
50
-
assay at
Haloarcula japonica
50
-
assay at
Thermococcus litoralis
90
100
-
Clostridioides difficile
90
100
-
Ferroplasma acidarmanus
90
100
-
Haloarcula japonica
90
100
-
Thermococcus litoralis
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.0235
-
D-proline
pH 8.0, 50C, mutant enzyme F62V
Thermococcus litoralis
0.026
-
D-proline
pH 8.0, 50C, mutant enzyme F62S
Thermococcus litoralis
0.092
-
L-proline
pH 8.0, 50C, mutant enzyme F62V
Thermococcus litoralis
0.119
-
D-proline
pH 8.0, 50C, wild-type enzyme
Ferroplasma acidarmanus
0.2
-
L-proline
pH 8.0, 50C, mutant enzyme F62S
Thermococcus litoralis
0.29
-
D-proline
pH 8.0, 50C, mutant enzyme L221H
Thermococcus litoralis
0.42
-
L-proline
pH 8.0, 50C, mutant enzyme F240W
Ferroplasma acidarmanus
0.6
-
L-proline
pH 8.0, 50C, wild-type enzyme
Ferroplasma acidarmanus
0.92
-
L-proline
pH 8.0, 50C, mutant enzyme L221H
Thermococcus litoralis
2.22
-
D-proline
pH 8.0, 50C, wild-type enzyme
Thermococcus litoralis
2.48
-
D-proline
pH 8.0, 50C, wild-type enzyme
Clostridioides difficile
2.78
-
L-proline
pH 8.0, 50C, wild-type enzyme
Thermococcus litoralis
3.17
-
L-proline
pH 8.0, 50C, mutant enzyme W241F
Thermococcus litoralis
3.18
-
D-proline
pH 8.0, 50C, mutant enzyme W241F
Thermococcus litoralis
14.15
-
L-proline
pH 8.0, 50C, wild-type enzyme
Clostridioides difficile
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
assay at
Clostridioides difficile
8
-
assay at
Ferroplasma acidarmanus
8
-
assay at
Haloarcula japonica
8
-
assay at
Thermococcus litoralis
IC50 Value
IC50 Value
IC50 Value Maximum
Commentary
Organism
Inhibitor
Structure
0.217
-
pH 8.0, 50C
Thermococcus litoralis
pyrrole-2-carboxylate
0.269
-
pH 8.0, 50C
Clostridioides difficile
pyrrole-2-carboxylate
0.295
-
pH 8.0, 50C
Haloarcula japonica
pyrrole-2-carboxylate
0.58
-
pH 8.0, 50C
Ferroplasma acidarmanus
pyrrole-2-carboxylate
Cloned(Commentary) (protein specific)
Commentary
Organism
expression in Escherichia coli
Clostridioides difficile
expression in Escherichia coli
Ferroplasma acidarmanus
expression in Escherichia coli
Haloarcula japonica
expression in Escherichia coli
Thermococcus litoralis
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
R240W
mutant enzyme shows similar kinetic constants for proline and hydroxyproline as compared to the wild-type enzyme
Ferroplasma acidarmanus
W241F the mutant enzyme
shows 5.3fold, 430fold, and 5.8fold lower kcat/Km values for trans-4-hydroxy-L-proline, trans-3-hydroxy-L-proline, and cis-4-hydroxy-D-proline respectively, mainly due to a marked decrease in kcat values, whereas no significant effects are found in the kinetic constants of proline, suggesting that this (hydrophobic and bulky) tryptophan residue plays an importance role in the recognition of hydroxyproline (more hydrophilic and bulky than proline)
Thermococcus litoralis
IC50 Value (protein specific)
IC50 Value
IC50 Value Maximum
Commentary
Organism
Inhibitor
Structure
0.217
-
pH 8.0, 50C
Thermococcus litoralis
pyrrole-2-carboxylate
0.269
-
pH 8.0, 50C
Clostridioides difficile
pyrrole-2-carboxylate
0.295
-
pH 8.0, 50C
Haloarcula japonica
pyrrole-2-carboxylate
0.58
-
pH 8.0, 50C
Ferroplasma acidarmanus
pyrrole-2-carboxylate
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
