Comparative analysis of the catalytic components in the archaeal dye-linked L-proline dehydrogenase complexes
Kawakami, R.; Noguchi, C.; Higashi, M.; Sakuraba, H.; Ohshima, T.; Appl. Microbiol. Biotechnol. 97, 3419-3427 (2013) 
Data extracted from this reference:
Cloned(Commentary)
Cloned (Commentary)
Organism
sequence comparisons and phylogenetic analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21-CodonPlus(DE3)-RIPL
Thermococcus profundus
sequence comparisons and phylogenetic analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21-CodonPlus(DE3)-RIPL
Pyrococcus horikoshii
sequence comparisons and phylogenetic analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21-CodonPlus(DE3)-RIPL
Pyrococcus furiosus
sequence comparisons and phylogenetic analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21-CodonPlus(DE3)-RIPL
Thermococcus kodakarensis
Inhibitors
Inhibitors
Commentary
Organism
Structure
L-proline
substrate inhibition at high L-proline concentrations; substrate inhibition at high L-proline concentrations
Pyrococcus furiosus
L-proline
substrate inhibition at high L-proline concentrations; substrate inhibition at high L-proline concentrations
Pyrococcus horikoshii
L-proline
substrate inhibition at high L-proline concentrations; substrate inhibition at high L-proline concentrations
Thermococcus kodakarensis
L-proline
substrate inhibition at high L-proline concentrations
Thermococcus profundus
pyrrolidone-5-carboxylate
-
Pyrococcus furiosus
pyrrolidone-5-carboxylate
-
Pyrococcus horikoshii
pyrrolidone-5-carboxylate
-
Thermococcus kodakarensis
pyrrolidone-5-carboxylate
-
Thermococcus profundus
Organism
Organism
UniProt
Commentary
Textmining
Pyrococcus furiosus
Q8U022
-
-
Pyrococcus furiosus
Q8U1G2
-
-
Pyrococcus horikoshii
O59089
-
-
Pyrococcus horikoshii
O59445
-
-
Pyrococcus horikoshii OT-3
O59089
-
-
Pyrococcus horikoshii OT-3
O59445
-
-
Thermococcus kodakarensis
Q5JFG2
-
-
Thermococcus kodakarensis
Q5JFG7
-
-
Thermococcus kodakarensis KOD1 JCM12380
Q5JFG7
-
-
Thermococcus profundus
Q76M73
-
-
Thermococcus profundus DSM 9503
Q76M73
-
-
Purification (Commentary)
Purification (Commentary)
Organism
recombinant His-tagged enzyme from Escherichia coli strain BL21-CodonPlus(DE3)-RIPL by nickel affinity chromatography and dialysis to homogeneity
Thermococcus profundus
recombinant His-tagged enzyme from Escherichia coli strain BL21-CodonPlus(DE3)-RIPL by nickel affinity chromatography and dialysis to homogeneity
Pyrococcus furiosus
recombinant His-tagged enzyme from Escherichia coli strain BL21-CodonPlus(DE3)-RIPL by nickel affinity chromatography and dialysis to homogeneity
Thermococcus kodakarensis
recombinant His-tagged enzyme from Escherichia coli strain BL21-CodonPlus(DE3)-RIPL by nickel affinity chromatography and dialysis to homogeneity, the PH1751 protein tends to aggregate during dialysis
Pyrococcus horikoshii
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
L-proline + 2,6-dichlorphenol-indophenol
-
741732
Thermococcus profundus
(S)-1-pyrroline-5-carboxylate + reduced 2,6-dichlorphenol-indophenol
-
-
-
?
L-proline + 2,6-dichlorphenol-indophenol
-
741732
Pyrococcus horikoshii
(S)-1-pyrroline-5-carboxylate + reduced 2,6-dichlorphenol-indophenol
-
-
-
?
L-proline + 2,6-dichlorphenol-indophenol
-
741732
Pyrococcus furiosus
(S)-1-pyrroline-5-carboxylate + reduced 2,6-dichlorphenol-indophenol
-
-
-
?
L-proline + 2,6-dichlorphenol-indophenol
-
741732
Thermococcus kodakarensis
(S)-1-pyrroline-5-carboxylate + reduced 2,6-dichlorphenol-indophenol
-
-
-
?
