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show all sequences of 1.5.5.2

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)
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; 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; 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; 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
Primary Accession No. (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)
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, the PH1751 protein tends to aggregate during dialysis; 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
recombinant His-tagged enzyme from Escherichia coli strain BL21-CodonPlus(DE3)-RIPL by nickel affinity chromatography and dialysis to homogeneity; 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; recombinant His-tagged enzyme from Escherichia coli strain BL21-CodonPlus(DE3)-RIPL by nickel affinity chromatography and dialysis to homogeneity
Thermococcus kodakarensis
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
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 furiosus
octamer
the enzyme is a alpha4beta4-type ProDH
Pyrococcus horikoshii
octamer
the enzyme is a alpha4beta4-type ProDH
Thermococcus kodakarensis
tetramer
the enzyme is a alphabetagammadelta-type ProDH
Pyrococcus furiosus
tetramer
the enzyme is a alphabetagammadelta-type ProDH
Pyrococcus horikoshii
tetramer
the enzyme is a alphabetagammadelta-type ProDH
Thermococcus kodakarensis
tetramer
the enzyme is a alphabetagammadelta-type ProDH
Thermococcus profundus
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
50
-
assay at; assay at
Pyrococcus furiosus
50
-
assay at; assay at
Pyrococcus horikoshii
50
-
assay at; assay at
Thermococcus kodakarensis
50
-
assay at
Thermococcus profundus
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; the alphabetagammadelta-type PDHbeta retains 100% of activity during incubation 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; the alphabetagammadelta-type PDHbeta nearly loses all of its activity during incubation 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; the alphabetagammadelta-type PDHbeta retains 76% of activity during incubation at 70°C for 20 min
Thermococcus kodakarensis
70
-
the alphabetagammadelta-type PDHbeta retains 68% of activity during incubation at 70°C for 20 min
Thermococcus profundus
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
assay at; assay at
Pyrococcus furiosus
8
-
assay at; assay at
Pyrococcus horikoshii
8
-
assay at; assay at
Thermococcus kodakarensis
8
-
assay at
Thermococcus profundus
Cofactor
Cofactor
Commentary
Organism
Structure
FAD
non-covalent binding; non-covalent binding
Pyrococcus furiosus
FAD
non-covalent binding; non-covalent binding
Pyrococcus horikoshii
FAD
non-covalent binding; non-covalent binding
Thermococcus kodakarensis
FAD
non-covalent binding
Thermococcus profundus
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
Pyrococcus furiosus
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
Thermococcus kodakarensis
sequence comparisons and phylogenetic analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21-CodonPlus(DE3)-RIPL
Thermococcus profundus
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
FAD
non-covalent binding
Pyrococcus furiosus
FAD
non-covalent binding
Pyrococcus horikoshii
FAD
non-covalent binding
Thermococcus kodakarensis
FAD
non-covalent binding
Thermococcus profundus
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
L-proline
substrate inhibition at high L-proline concentrations
Pyrococcus furiosus
L-proline
substrate inhibition at high L-proline concentrations
Pyrococcus horikoshii
L-proline
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
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
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
Thermococcus profundus
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
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 furiosus
octamer
the enzyme is a alpha4beta4-type ProDH
Pyrococcus horikoshii
octamer
the enzyme is a alpha4beta4-type ProDH
Thermococcus kodakarensis
tetramer
the enzyme is a alphabetagammadelta-type ProDH
Pyrococcus furiosus
tetramer
the enzyme is a alphabetagammadelta-type ProDH
Pyrococcus horikoshii
tetramer
the enzyme is a alphabetagammadelta-type ProDH
Thermococcus kodakarensis
tetramer
the enzyme is a alphabetagammadelta-type ProDH
Thermococcus profundus
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
50
-
assay at
Pyrococcus furiosus
50
-
assay at
Pyrococcus horikoshii
50
-
assay at
Thermococcus kodakarensis
50
-
assay at
Thermococcus profundus
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 furiosus
70
-
the alphabetagammadelta-type PDHbeta retains 100% of activity during incubation 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
Pyrococcus horikoshii
70
-
the alphabetagammadelta-type PDHbeta nearly loses all of its activity during incubation 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
Thermococcus kodakarensis
70
-
the alphabetagammadelta-type PDHbeta retains 76% of activity during incubation at 70°C for 20 min
Thermococcus kodakarensis
70
-
the alphabetagammadelta-type PDHbeta retains 68% of activity during incubation at 70°C for 20 min
Thermococcus profundus
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
assay at
Pyrococcus furiosus
8
-
assay at
Pyrococcus horikoshii
8
-
assay at
Thermococcus kodakarensis
8
-
assay at
Thermococcus profundus
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; 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; 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; 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
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
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; 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; 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; 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
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
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
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
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
Thermococcus kodakarensis
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
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
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
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
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
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.