pyrrole-2-carboxylate
-
Clostridioides difficile
pyrrole-2-carboxylate
-
Ferroplasma acidarmanus
pyrrole-2-carboxylate
-
Haloarcula japonica
pyrrole-2-carboxylate
-
Thermococcus litoralis
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.092
-
D-proline
pH 8.0, 50C, wild-type enzyme
Thermococcus litoralis
0.156
-
D-proline
pH 8.0, 50C, mutant enzyme F62V
Thermococcus litoralis
0.194
-
D-proline
pH 8.0, 50C, mutant enzyme W241F
Thermococcus litoralis
0.612
-
D-proline
pH 8.0, 50C, wild-type enzyme
Clostridioides difficile
1.17
-
D-proline
pH 8.0, 50C, wild-type enzyme
Ferroplasma acidarmanus
1.21
-
L-proline
pH 8.0, 50C, wild-type enzyme
Thermococcus litoralis
1.29
-
L-proline
pH 8.0, 50C, mutant enzyme W241F
Thermococcus litoralis
1.93
-
L-proline
pH 8.0, 50C, mutant enzyme F62V
Thermococcus litoralis
2.54
-
D-proline
pH 8.0, 50C, mutant enzyme L221H
Thermococcus litoralis
4
-
D-proline
pH 8.0, 50C, mutant enzyme F62S
Thermococcus litoralis
8.53
-
L-proline
pH 8.0, 50C, wild-type enzyme
Clostridioides difficile
20.5
-
L-proline
pH 8.0, 50C, mutant enzyme L221H
Thermococcus litoralis
31.6
-
L-proline
pH 8.0, 50C, wild-type enzyme
Ferroplasma acidarmanus
53
-
L-proline
pH 8.0, 50C, mutant enzyme F240W
Ferroplasma acidarmanus
154
-
L-proline
pH 8.0, 50C, mutant enzyme F62S
Thermococcus litoralis
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
40000
-
x * 40000, SDS-PAGE
Clostridioides difficile
40000
-
x * 40000, SDS-PAGE
Ferroplasma acidarmanus
40000
-
x * 40000, SDS-PAGE
Thermococcus litoralis
42000
-
x * 42000, SDS-PAGE
Haloarcula japonica
80000
-
gel filtration
Clostridioides difficile
80000
-
gel filtration
Ferroplasma acidarmanus
80000
-
gel filtration
Haloarcula japonica
80000
-
gel filtration
Thermococcus litoralis
Purification (Commentary) (protein specific)
Commentary
Organism
-
Clostridioides difficile
-
Ferroplasma acidarmanus
-
Haloarcula japonica
-
Thermococcus litoralis
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-proline
the reaction is completely bi-directional, and the reverse reactions. The specific activity with D-proline is 130% compared to the L-enantiomer. The bifunctional enzyme reversibly catalyzes the racemization of proline and the epimerization of 4-hydroxyproline and 3-hydroxyproline with similar kinetic constants. Catalysis is based on the same 1,1-proton transfer mechanism using two general acidic/basic cysteine residues located on opposite faces of the active site
730678
Thermococcus litoralis
L-proline
-
-
-
?
D-proline
the reaction is completely bi-directional, and the reverse reactions. The specific activity with D-proline is 130% compared to the L-enantiomer. The bifunctional enzyme reversibly catalyzes the racemization of proline and the epimerization of 4-hydroxyproline and 3-hydroxyproline with similar kinetic constants. Catalysis is based on the same 1,1-proton transfer mechanism using two general acidic/basic cysteine residues located on opposite faces of the active site
730678
Thermococcus litoralis DSM 5473
L-proline
-
-
-
?
L-azetidine-2-carboxylate
low activity
730678
Thermococcus litoralis
D-azetidine-2-carboxylate
-
-
-
?
L-azetidine-2-carboxylate
low activity
730678
Thermococcus litoralis DSM 5473
D-azetidine-2-carboxylate
-
-
-
?