L-proline + 2,6-dichlorphenol-indophenol
-
741732
Thermococcus kodakarensis KOD1 JCM12380
(S)-1-pyrroline-5-carboxylate + reduced 2,6-dichlorphenol-indophenol
-
-
-
?
L-proline + 2,6-dichlorphenol-indophenol
-
741732
Thermococcus profundus DSM 9503
(S)-1-pyrroline-5-carboxylate + reduced 2,6-dichlorphenol-indophenol
-
-
-
?
L-proline + 2,6-dichlorphenol-indophenol
-
741732
Pyrococcus horikoshii OT-3
(S)-1-pyrroline-5-carboxylate + reduced 2,6-dichlorphenol-indophenol
-
-
-
?
additional information
no activity with D-proline, L-hydroxyproline, pyrrolidone-5-carboxylate, sarcosine, and glycine
741732
Thermococcus profundus
?
-
-
-
?
additional information
no activity with D-proline, L-hydroxyproline, pyrrolidone-5-carboxylate, sarcosine, and glycine
741732
Pyrococcus horikoshii
?
-
-
-
?
additional information
no activity with D-proline, L-hydroxyproline, pyrrolidone-5-carboxylate, sarcosine, and glycine
741732
Pyrococcus furiosus
?
-
-
-
?
additional information
no activity with D-proline, L-hydroxyproline, pyrrolidone-5-carboxylate, sarcosine, and glycine
741732
Thermococcus kodakarensis
?
-
-
-
?
additional information
no activity with D-proline, L-hydroxyproline, pyrrolidone-5-carboxylate, sarcosine, and glycine
741732
Thermococcus kodakarensis KOD1 JCM12380
?
-
-
-
?
additional information
no activity with D-proline, L-hydroxyproline, pyrrolidone-5-carboxylate, sarcosine, and glycine
741732
Thermococcus profundus DSM 9503
?
-
-
-
?
additional information
no activity with D-proline, L-hydroxyproline, pyrrolidone-5-carboxylate, sarcosine, and glycine
741732
Pyrococcus horikoshii OT-3
?
-
-
-
?
Subunits
Subunits
Commentary
Organism
octamer
the enzyme is a alpha4beta4-type ProDH
Pyrococcus horikoshii
octamer
the enzyme is a alpha4beta4-type ProDH
Pyrococcus furiosus
octamer
the enzyme is a alpha4beta4-type ProDH
Thermococcus kodakarensis
tetramer
the enzyme is a alphabetagammadelta-type ProDH
Thermococcus profundus
tetramer
the enzyme is a alphabetagammadelta-type ProDH
Thermococcus kodakarensis
tetramer
the enzyme is a alphabetagammadelta-type ProDH
Pyrococcus horikoshii
tetramer
the enzyme is a alphabetagammadelta-type ProDH
Pyrococcus furiosus
Synonyms
Synonyms
Commentary
Organism
L-proline dehydrogenase
-
Thermococcus profundus
L-proline dehydrogenase
-
Pyrococcus horikoshii
L-proline dehydrogenase
-
Pyrococcus furiosus
L-proline dehydrogenase
-
Thermococcus kodakarensis
PdhB
-
Thermococcus profundus
PdhB
-
Thermococcus kodakarensis
PDHbeta
-
Pyrococcus horikoshii
PDHbeta
-
Pyrococcus furiosus
PDHbeta
-
Thermococcus kodakarensis
PF1246
-
Pyrococcus furiosus
PF1798
-
Pyrococcus furiosus
PH1364
-
Pyrococcus horikoshii
PH1751
-
Pyrococcus horikoshii
proDH-B1
-
Pyrococcus horikoshii
proDH-B2
-
Pyrococcus horikoshii
TK0117
-
Thermococcus kodakarensis
TK0122
-
Thermococcus kodakarensis
TPpdhbeta
-
Thermococcus profundus
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
50
-
assay at
Thermococcus profundus
50
-
assay at
Pyrococcus horikoshii
50
-
assay at
Pyrococcus furiosus
50
-
assay at
Thermococcus kodakarensis
Temperature Stability [°C]
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
70
-
the alpha4beta4-type PDHbeta retains more than 80% of its activity after heating at 70°C for 20 min
Pyrococcus horikoshii
70
-
the alpha4beta4-type PDHbeta retains more than 80% of its activity after heating at 70°C for 20 min
Pyrococcus furiosus
70
-
the alpha4beta4-type PDHbeta retains more than 80% of its activity after heating at 70°C for 20 min
Thermococcus kodakarensis
70
-
the alphabetagammadelta-type PDHbeta nearly loses all of its activity during incubation at 70°C for 20 min
