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
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
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
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
?
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
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
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
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
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
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
?
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
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
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
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
743834
Huijbers
Proline dehydrogenase from Th ...
Thermus thermophilus, Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
Sci. Rep.
7
43880
2017
-
-
1
1
1
-
-
3
-
-
-
2
-
6
-
-
-
-
-
-
4
-
4
1
1
1
-
-
3
1
-
-
3
-
-
-
-
-
1
3
1
1
-
-
-
-
3
-
-
-
2
-
-
-
-
-
-
4
-
4
1
1
-
-
3
1
-
-
-
-
-
-
-
3
3
741588
Hancock
Co-regulation of mitochondria ...
Homo sapiens, Mus musculus
Amino Acids
48
859-872
2016
-
-
2
-
1
-
12
-
2
-
-
-
-
4
-
-
1
-
-
-
-
-
-
-
4
2
-
-
-
2
-
-
2
-
-
-
-
-
2
2
-
1
-
-
12
-
-
2
-
-
-
-
-
-
1
-
-
-
-
-
-
2
-
-
-
2
-
-
-
-
6
6
-
-
-
741858
Cabassa-Hourton
Proteomic and functional anal ...
Arabidopsis thaliana
Biochem. J.
473
2623-2634
2016
-
-
-
-
1
-
-
-
3
-
-
-
-
5
-
-
1
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
3
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
1
1
-
-
741642
Wang
Molecular cloning and express ...
Jatropha curcas
Appl. Biochem. Biotechnol.
175
2413-2426
2015
-
-
1
-
-
-
-
-
-
-
-
-
-
4
-
-
-
-
-
6
-
-
-
2
2
-
-
-
-
-
-
-
-
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
6
-
-
-
2
-
-
-
-
-
-
-
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
-
1
1
-
-
-
1
-
1
-
3
2
-
5
-
-
1
-
-
-
1
-
6
1
2
1
-
2
-
1
-
-
1
-
-
-
-
1
1
1
-
-
-
-
1
-
-
1
-
3
2
-
-
-
1
-
-
1
-
6
1
1
-
2
-
1
-
-
-
-
1
1
-
-
-
740734
Moxley
Evidence for hysteretic substr ...
Escherichia coli
J. Biol. Chem.
289
3639-3651
2014
-
-
-
-
-
-
-
3
-
-
-
-
-
2
-
-
-
-
-
-
-
-
2
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
1
-
-
-
-
-
-
-
-
3
3
742487
Schertl
Biochemical characterization ...
Arabidopsis thaliana
FEBS J.
281
2794-2804
2014
-
-
-
-
-
-
2
-
2
-
-
1
-
4
-
-
-
-
-
-
-
-
2
1
1
-
-
-
-
-
-
-
2
-
-
-
-
-
-
2
-
-
-
-
2
-
-
2
-
-
1
-
-
-
-
-
-
-
-
2
1
-
-
-
-
-
-
-
-
1
2
2
1
-
-
724389
Serrano
Kinetic and isotopic character ...
Mycobacterium tuberculosis
Biochemistry
52
5009-5015
2013
-
-
-
-
2
-
-
3
-
-
1
-
-
2
-
-
1
-
-
-
-
-
1
1
3
-
-
-
2
-
-
-
1
-
-
-
-
-
-
1
-
2
-
-
-
-
3
-
-
1
-
-
-
-
1
-
-
-
-
1
1
-
-
-
2
-
-
-
-
-
-
-
-
2
2
741732
Kawakami
Comparative analysis of the c ...
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Proline dehydrogenase activity ...
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