L-pipecolate
low activity
730678
Thermococcus litoralis
D-pipecolate
-
-
-
?
L-pipecolate
low activity
730678
Thermococcus litoralis DSM 5473
D-pipecolate
-
-
-
?
L-proline
-
730678
Clostridioides difficile
D-proline
-
-
-
r
L-proline
kcat/Km value for trans-4-hydroxy-L-proline is about 3fold lower than that for L-proline, which is attributed to a 17fold lower kcat value. The kinetic parameters of the epimerization of cis-4-hydroxy-D-proline can not be determined
730678
Ferroplasma acidarmanus
D-proline
-
-
-
r
L-proline
the enzyme can utilize both proline and hydroxyprolines as substrate
730678
Haloarcula japonica
D-proline
-
-
-
r
L-proline
the reaction is completely bi-directional, and the reverse reactions. The specific activity with D-proline is 130% compared to the L-enantiomer. The bifunctional enzyme reversibly catalyzes the racemization of proline and the epimerization of 4-hydroxyproline and 3-hydroxyproline with similar kinetic constants. Catalysis is based on the same 1,1-proton transfer mechanism using two general acidic/basic cysteine residues located on opposite faces of the active site
730678
Thermococcus litoralis
D-proline
-
-
-
r
L-proline
the reaction is completely bi-directional, and the reverse reactions. The specific activity with D-proline is 130% compared to the L-enantiomer. The bifunctional enzyme reversibly catalyzes the racemization of proline and the epimerization of 4-hydroxyproline and 3-hydroxyproline with similar kinetic constants. Catalysis is based on the same 1,1-proton transfer mechanism using two general acidic/basic cysteine residues located on opposite faces of the active site
730678
Thermococcus litoralis DSM 5473
D-proline
-
-
-
r
L-proline
the enzyme can utilize both proline and hydroxyprolines as substrate
730678
Haloarcula japonica DSM 6131
D-proline
-
-
-
r
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 40000, SDS-PAGE
Clostridioides difficile
?
x * 40000, SDS-PAGE
Ferroplasma acidarmanus
?
x * 42000, SDS-PAGE
Haloarcula japonica
?
x * 40000, SDS-PAGE
Thermococcus litoralis
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
50
-
assay at
Clostridioides difficile
50
-
assay at
Ferroplasma acidarmanus
50
-
assay at
Haloarcula japonica
50
-
assay at
Thermococcus litoralis
90
100
-
Clostridioides difficile
90
100
-
Ferroplasma acidarmanus
90
100
-
Haloarcula japonica
90
100
-
Thermococcus litoralis
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.0235
-
D-proline
pH 8.0, 50C, mutant enzyme F62V
Thermococcus litoralis
0.026
-
D-proline
pH 8.0, 50C, mutant enzyme F62S
Thermococcus litoralis
0.092
-
L-proline
pH 8.0, 50C, mutant enzyme F62V
Thermococcus litoralis
0.119
-
D-proline
pH 8.0, 50C, wild-type enzyme
Ferroplasma acidarmanus
0.2
-
L-proline
pH 8.0, 50C, mutant enzyme F62S
Thermococcus litoralis
0.29
-
D-proline
pH 8.0, 50C, mutant enzyme L221H
Thermococcus litoralis
0.42
-
L-proline
pH 8.0, 50C, mutant enzyme F240W
Ferroplasma acidarmanus
0.6
-
L-proline
pH 8.0, 50C, wild-type enzyme
Ferroplasma acidarmanus
0.92
-
L-proline
pH 8.0, 50C, mutant enzyme L221H