Pyrococcus horikoshii
70
-
the alphabetagammadelta-type PDHbeta retains 100% of activity during incubation at 70°C for 20 min
Pyrococcus furiosus
70
-
the alphabetagammadelta-type PDHbeta retains 68% of activity during incubation at 70°C for 20 min
Thermococcus profundus
70
-
the alphabetagammadelta-type PDHbeta retains 76% of activity during incubation at 70°C for 20 min
Thermococcus kodakarensis
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
assay at
Thermococcus profundus
8
-
assay at
Pyrococcus horikoshii
8
-
assay at
Pyrococcus furiosus
8
-
assay at
Thermococcus kodakarensis
Cofactor
Cofactor
Commentary
Organism
Structure
FAD
non-covalent binding
Thermococcus profundus
FAD
non-covalent binding
Pyrococcus horikoshii
FAD
non-covalent binding
Pyrococcus furiosus
FAD
non-covalent binding
Thermococcus kodakarensis
Cloned(Commentary) (protein specific)
Commentary
Organism
sequence comparisons and phylogenetic analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21-CodonPlus(DE3)-RIPL
Thermococcus profundus
sequence comparisons and phylogenetic analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21-CodonPlus(DE3)-RIPL
Pyrococcus horikoshii
sequence comparisons and phylogenetic analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21-CodonPlus(DE3)-RIPL
Pyrococcus furiosus
sequence comparisons and phylogenetic analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21-CodonPlus(DE3)-RIPL
Thermococcus kodakarensis
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
FAD
non-covalent binding
Thermococcus profundus
FAD
non-covalent binding
Pyrococcus horikoshii
FAD
non-covalent binding
Pyrococcus furiosus
FAD
non-covalent binding
Thermococcus kodakarensis
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
L-proline
substrate inhibition at high L-proline concentrations
Thermococcus profundus
L-proline
substrate inhibition at high L-proline concentrations
Pyrococcus horikoshii
L-proline
substrate inhibition at high L-proline concentrations
Pyrococcus furiosus
L-proline
substrate inhibition at high L-proline concentrations
Thermococcus kodakarensis
pyrrolidone-5-carboxylate
-
Thermococcus profundus
pyrrolidone-5-carboxylate
-
Pyrococcus horikoshii
pyrrolidone-5-carboxylate
-
Pyrococcus furiosus
pyrrolidone-5-carboxylate
-
Thermococcus kodakarensis
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant His-tagged enzyme from Escherichia coli strain BL21-CodonPlus(DE3)-RIPL by nickel affinity chromatography and dialysis to homogeneity
Thermococcus profundus
recombinant His-tagged enzyme from Escherichia coli strain BL21-CodonPlus(DE3)-RIPL by nickel affinity chromatography and dialysis to homogeneity
Pyrococcus furiosus
recombinant His-tagged enzyme from Escherichia coli strain BL21-CodonPlus(DE3)-RIPL by nickel affinity chromatography and dialysis to homogeneity
Thermococcus kodakarensis
recombinant His-tagged enzyme from Escherichia coli strain BL21-CodonPlus(DE3)-RIPL by nickel affinity chromatography and dialysis to homogeneity, the PH1751 protein tends to aggregate during dialysis
Pyrococcus horikoshii
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
L-proline + 2,6-dichlorphenol-indophenol
-
741732
Thermococcus profundus
(S)-1-pyrroline-5-carboxylate + reduced 2,6-dichlorphenol-indophenol
-
-
-
?
L-proline + 2,6-dichlorphenol-indophenol
-
741732
Pyrococcus horikoshii
(S)-1-pyrroline-5-carboxylate + reduced 2,6-dichlorphenol-indophenol
-
-
-
?
L-proline + 2,6-dichlorphenol-indophenol
-
741732
Pyrococcus furiosus
(S)-1-pyrroline-5-carboxylate + reduced 2,6-dichlorphenol-indophenol
-
-
-
?
