EC Number | Cloned (Comment) | Organism |
---|---|---|
1.5.5.2 | sequence comparisons and phylogenetic analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21-CodonPlus(DE3)-RIPL | Thermococcus profundus |
1.5.5.2 | sequence comparisons and phylogenetic analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21-CodonPlus(DE3)-RIPL | Pyrococcus horikoshii |
1.5.5.2 | sequence comparisons and phylogenetic analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21-CodonPlus(DE3)-RIPL | Pyrococcus furiosus |
1.5.5.2 | sequence comparisons and phylogenetic analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21-CodonPlus(DE3)-RIPL | Thermococcus kodakarensis |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
1.5.5.2 | L-proline | substrate inhibition at high L-proline concentrations; substrate inhibition at high L-proline concentrations | Pyrococcus furiosus | |
1.5.5.2 | L-proline | substrate inhibition at high L-proline concentrations; substrate inhibition at high L-proline concentrations | Pyrococcus horikoshii | |
1.5.5.2 | L-proline | substrate inhibition at high L-proline concentrations; substrate inhibition at high L-proline concentrations | Thermococcus kodakarensis | |
1.5.5.2 | L-proline | substrate inhibition at high L-proline concentrations | Thermococcus profundus | |
1.5.5.2 | pyrrolidone-5-carboxylate | - |
Pyrococcus furiosus | |
1.5.5.2 | pyrrolidone-5-carboxylate | - |
Pyrococcus horikoshii | |
1.5.5.2 | pyrrolidone-5-carboxylate | - |
Thermococcus kodakarensis | |
1.5.5.2 | pyrrolidone-5-carboxylate | - |
Thermococcus profundus |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.5.5.2 | Pyrococcus furiosus | Q8U022 | - |
- |
1.5.5.2 | Pyrococcus furiosus | Q8U1G2 | - |
- |
1.5.5.2 | Pyrococcus horikoshii | O59089 | - |
- |
1.5.5.2 | Pyrococcus horikoshii | O59445 | - |
- |
1.5.5.2 | Pyrococcus horikoshii OT-3 | O59089 | - |
- |
1.5.5.2 | Pyrococcus horikoshii OT-3 | O59445 | - |
- |
1.5.5.2 | Thermococcus kodakarensis | Q5JFG2 | - |
- |
1.5.5.2 | Thermococcus kodakarensis | Q5JFG7 | - |
- |
1.5.5.2 | Thermococcus kodakarensis KOD1 JCM12380 | Q5JFG7 | - |
- |
1.5.5.2 | Thermococcus profundus | Q76M73 | - |
- |
1.5.5.2 | Thermococcus profundus DSM 9503 | Q76M73 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
1.5.5.2 | recombinant His-tagged enzyme from Escherichia coli strain BL21-CodonPlus(DE3)-RIPL by nickel affinity chromatography and dialysis to homogeneity | Thermococcus profundus |
1.5.5.2 | recombinant His-tagged enzyme from Escherichia coli strain BL21-CodonPlus(DE3)-RIPL by nickel affinity chromatography and dialysis to homogeneity | Pyrococcus furiosus |
1.5.5.2 | recombinant His-tagged enzyme from Escherichia coli strain BL21-CodonPlus(DE3)-RIPL by nickel affinity chromatography and dialysis to homogeneity | Thermococcus kodakarensis |
1.5.5.2 | 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 |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.5.5.2 | L-proline + 2,6-dichlorphenol-indophenol | - |
Thermococcus profundus | (S)-1-pyrroline-5-carboxylate + reduced 2,6-dichlorphenol-indophenol | - |
? | |
1.5.5.2 | L-proline + 2,6-dichlorphenol-indophenol | - |
Pyrococcus horikoshii | (S)-1-pyrroline-5-carboxylate + reduced 2,6-dichlorphenol-indophenol | - |
? | |
1.5.5.2 | L-proline + 2,6-dichlorphenol-indophenol | - |
Pyrococcus furiosus | (S)-1-pyrroline-5-carboxylate + reduced 2,6-dichlorphenol-indophenol | - |
? | |
1.5.5.2 | L-proline + 2,6-dichlorphenol-indophenol | - |
Thermococcus kodakarensis | (S)-1-pyrroline-5-carboxylate + reduced 2,6-dichlorphenol-indophenol | - |
? | |
1.5.5.2 | L-proline + 2,6-dichlorphenol-indophenol | - |
Thermococcus kodakarensis KOD1 JCM12380 | (S)-1-pyrroline-5-carboxylate + reduced 2,6-dichlorphenol-indophenol | - |
? | |
1.5.5.2 | L-proline + 2,6-dichlorphenol-indophenol | - |
Thermococcus profundus DSM 9503 | (S)-1-pyrroline-5-carboxylate + reduced 2,6-dichlorphenol-indophenol | - |
? | |
1.5.5.2 | L-proline + 2,6-dichlorphenol-indophenol | - |
Pyrococcus horikoshii OT-3 | (S)-1-pyrroline-5-carboxylate + reduced 2,6-dichlorphenol-indophenol | - |
? | |
1.5.5.2 | additional information | no activity with D-proline, L-hydroxyproline, pyrrolidone-5-carboxylate, sarcosine, and glycine | Thermococcus profundus | ? | - |
? | |
1.5.5.2 | additional information | no activity with D-proline, L-hydroxyproline, pyrrolidone-5-carboxylate, sarcosine, and glycine | Pyrococcus horikoshii | ? | - |
? | |
1.5.5.2 | additional information | no activity with D-proline, L-hydroxyproline, pyrrolidone-5-carboxylate, sarcosine, and glycine | Pyrococcus furiosus | ? | - |
? | |
1.5.5.2 | additional information | no activity with D-proline, L-hydroxyproline, pyrrolidone-5-carboxylate, sarcosine, and glycine | Thermococcus kodakarensis | ? | - |