Thermococcus litoralis
2.22
-
D-proline
pH 8.0, 50C, wild-type enzyme
Thermococcus litoralis
2.48
-
D-proline
pH 8.0, 50C, wild-type enzyme
Clostridioides difficile
2.78
-
L-proline
pH 8.0, 50C, wild-type enzyme
Thermococcus litoralis
3.17
-
L-proline
pH 8.0, 50C, mutant enzyme W241F
Thermococcus litoralis
3.18
-
D-proline
pH 8.0, 50C, mutant enzyme W241F
Thermococcus litoralis
14.15
-
L-proline
pH 8.0, 50C, wild-type enzyme
Clostridioides difficile
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
assay at
Clostridioides difficile
8
-
assay at
Ferroplasma acidarmanus
8
-
assay at
Haloarcula japonica
8
-
assay at
Thermococcus litoralis
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.0013
-
L-proline
pH 8.0, 50C, mutant enzyme F62S
Thermococcus litoralis
0.0065
-
D-proline
pH 8.0, 50C, mutant enzyme F62S
Thermococcus litoralis
0.0079
-
L-proline
pH 8.0, 50C, mutant enzyme F240W
Ferroplasma acidarmanus
0.019
-
L-proline
pH 8.0, 50C, wild-type enzyme
Ferroplasma acidarmanus
0.045
-
L-proline
pH 8.0, 50C, mutant enzyme L221H
Thermococcus litoralis
0.048
-
L-proline
pH 8.0, 50C, mutant enzyme F62V
Thermococcus litoralis
0.1
-
D-proline
pH 8.0, 50C, wild-type enzyme
Ferroplasma acidarmanus
0.11
-
D-proline
pH 8.0, 50C, mutant enzyme L221H
Thermococcus litoralis
0.15
-
D-proline
pH 8.0, 50C, mutant enzyme F62V
Thermococcus litoralis
1.65
-
L-proline
pH 8.0, 50C, wild-type enzyme
Clostridioides difficile
2.3
-
L-proline
pH 8.0, 50C, wild-type enzyme
Thermococcus litoralis
2.45
-
L-proline
pH 8.0, 50C, mutant enzyme W241F
Thermococcus litoralis
4.08
-
D-proline
pH 8.0, 50C, wild-type enzyme
Clostridioides difficile
16.5
-
D-proline
pH 8.0, 50C, mutant enzyme W241F
Thermococcus litoralis
26.2
-
D-proline
pH 8.0, 50C, wild-type enzyme
Thermococcus litoralis
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.0013
-
L-proline
pH 8.0, 50C, mutant enzyme F62S
Thermococcus litoralis
0.0065
-
D-proline
pH 8.0, 50C, mutant enzyme F62S
Thermococcus litoralis
0.0079
-
L-proline
pH 8.0, 50C, mutant enzyme F240W
Ferroplasma acidarmanus
0.019
-
L-proline
pH 8.0, 50C, wild-type enzyme
Ferroplasma acidarmanus
0.045
-
L-proline
pH 8.0, 50C, mutant enzyme L221H
Thermococcus litoralis
0.048
-
L-proline
pH 8.0, 50C, mutant enzyme F62V
Thermococcus litoralis
0.1
-
D-proline
pH 8.0, 50C, wild-type enzyme
Ferroplasma acidarmanus
0.11
-
D-proline
pH 8.0, 50C, mutant enzyme L221H
Thermococcus litoralis
0.15
-
D-proline
pH 8.0, 50C, mutant enzyme F62V
Thermococcus litoralis
1.65
-
L-proline
pH 8.0, 50C, wild-type enzyme
Clostridioides difficile
2.3
-
L-proline
pH 8.0, 50C, wild-type enzyme
Thermococcus litoralis
2.45
-
L-proline
pH 8.0, 50C, mutant enzyme W241F
Thermococcus litoralis
4.08
-
D-proline
pH 8.0, 50C, wild-type enzyme
Clostridioides difficile
16.5
-
D-proline
pH 8.0, 50C, mutant enzyme W241F
Thermococcus litoralis
26.2
-
D-proline
pH 8.0, 50C, wild-type enzyme
Thermococcus litoralis
Other publictions for EC 5.1.1.4
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)
730678
Watanabe
Identification and characteriz ...