7
43880
2017
-
-
1
1
1
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-
3
-
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2
-
6
-
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-
4
-
4
1
1
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3
1
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3
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1
3
1
1
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3
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2
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4
-
4
1
1
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3
1
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3
3
741588
Hancock
Co-regulation of mitochondria ...
Homo sapiens, Mus musculus
Amino Acids
48
859-872
2016
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-
2
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1
-
12
-
2
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4
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1
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2
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1
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12
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2
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1
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2
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2
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6
6
-
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-
741858
Cabassa-Hourton
Proteomic and functional anal ...
Arabidopsis thaliana
Biochem. J.
473
2623-2634
2016
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-
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1
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5
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1
1
1
1
-
-
741642
Wang
Molecular cloning and express ...
Jatropha curcas
Appl. Biochem. Biotechnol.
175
2413-2426
2015
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1
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1
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6
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2
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1
1
2
2
1
-
-
742162
Huijbers
High yields of active Thermus ...
Thermus thermophilus, Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
Biotechnol. J.
10
395-403
2015
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1
1
-
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1
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1
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3
2
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5
-
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1
-
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-
1
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6
1
1
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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
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3
2
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1
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-
1
-
6
1
1
-
2
-
1
-
-
-
-
1
1
-
-
-
740734
Moxley
Evidence for hysteretic substr ...
Escherichia coli
J. Biol. Chem.
289
3639-3651
2014
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3
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2
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3
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2
-
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1
-
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-
-
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3
3
742487
Schertl
Biochemical characterization ...
Arabidopsis thaliana
FEBS J.
281
2794-2804
2014
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-
-
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2
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2
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1
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4
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2
1
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2
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2
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2
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1
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2
1
-
-
-
-
-
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-
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1
2
2
1
-
-
724389
Serrano
Kinetic and isotopic character ...
Mycobacterium tuberculosis
Biochemistry
52
5009-5015
2013
-
-
-
-
2
-
-
3
-
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1
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-
2
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1
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1
1
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2
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1
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1
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2
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3
-
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1
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1
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-
1
1
-
-
-
2
-
-
-
-
-
-
-
-
2
2
741732
Kawakami
Comparative analysis of the c ...
Pyrococcus furiosus, Pyrococcus horikoshii, Pyrococcus horikoshii OT-3, Thermococcus kodakarensis, Thermococcus kodakarensis KOD1 JCM12380, Thermococcus profundus, Thermococcus profundus DSM 9503
Appl. Microbiol. Biotechnol.
97
3419-3427
2013
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4
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8
-
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-
-
13
-
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4
-
-
-
-
-
22
7
4
-
4
-
4
-
-
4
-
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-
7
7
-
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-
-
14
-
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-
-
-
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-
-
7
-
-
-
-
22
7
7
-
7
-
7
-
-
-
-
8
14
-
-
-
742641
Omidinia
Expression, purification and ...
Pseudomonas putida, Pseudomonas putida POS-F84
Indian J. Microbiol.
53
297-302
2013
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1
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1
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5
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1
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2
2
1
1
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1
1
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1
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1
1
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1
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1
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-
2
2
1
1
-
-
1
1
-
-
-
1
1
-
-
-
743635
Paes
Proline dehydrogenase regulat ...
Trypanosoma cruzi, Trypanosoma cruzi CL Brener
PLoS ONE
8
e69419
2013
-
-
1
-
-
-
-
1
1
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-
2
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5
-
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1
-
-
1
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10
1
1
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1
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2
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1
2
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-
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1
1
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2
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1
-
1
-
-
10
1
1
-
-
-
1
-
-
-
1
2
2
1
-
-
724345
Moxley
Rapid reaction kinetics of pro ...
Escherichia coli
Biochemistry
51
511-520
2012
-
-
-
-
-
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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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1
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1
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1
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-
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-
739932
Kawakami
L-proline dehydrogenases in hy ...
Pyrococcus horikoshii
Appl. Microbiol. Biotechnol.