? | |
1.5.5.2 | additional information | no activity with D-proline, L-hydroxyproline, pyrrolidone-5-carboxylate, sarcosine, and glycine | Thermococcus kodakarensis KOD1 JCM12380 | ? | - |
? | |
1.5.5.2 | additional information | no activity with D-proline, L-hydroxyproline, pyrrolidone-5-carboxylate, sarcosine, and glycine | Thermococcus profundus DSM 9503 | ? | - |
? | |
1.5.5.2 | additional information | no activity with D-proline, L-hydroxyproline, pyrrolidone-5-carboxylate, sarcosine, and glycine | Pyrococcus horikoshii OT-3 | ? | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
1.5.5.2 | octamer | the enzyme is a alpha4beta4-type ProDH | Pyrococcus horikoshii |
1.5.5.2 | octamer | the enzyme is a alpha4beta4-type ProDH | Pyrococcus furiosus |
1.5.5.2 | octamer | the enzyme is a alpha4beta4-type ProDH | Thermococcus kodakarensis |
1.5.5.2 | tetramer | the enzyme is a alphabetagammadelta-type ProDH | Thermococcus profundus |
1.5.5.2 | tetramer | the enzyme is a alphabetagammadelta-type ProDH | Thermococcus kodakarensis |
1.5.5.2 | tetramer | the enzyme is a alphabetagammadelta-type ProDH | Pyrococcus horikoshii |
1.5.5.2 | tetramer | the enzyme is a alphabetagammadelta-type ProDH | Pyrococcus furiosus |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.5.5.2 | L-proline dehydrogenase | - |
Thermococcus profundus |
1.5.5.2 | L-proline dehydrogenase | - |
Pyrococcus horikoshii |
1.5.5.2 | L-proline dehydrogenase | - |
Pyrococcus furiosus |
1.5.5.2 | L-proline dehydrogenase | - |
Thermococcus kodakarensis |
1.5.5.2 | PdhB | - |
Thermococcus profundus |
1.5.5.2 | PdhB | - |
Thermococcus kodakarensis |
1.5.5.2 | PDHbeta | - |
Pyrococcus horikoshii |
1.5.5.2 | PDHbeta | - |
Pyrococcus furiosus |
1.5.5.2 | PDHbeta | - |
Thermococcus kodakarensis |
1.5.5.2 | PF1246 | - |
Pyrococcus furiosus |
1.5.5.2 | PF1798 | - |
Pyrococcus furiosus |
1.5.5.2 | PH1364 | - |
Pyrococcus horikoshii |
1.5.5.2 | PH1751 | - |
Pyrococcus horikoshii |
1.5.5.2 | proDH-B1 | - |
Pyrococcus horikoshii |
1.5.5.2 | proDH-B2 | - |
Pyrococcus horikoshii |
1.5.5.2 | TK0117 | - |
Thermococcus kodakarensis |
1.5.5.2 | TK0122 | - |
Thermococcus kodakarensis |
1.5.5.2 | TPpdhbeta | - |
Thermococcus profundus |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
1.5.5.2 | 50 | - |
assay at | Thermococcus profundus |
1.5.5.2 | 50 | - |
assay at | Pyrococcus horikoshii |
1.5.5.2 | 50 | - |
assay at | Pyrococcus furiosus |
1.5.5.2 | 50 | - |
assay at | Thermococcus kodakarensis |
EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|---|
1.5.5.2 | 70 | - |
the alpha4beta4-type PDHbeta retains more than 80% of its activity after heating at 70°C for 20 min | Pyrococcus horikoshii |
1.5.5.2 | 70 | - |
the alpha4beta4-type PDHbeta retains more than 80% of its activity after heating at 70°C for 20 min | Pyrococcus furiosus |
1.5.5.2 | 70 | - |
the alpha4beta4-type PDHbeta retains more than 80% of its activity after heating at 70°C for 20 min | Thermococcus kodakarensis |
1.5.5.2 | 70 | - |
the alphabetagammadelta-type PDHbeta nearly loses all of its activity during incubation at 70°C for 20 min | Pyrococcus horikoshii |
1.5.5.2 | 70 | - |
the alphabetagammadelta-type PDHbeta retains 100% of activity during incubation at 70°C for 20 min | Pyrococcus furiosus |
1.5.5.2 | 70 | - |
the alphabetagammadelta-type PDHbeta retains 68% of activity during incubation at 70°C for 20 min | Thermococcus profundus |
1.5.5.2 | 70 | - |
the alphabetagammadelta-type PDHbeta retains 76% of activity during incubation at 70°C for 20 min | Thermococcus kodakarensis |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
1.5.5.2 | 8 | - |
assay at | Thermococcus profundus |
1.5.5.2 | 8 | - |
assay at | Pyrococcus horikoshii |
1.5.5.2 | 8 | - |
assay at | Pyrococcus furiosus |
1.5.5.2 | 8 | - |
assay at | Thermococcus kodakarensis |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.5.5.2 | FAD | non-covalent binding | Thermococcus profundus | |
1.5.5.2 | FAD | non-covalent binding | Pyrococcus horikoshii | |
1.5.5.2 | FAD | non-covalent binding | Pyrococcus furiosus | |
1.5.5.2 | FAD | non-covalent binding | Thermococcus kodakarensis |
EC Number | General Information | Comment | Organism |
---|---|---|---|
1.5.5.2 | 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 |
1.5.5.2 | 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 |
1.5.5.2 | 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 |
1.5.5.2 | 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 |
1.5.5.2 | 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 |
1.5.5.2 | 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 |
1.5.5.2 | 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 |
1.5.5.2 | 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 |