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. 1998 Mar 3;95(5):2056–2060. doi: 10.1073/pnas.95.5.2056

Table 3.

Stabilities of the 8-fold TLP-ste mutant and a selection of enzymes from extremophiles

Enzyme Source Half-life, hr T, °C Ref.
2-Ketoisovalerate-ferredoxin oxidoreductase Thermococcus litoralis 0.8 95 (41)
Carbamoyl-phosphate synthetase Pyrococcus abyssi 3 95 (42)
Sulfide dehydrogenase Pyrococcus furiosus 12 95 (43)
α-Glucosidase Thermococcus AN1 0.6 98 (44)
3-Phosphoglycerate kinase Pyrococcus woesei 0.45 100 (45)
Glyceraldehyde-3-phosphate dehydrogenase Pyrococcus woesei 0.7 100 (46)
DNA-RNA polymerase Thermoproteus tenax 2 100 (26)
Hydrogenase Pyrococcus furiosus 2 100 (47)
Glyceraldehyde-3-phosphate dehydrogenase Thermotoga maritima >2 100 (48)
Eightfold TLP-ste mutant B. stearothermophilus 2.8 100 (This study)
ADP-dependent glucokinase Pyrococcus furiosus 3.6 100 (49)
Amylase Pyrococcus woesei 6 100 (26)
Glutamate dehydrogenase Pyrococcus furiosus 10 100 (50)
β-Glucosidase Pyrococcus furiosus 85 100 (51)
Cellobiohydrolase Thermotoga sp. 1 108 (26)
α-Amylase Pyrococcus furiosus 2 120 (52)