L-proline + 2,6-dichlorphenol-indophenol
-
741732
Thermococcus kodakarensis
(S)-1-pyrroline-5-carboxylate + reduced 2,6-dichlorphenol-indophenol
-
-
-
?
L-proline + 2,6-dichlorphenol-indophenol
-
741732
Thermococcus kodakarensis KOD1 JCM12380
(S)-1-pyrroline-5-carboxylate + reduced 2,6-dichlorphenol-indophenol
-
-
-
?
L-proline + 2,6-dichlorphenol-indophenol
-
741732
Thermococcus profundus DSM 9503
(S)-1-pyrroline-5-carboxylate + reduced 2,6-dichlorphenol-indophenol
-
-
-
?
L-proline + 2,6-dichlorphenol-indophenol
-
741732
Pyrococcus horikoshii OT-3
(S)-1-pyrroline-5-carboxylate + reduced 2,6-dichlorphenol-indophenol
-
-
-
?
additional information
no activity with D-proline, L-hydroxyproline, pyrrolidone-5-carboxylate, sarcosine, and glycine
741732
Thermococcus profundus
?
-
-
-
?
additional information
no activity with D-proline, L-hydroxyproline, pyrrolidone-5-carboxylate, sarcosine, and glycine
741732
Pyrococcus horikoshii
?
-
-
-
?
additional information
no activity with D-proline, L-hydroxyproline, pyrrolidone-5-carboxylate, sarcosine, and glycine
741732
Pyrococcus furiosus
?
-
-
-
?
additional information
no activity with D-proline, L-hydroxyproline, pyrrolidone-5-carboxylate, sarcosine, and glycine
741732
Thermococcus kodakarensis
?
-
-
-
?
additional information
no activity with D-proline, L-hydroxyproline, pyrrolidone-5-carboxylate, sarcosine, and glycine
741732
Thermococcus kodakarensis KOD1 JCM12380
?
-
-
-
?
additional information
no activity with D-proline, L-hydroxyproline, pyrrolidone-5-carboxylate, sarcosine, and glycine
741732
Thermococcus profundus DSM 9503
?
-
-
-
?
additional information
no activity with D-proline, L-hydroxyproline, pyrrolidone-5-carboxylate, sarcosine, and glycine
741732
Pyrococcus horikoshii OT-3
?
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
octamer
the enzyme is a alpha4beta4-type ProDH
Pyrococcus horikoshii
octamer
the enzyme is a alpha4beta4-type ProDH
Pyrococcus furiosus
octamer
the enzyme is a alpha4beta4-type ProDH
Thermococcus kodakarensis
tetramer
the enzyme is a alphabetagammadelta-type ProDH
Thermococcus profundus
tetramer
the enzyme is a alphabetagammadelta-type ProDH
Thermococcus kodakarensis
tetramer
the enzyme is a alphabetagammadelta-type ProDH
Pyrococcus horikoshii
tetramer
the enzyme is a alphabetagammadelta-type ProDH
Pyrococcus furiosus
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
50
-
assay at
Thermococcus profundus
50
-
assay at
Pyrococcus horikoshii
50
-
assay at
Pyrococcus furiosus
50
-
assay at
Thermococcus kodakarensis
Temperature Stability [°C] (protein specific)
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
70
-
the alpha4beta4-type PDHbeta retains more than 80% of its activity after heating at 70°C for 20 min
Pyrococcus horikoshii
70
-
the alpha4beta4-type PDHbeta retains more than 80% of its activity after heating at 70°C for 20 min
Pyrococcus furiosus
70
-
the alpha4beta4-type PDHbeta retains more than 80% of its activity after heating at 70°C for 20 min
Thermococcus kodakarensis
70
-
the alphabetagammadelta-type PDHbeta nearly loses all of its activity during incubation at 70°C for 20 min
Pyrococcus horikoshii
70
-
the alphabetagammadelta-type PDHbeta retains 100% of activity during incubation at 70°C for 20 min
Pyrococcus furiosus
70
-
the alphabetagammadelta-type PDHbeta retains 68% of activity during incubation at 70°C for 20 min
Thermococcus profundus
70
-
the alphabetagammadelta-type PDHbeta retains 76% of activity during incubation at 70°C for 20 min
Thermococcus kodakarensis
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
assay at
Thermococcus profundus
8
-
assay at
Pyrococcus horikoshii
8
-
assay at
Pyrococcus furiosus
8
-
assay at
Thermococcus kodakarensis
General Information
General Information
Commentary
Organism
evolution
nearly all of the residues responsible for the interaction with substrate and FAD are highly conserved in Pyrococcus and Thermococcus. Phylogenetic analysis shows that the divergence of the alphabetagammadelta-type PDHbetas is spread wider than that of alpha4beta4-type PDHbetas
Thermococcus profundus
evolution
nearly all of the residues responsible for the interaction with substrate and FAD are highly conserved in Pyrococcus and Thermococcus. Phylogenetic analysis shows that the divergence of the alphabetagammadelta-type PDHbetas is spread wider than that of alpha4beta4-type PDHbetas
Pyrococcus horikoshii
evolution
nearly all of the residues responsible for the interaction with substrate and FAD are highly conserved in Pyrococcus and Thermococcus. Phylogenetic analysis shows that the divergence of the alphabetagammadelta-type PDHbetas is spread wider than that of alpha4beta4-type PDHbetas
Pyrococcus furiosus
evolution
nearly all of the residues responsible for the interaction with substrate and FAD are highly conserved in Pyrococcus and Thermococcus. Phylogenetic analysis shows that the divergence of the alphabetagammadelta-type PDHbetas is spread wider than that of alpha4beta4-type PDHbetas