Clostridioides difficile, Ferroplasma acidarmanus, Haloarcula japonica, Haloarcula japonica DSM 6131, Thermococcus litoralis, Thermococcus litoralis DSM 5473
PLoS One
10
e0120349
2015
-
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4
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2
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4
15
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8
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12
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4
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12
4
8
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15
4
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4
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4
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2
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4
4
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15
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8
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4
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12
4
8
-
-
15
4
-
-
-
-
-
-
-
15
15
748829
Caballero
Phylogenetic and syntenic dat ...
no activity in Trypanosoma brucei, no activity in Trypanosoma congolense, Trypanosoma conorhini, Trypanosoma conorhini TCC025, Trypanosoma cruzi, Trypanosoma cruzi CL Brener, Trypanosoma cruzi marinkellei, Trypanosoma cruzi marinkellei TCC344, Trypanosoma dionisii, Trypanosoma dionisii TCC211, Trypanosoma erneyi, Trypanosoma erneyi TCC1946, Trypanosoma grayi, Trypanosoma grayi ANR4, Trypanosoma lewisi, Trypanosoma lewisi TCC034, Trypanosoma rangeli, Trypanosoma serpentis, Trypanosoma serpentis TCC1052, Trypanosoma sp., Trypanosoma sp. TCC1825 / RCF-2014, Trypanosoma sp. TCC339, Trypanosoma sp. TCC878, Trypanosoma sp. TCC878 RCF-2014, Trypanosoma vivax, Trypanosoma vivax Y486
Parasit. Vectors
8
222
2015
-
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13
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47
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14
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13
14
-
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727156
Harty
Inhibition of serine and proli ...
Acetoanaerobium sticklandii
Bioorg. Med. Chem. Lett.
24
390-393
2014
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1
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4
1
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1
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3
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1
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1
1
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4
1
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2
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1
1
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-
727265
Wu
The Clostridium difficile prol ...
Clostridioides difficile
Can. J. Microbiol.
60
251-254
2014
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3
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1
1
-
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-
749144
Fikru
A proline racemase based PCR ...
Trypanosoma vivax, Trypanosoma vivax ILRAD 1392
PLoS ONE
9
e84819
2014
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1
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1
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15
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2
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-
728600
Berneman
Combined approaches for drug d ...
Trypanosoma cruzi
PLoS ONE
8
e60955
2013
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1
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9
-
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1
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4
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1
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1
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1
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1
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6
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1
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9
6
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1
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1
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1
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
715163
Bryan
Genetic immunization converts ...
Trypanosoma cruzi, Trypanosoma cruzi Y
Infect. Immun.
78
810-822
2010
-
-
1
-
-
-
-
-
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1
-
-
12
-
-
1
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1
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1
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1
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1
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1
-
1
-
-
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1
-
-
-
-
-
-
-
-
-
1
1
-
-
-
704196
Rubinstein
Catalyzing racemizations in th ...
Trypanosoma cruzi
J. Am. Chem. Soc.
131
8513-8521
2009
-
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1
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1
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1
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1
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1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
704292
Fonknechten
A conserved gene cluster rules ...
Acetoanaerobium sticklandii
J. Bacteriol.
191
3162-3167
2009
-
-
-
-
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1
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1
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1
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1
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-
1
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-
-
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-
-
-
1
1
-
-
-
705499
Coutinho
Inhibition of Trypanosoma cruz ...
Trypanosoma cruzi
Mem. Inst. Oswaldo Cruz
104
1055-1062
2009
-
-
-
-
-
-
1
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1
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1
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3
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3
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1
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1
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3
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1
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-
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2
1
1
2
-
-
705500
Coatnoan
Proline racemases: Insights in ...
Trypanosoma cruzi
Mem. Inst. Oswaldo Cruz
104
295-300
2009
-
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1
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2
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3
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1
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2
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2
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4
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2
2
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-
-
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-
1
1
2
2
-
-
705596
Chamond
Proline racemases are conserve ...
Trypanosoma vivax
Mol. Biochem. Parasitol.
165
170-179
2009
-
1
1
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1
2
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1
1
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7
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1
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3
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1
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1
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1
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1
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1
1
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1
1
2
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1
1
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1
-
3
-
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1
-
1
-
-
-
1
-
-
-
-
1
1
-
-
-
675621
Stenta
The Catalytic Activity of Prol ...
