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Literature summary for 2.7.7.7 extracted from

  • Summit, M.; Scott, B.; Nielson, K.; Mathur, E.; Baross, J.
    Pressure enhances thermal stability of DNA polymerase from three thermophilic organisms (1998), Extremophiles, 2, 339-345.
    View publication on PubMed
Search for more literature for 2.7.7.7

General Stability

General Stability Organism
the enzyme is stabilized in vitro by hydrostatic pressure at denaturing temperature of 100°C Thermus aquaticus
the enzyme is stabilized in vitro by hydrostatic pressure at denaturing temperature of 107.5°C Pyrococcus furiosus
the enzyme is stabilized in vitro by hydrostatic pressure at denaturing temperature of 111°C Pyrococcus sp.

Organism

Organism UniProt Comment Textmining
Pyrococcus furiosus
-
-
-
Pyrococcus sp.
-
-
-
Pyrococcus sp. ES4
-
-
-
Thermus aquaticus
-
-
-

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
-
 the enzyme is stabilized in vitro by hydrostatic pressure at denaturing temperature of 100°C Thermus aquaticus
additional information
-
 the enzyme is stabilized in vitro by hydrostatic pressure at denaturing temperature of 107.5°C Pyrococcus furiosus
additional information
-
 the enzyme is stabilized in vitro by hydrostatic pressure at denaturing temperature of 111°C Pyrococcus sp.
100
-
 half-life at 3 MPa is 5.2 min, half-life at 45 MPa is 13 min, half-life at 89 MPa is 39 min Thermus aquaticus
107.5
-
 half-life at 3 MPa is 6.9 min, half-life at 45 MPa is 36 min, half-life at 89 MPa is 50 min Pyrococcus furiosus
111
-
 half-life at 3 MPa is 5.0 min, half-life at 45 MPa is 12 min, half-life at 89 MPa is 26 min Pyrococcus sp.