Thermococcus kodakarensis
additional information
values for kcat, Km, and Ki values for L-proline and Ki' for pyrrolidone-5-carboxylate differ greatly among the PDHbeta enzymes, which is in contrast to the optimal temperature and thermostability, and indicates that the kinetic parameters of the PDHbetas are not a reflection of whether the protein is a subunit of an alphabetagammadelta-type PDHbeta or alpha4beta4-type PDHbeta ProDH complex
Thermococcus profundus
additional information
values for kcat, Km, and Ki values for L-proline and Ki' for pyrrolidone-5-carboxylate differ greatly among the PDHbeta enzymes, which is in contrast to the optimal temperature and thermostability, and indicates that the kinetic parameters of the PDHbetas are not a reflection of whether the protein is a subunit of an alphabetagammadelta-type PDHbeta or alpha4beta4-type PDHbeta ProDH complex
Pyrococcus horikoshii
additional information
values for kcat, Km, and Ki values for L-proline and Ki' for pyrrolidone-5-carboxylate differ greatly among the PDHbeta enzymes, which is in contrast to the optimal temperature and thermostability, and indicates that the kinetic parameters of the PDHbetas are not a reflection of whether the protein is a subunit of an alphabetagammadelta-type PDHbeta or alpha4beta4-type PDHbeta ProDH complex
Pyrococcus furiosus
additional information
values for kcat, Km, and Ki values for L-proline and Ki' for pyrrolidone-5-carboxylate differ greatly among the PDHbeta enzymes, which is in contrast to the optimal temperature and thermostability, and indicates that the kinetic parameters of the PDHbetas are not a reflection of whether the protein is a subunit of an alphabetagammadelta-type PDHbeta or alpha4beta4-type PDHbeta ProDH complex
Thermococcus kodakarensis
General Information (protein specific)
General Information
Commentary
Organism
evolution
nearly all of the residues responsible for the interaction with substrate and FAD are highly conserved in Pyrococcus and Thermococcus. Phylogenetic analysis shows that the divergence of the alphabetagammadelta-type PDHbetas is spread wider than that of alpha4beta4-type PDHbetas
Thermococcus profundus
evolution
nearly all of the residues responsible for the interaction with substrate and FAD are highly conserved in Pyrococcus and Thermococcus. Phylogenetic analysis shows that the divergence of the alphabetagammadelta-type PDHbetas is spread wider than that of alpha4beta4-type PDHbetas
Pyrococcus horikoshii
evolution
nearly all of the residues responsible for the interaction with substrate and FAD are highly conserved in Pyrococcus and Thermococcus. Phylogenetic analysis shows that the divergence of the alphabetagammadelta-type PDHbetas is spread wider than that of alpha4beta4-type PDHbetas
Pyrococcus furiosus
evolution
nearly all of the residues responsible for the interaction with substrate and FAD are highly conserved in Pyrococcus and Thermococcus. Phylogenetic analysis shows that the divergence of the alphabetagammadelta-type PDHbetas is spread wider than that of alpha4beta4-type PDHbetas
Thermococcus kodakarensis
additional information
values for kcat, Km, and Ki values for L-proline and Ki' for pyrrolidone-5-carboxylate differ greatly among the PDHbeta enzymes, which is in contrast to the optimal temperature and thermostability, and indicates that the kinetic parameters of the PDHbetas are not a reflection of whether the protein is a subunit of an alphabetagammadelta-type PDHbeta or alpha4beta4-type PDHbeta ProDH complex
Thermococcus profundus
additional information
values for kcat, Km, and Ki values for L-proline and Ki' for pyrrolidone-5-carboxylate differ greatly among the PDHbeta enzymes, which is in contrast to the optimal temperature and thermostability, and indicates that the kinetic parameters of the PDHbetas are not a reflection of whether the protein is a subunit of an alphabetagammadelta-type PDHbeta or alpha4beta4-type PDHbeta ProDH complex
Pyrococcus horikoshii
additional information
values for kcat, Km, and Ki values for L-proline and Ki' for pyrrolidone-5-carboxylate differ greatly among the PDHbeta enzymes, which is in contrast to the optimal temperature and thermostability, and indicates that the kinetic parameters of the PDHbetas are not a reflection of whether the protein is a subunit of an alphabetagammadelta-type PDHbeta or alpha4beta4-type PDHbeta ProDH complex
Pyrococcus furiosus
additional information
values for kcat, Km, and Ki values for L-proline and Ki' for pyrrolidone-5-carboxylate differ greatly among the PDHbeta enzymes, which is in contrast to the optimal temperature and thermostability, and indicates that the kinetic parameters of the PDHbetas are not a reflection of whether the protein is a subunit of an alphabetagammadelta-type PDHbeta or alpha4beta4-type PDHbeta ProDH complex
Thermococcus kodakarensis
Other publictions for EC 1.5.5.2
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
Synonyms
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)
743834
Huijbers
