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24
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two stable, folded conformers with an abrupt conformational transition occurring at 24°C. The transition state thermodynamics for the low- to high-temperature conformational change are calculated from slow-scan-rate differential scanning calorimetry measurements where it is found that the free energy barrier for the conversion is 90 kJ/mol and the transition state possesses a significant unfolding quality
25
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30 min, 27% loss of activity
30 - 40
recombinant enzyme, highly stable at
37
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30 min, nearly 80% loss of activity
47
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midpoint temperature Tm, without a ligand, carboxamidomethylated enzyme, value determined by differential scanning calometry
52.8
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Tm (wild-type): 52.8°C, t1/2 (wild-type, 37°C): 3 years
54
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midpoint temperature Tm, mutant enzyme W308F/W333F, with 3-phosphoglycerate and MgADP- as ligand, value determined by differential scanning calometry
55
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midpoint temperature Tm, with MgATP2- as ligand, unmodified enzyme, value determined by differential scanning calometry
58
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midpoint temperature Tm, with 3-phosphoglycerate as ligand, unmodified enzyme, value determined by differential scanning calometry
63
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midpoint temperature Tm, with 3-phosphoglycerate and MgADP- as ligand, wild-type enzyme, value determined by differential scanning calometry
79
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20 min, no loss of activity
92
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5 min, 75% loss of activity
100
half-life: 28 min
100
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the enzyme has a half-life of irreversible thermal inactivation of 2 h at 100°C
48
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midpoint temperature Tm, without a ligand, mutant enzyme W308F/W333F, value determined by differential scanning calometry
48
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midpoint temperature Tm, with MgATP2- as ligand, carboxamidomethylated enzyme, value determined by differential scanning calometry
49
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30 min, approximately 95% loss of activity
49
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midpoint temperature Tm, with MgATP2- as ligand, mutant enzyme W308F/W333F, value determined by differential scanning calometry
49
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midpoint temperature Tm, with MgADP- as ligand, carboxamidomethylated enzyme, value determined by differential scanning calometry
50
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wild-type, mutants V311L and Y239F/E309Q incubated for 1-12 min do not show drastic reductions in activity at 50°C. 30% of their initial activities decay after 1 min incubation at 60°C
50
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pH 6.0, 10 min: 20% loss of activity, PGKA, 80% loss of activity PGKB
51
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midpoint temperature Tm, with 3-phosphoglycerate as ligand, mutant enzyme W308F/W333F, value determined by differential scanning calometry
51
-
midpoint temperature Tm, with 3-phosphoglycerate and MgADP- as ligand, carboxamidomethylated enzyme
52
-
midpoint temperature Tm, with MgADP- as ligand, mutant enzyme W308F/W333F, value determined by differential scanning calometry
52
-
midpoint temperature Tm, with 3-phosphoglycerate as ligand, carboxamidomethylated enzyme, value determined by differential scanning calometry
53
-
midpoint temperature Tm, without a ligand, mutant enzyme W333F, value determined by differential scanning calometry
53
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midpoint temperature Tm, without a ligand, unmodified enzyme, value determined by differential scanning calometry
56
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midpoint temperature Tm, with MgATP2- as ligand, mutant enzyme W333F, value determined by differential scanning calometry
56
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midpoint temperature Tm, without a ligand, wild-type enzyme, value determined by differential scanning calometry
57
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midpoint temperature Tm, with 3-phosphoglycerate as ligand, mutant enzyme W333F, value determined by differential scanning calometry
57
-
midpoint temperature Tm, with MgADP- as ligand, mutant enzyme W333F, value determined by differential scanning calometry
57
-
midpoint temperature Tm, with MgADP- as ligand, unmodified enzyme, value determined by differential scanning calometry
59
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midpoint temperature Tm, mutant enzyme W333F, with 3-phosphoglycerate and MgADP- as ligand, value determined by differential scanning calometry
59
-
midpoint temperature Tm, with 3-phosphoglycerate and MgADP- as ligand, unmodified enzyme, value determined by differential scanning calometry
60
-
10 min, stable
60
-
midpoint temperature Tm, with 3-phosphoglycerate as ligand, wild-type enzyme, value determined by differential scanning calometry
60
-
midpoint temperature Tm, with MgATP2- as ligand, wild-type enzyme, value determined by differential scanning calometry
61
-
30 min, enzyme retains less than 4% of its activity
61
-
midpoint temperature Tm, with MgADP- as ligand, wild-type enzymne, value determined by differential scanning calometry
65
-
80% activity at 65°C, then rapidly decreasing between 65-80°C
65
-
enzymatic activity is completely lost at temperatures over 65°C
85
the enzyme from the original organism is completely resistant to heat inactivation for 35 min. Expression in Escherichia coli at optimal growth temperatures (37°C) yields a product which shows a tight association with a 28000 Da protein and exhibits low thermal stability (about 80% loss of activity after 5 min) suggesting a misfolding of the protein. As proved by N-terminal amino acid sequence analysis, the 28000 Da protein represents a 226-amino acid C-terminal fragment of the 3-phosphoglycerate kinase. Mutagenesis experiments confirm the assumption that the fragment originates by an internal translation initiation
additional information
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additional information
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PGK1 is more heat-stable than PGK2
additional information
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L-MgADP binds to the specific adenosine-binding site and protects the conformation of hPGK molecule against heat denaturation
additional information
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stabilizing effects of anions on thermal stability
additional information
stabilizing effects of anions on thermal stability
additional information
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thermal denaturation at pH 5.5 and pH 7.5 of the isoenzymes
additional information
decreased thermostability, cold-adapted organism
additional information
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decreased thermostability, cold-adapted organism
additional information
the recombinant His-tagged wild-type enzyme shows reduced thermostability compared to the native and recombinant wild-type without tag
additional information
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the recombinant His-tagged wild-type enzyme shows reduced thermostability compared to the native and recombinant wild-type without tag
additional information
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the psychrophilic enzyme enzyme exhibits two distinct stability domains in the free, open conformation. These stability domains do not match the structural N- and C-domains as the heat-stable domain corresponds to about 80 residues of the C-domain, including the nucleotide binding site, whereas the remaining of the protein contributes to the main heat-labile domain
additional information
stabilizing effects of anions on thermal stability
additional information
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stabilizing effects of anions on thermal stability
additional information
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thermal analysis
additional information
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additional information
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thermal analysis
additional information
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thermal analysis