93
83-93
2012
-
-
-
-
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1
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3
1
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5
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1
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1
1
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1
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4
-
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4
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1
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3
1
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1
-
1
1
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1
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-
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-
711252
Srivastava
The structure of the proline u ...
Escherichia coli
Biochemistry
49
560-569
2010
-
-
1
1
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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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-
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-
-
-
696361
Ostrander
A conserved active site tyrosi ...
Escherichia coli
Biochemistry
48
951-959
2009
-
-
1
1
2
-
1
6
-
-
-
-
-
3
-
-
1
-
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2
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6
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1
3
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1
1
1
2
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1
3
6
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1
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2
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6
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671977
Zhu
Exploring the proline-dependen ...
Escherichia coli
Biochemistry
44
12297-12306
2005
-
-
-
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4
-
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4
1
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2
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1
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1
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4
-
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4
-
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4
1
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1
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-
-
4
-
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-
658033
Zhang
Structures of the Escherichia ...
Escherichia coli
Biochemistry
43
12539-12548
2004
-
-
1
1
1
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3
2
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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
2
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3
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1
-
1
1
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3
3
2
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1
1
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1
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-
-
1
-
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-
1
2
-
-
-
-
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-
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-
-
658211
Baban
Probing a hydrogen bond pair a ...
Escherichia coli
Biochim. Biophys. Acta
1701
49-59
2004
-
-
1
-
3
-
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4
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2
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1
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4
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1
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3
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4
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1
-
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4
-
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-
-
-
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-
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658668
Kawakami
Gene and primary structures of ...
Thermococcus profundus
Extremophiles
8
99-108
2004
-
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1
-
-
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-
1
-
1
5
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10
-
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1
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-
1
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2
1
1
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1
-
1
-
1
1
-
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-
1
1
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-
-
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1
-
1
5
-
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1
-
-
1
-
2
1
1
-
1
-
1
-
1
-
-
-
-
-
-
-
659987
Lee
Structure of the proline dehyd ...
Escherichia coli
Nat. Struct. Biol.
10
109-114
2003
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1
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-
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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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1
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1
1
-
-
-
-
-
-
-
-
-
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-
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392565
Nadaraia
Crystallization and preliminar ...
Escherichia coli
Acta Crystallogr. Sect. D
57
1925-1927
2001
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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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-
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-
-
-
-
-
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-
-
-
392570
Sakuraba
Purification, characterization ...
Thermococcus profundus
Appl. Environ. Microbiol.
67
1470-1475
2001
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-
-
-
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1
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3
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6
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1
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1
1
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2
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1
1
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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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-
2
-
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-
1
-
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-
-
-
-
-
392572
Chaudhary
-
Proline dehydrogenase activity ...
Vigna radiata
Indian J. Exp. Biol.
37
1234-1240
1999
-
-
-
-
1
-
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1
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-
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-
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392571
Brown
Conformational change and memb ...
Escherichia coli
J. Biol. Chem.
268
8972-8979
1993
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1
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1
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1
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-
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-
-
-
-
-
-
-
-
-
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-
-
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-
392569
Deutch
-
Oxidation of L-thiazolidine-4- ...
Escherichia coli
J. Gen. Microbiol.
138
1593-1598
1992
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2
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-
1
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-
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-
-
-
2
-
-
-
-
-
-
-
-
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-
-
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-
722591
Brown
Redesigned purification yields ...
Escherichia coli
J. Biol. Chem.
267
13086-13092
1992
-
-
-
-
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2
1
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1
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1
-
1
1
1
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-
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1
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
2
1
-
-
-
1
-
-
1
-
1
1
1
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-
-
1
-
-
-
-
-
-
-
-
-
392555
Wood
Membrane association of prolin ...
Escherichia coli
Proc. Natl. Acad. Sci. USA
84
373-377
1987
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1
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2
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2
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1
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2
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1
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-
-
2
-
-
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-
392556
Graham
Proline dehydrogenase from Esc ...
Escherichia coli
J. Biol. Chem.
259
2656-2661
1984
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2
2
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1
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-
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3
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1
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1
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2
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2
2
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1
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1
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-
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3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
392560
Scarpulla
Membrane-bound proline dehydro ...
Escherichia coli
J. Biol. Chem.
253
5997-6001
1978
-
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5
1
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1
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1
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4
1
-
-
-
-
1
-
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1
4
-
-
-
-
-
1
-
-
-
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5
4
1
1
-
1
1
-
-
-
1
-
-
1
-
4
1
-
-
-
-
1
-
-
-
-
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