Proline dehydrogenase from Th ...
Thermus thermophilus, Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
Sci. Rep.
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Co-regulation of mitochondria ...
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Cabassa-Hourton
Proteomic and functional anal ...
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2016
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Molecular cloning and express ...
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Huijbers
High yields of active Thermus ...
Thermus thermophilus, Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
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6
1
1
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2
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Moxley
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1
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3
742487
Schertl
Biochemical characterization ...
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2014
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1
2
2
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724389
Serrano
Kinetic and isotopic character ...
Mycobacterium tuberculosis
Biochemistry
52
5009-5015
2013
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2
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1
1
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2
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2
2
741732
Kawakami
Comparative analysis of the c ...
Pyrococcus horikoshii, Thermococcus kodakarensis, Thermococcus profundus, Pyrococcus furiosus, Thermococcus kodakarensis KOD1 JCM12380, Thermococcus profundus DSM 9503, Pyrococcus horikoshii OT-3
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22
7
24
7
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7
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7
7
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14
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7
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22
7
7
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7
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14
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742641
Omidinia
Expression, purification and ...
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297-302
2013
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2
2
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1
1
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743635
Paes
Proline dehydrogenase regulat ...
Trypanosoma cruzi, Trypanosoma cruzi CL Brener
PLoS ONE
8
e69419
2013
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1
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1
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1
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10
1
1
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2
2
1
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Moxley
Rapid reaction kinetics of pro ...
Escherichia coli
Biochemistry
51
511-520
2012
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1
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739932
Kawakami
L-proline dehydrogenases in hy ...
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83-93
2012
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4
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1
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711252
Srivastava
The structure of the proline u ...
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Biochemistry
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696361
Ostrander
A conserved active site tyrosi ...
Escherichia coli
Biochemistry
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1
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6
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Zhu
Exploring the proline-dependen ...
Escherichia coli
Biochemistry
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12297-12306
2005
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4
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658033
Zhang
Structures of the Escherichia ...
Escherichia coli
Biochemistry
43
12539-12548
2004
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1
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2
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658211
Baban
Probing a hydrogen bond pair a ...
Escherichia coli
Biochim. Biophys. Acta
1701
49-59
2004
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Kawakami
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Nadaraia
Crystallization and preliminar ...
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Sakuraba
Purification, characterization ...
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Proline dehydrogenase activity ...
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Oxidation of L-thiazolidine-4- ...
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Membrane association of prolin ...
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