Trypanosoma cruzi
J. Phys. Chem. B
112
1057-1059
2008
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2
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676749
Goytia
Molecular and structural discr ...
Clostridioides difficile, Clostridioides difficile VPI10463
PLoS ONE
2
e885
2007
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1
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2
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1
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1
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1
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1
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2
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2
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
676832
Buschiazzo
Crystal structure, catalytic m ...
Trypanosoma cruzi
Proc. Natl. Acad. Sci. USA
103
1705-1710
2006
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1
1
2
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1
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1
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1
1
1
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1
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1
2
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1
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1
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-
-
-
1
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
662908
Chamond
Trypanosoma cruzi proline race ...
Trypanosoma cruzi
Mol. Microbiol.
58
46-60
2005
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2
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1
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652377
Chamond
Biochemical characterization o ...
Trypanosoma cruzi
J. Biol. Chem.
278
15484-15494
2003
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3
1
1
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1
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2
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1
2
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1
1
1
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1
2
2
3
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3
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5
3
1
1
-
1
-
2
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-
-
-
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653295
Reina-San-Martin
A B-cell mitogen from a pathog ...
Trypanosoma cruzi
Nat. Med.
6
890-897
2000
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1
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4
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1
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1
1
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3
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1
1
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1
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1
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1
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4
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1
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1
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1
1
1
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1
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1
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-
-
-
2125
Fisher
Energetics of proline racemase ...
Acetoanaerobium sticklandii
Biochemistry
25
2529-2537
1986
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1
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1
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1
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1
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1
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2126
Fisher
Energetics of proline racemase ...
Acetoanaerobium sticklandii
Biochemistry
25
2543-2551
1986
-
-
-
-
-
-
-
-
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1
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1
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1
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1
-
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-
-
-
-
-
-
-
-
2127
Belasco
Energetics of proline racemase ...
Acetoanaerobium sticklandii
Biochemistry
25
2564-2571
1986
-
-
-
-
-
-
-
-
-
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1
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1
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1
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1
-
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-
-
-
-
-
-
-
-
-
-
-
2128
Fisher
Energetics of proline racemase ...
Acetoanaerobium sticklandii
Biochemistry
25
2538-2542
1986
-
-
-
-
-
-
-
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1
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1
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1
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-
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1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2129
Belasco
Energetics of proline racemase ...
Acetoanaerobium sticklandii
Biochemistry
25
2558-2564
1986
-
-
-
-
-
-
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1
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1
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1
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1
-
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-
-
-
-
-
-
-
-
-
-
-
2130
Albery
Energetics and mechanism of pr ...
Acetoanaerobium sticklandii
Biochemistry
25
2572-2577
1986
-
-
-
-
-
-
-
-
-
-
-
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1
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1
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1
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-
-
-
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-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2131
Belasco
Energetics of proline racemase ...
Acetoanaerobium sticklandii
Biochemistry
25
2552-2558
1986
-
-
-
-
-
-
-
-
-
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-
-
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1
-
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1
-
-
-
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1
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-
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1
-
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-
-
-
-
-
-
-
-
-
-
-
2124
Rudnick
Reaction mechanism and structu ...
Acetoanaerobium sticklandii
Biochemistry
14
4515-4522
1975
-
-
-
-
-
-
3
-
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1
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2
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1
1
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1
1
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3
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1
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1
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1
1
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2123
Keenan
The inhibition of proline race ...
Acetoanaerobium sticklandii
Biochem. Biophys. Res. Commun.
57
500-504
1974
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1
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1
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1
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1
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1
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2122
Cardinale
Purification and mechanism of ...
Acetoanaerobium sticklandii
Biochemistry
7
3970-3978
1968
3
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18
2
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1
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1
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1
1
1
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1
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3
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18
-
2
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1
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1
1
1
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1
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2121
Stadtman
Studies on the enzymic reducti ...
Acetoanaerobium sticklandii
J. Biol. Chem.
228
983-997
1957
3
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3
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1
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3
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1
1
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1
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3
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3
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1
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1
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1
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1
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1
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1
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