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Literature summary extracted from

  • Pedone, E.; Saviano, M.; Bartolucci, S.; Rossi, M.; Ausili, A.; Scirè, A.; Bertoli, E.; Tanfani, F.
    Temperature-, SDS-, and pH-induced conformational changes in protein disulfide oxidoreductase from the archaeon Pyrococcus furiosus A dynamic simulation and fourier transform infrared spectroscopic study (2005), J. Proteome Res., 4, 1972-1980 .
    View publication on PubMed

General Stability

EC Number General Stability Organism
1.8.1.8 The structure and thermal stability of the protein are analyzed under different conditions by Fourier transform infrared spectroscopy and Molecular Dynamics simulations. The effects of SDS, pH, and temperature on the protein structure are characterized. The data indicated that pD affects differently the thermostability of alpha-helices and beta-sheets, and that 0.5% or higher SDS concentration have a significant repercussion on the structure Pyrococcus furiosus

Organic Solvent Stability

EC Number Organic Solvent Comment Organism
1.8.1.8 SDS The secondary structure of the protein is not affected by 0.1 or 0.2% of SDS. In the presence of 0.5%, the intensity of the alpha-helix band decreases markedly while the intensity of the beta-sheet band is slightly affected. In the presence of 0.7% SDS the beta-sheet band intensity decreases further and in the presence of 4% SDS it results very low Pyrococcus furiosus

Organism

EC Number Organism UniProt Comment Textmining
1.8.1.8 Pyrococcus furiosus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.8.1.8
-
Pyrococcus furiosus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.8.1.8 additional information computational analysis reveals the different behavior of the two active sites Pyrococcus furiosus ?
-
?

Synonyms

EC Number Synonyms Comment Organism
1.8.1.8 PfPDO
-
Pyrococcus furiosus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.8.1.8 additional information
-
pH affects differently the thermostability of alpha-helices and beta-sheets Pyrococcus furiosus
1.8.1.8 20
-
the C terminal active site at 20°C shows a reduced flexibility at all pH values, while at 100°C the flexibility increases with the pH, with a high value at pH 7.0 Pyrococcus furiosus
1.8.1.8 100
-
flexibility increases with the pH, with a high value at pH 7.0 Pyrococcus furiosus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.8.1.8 7
-
-
Pyrococcus furiosus

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
1.8.1.8 5.8
-
the residual amide II band intensity is higher at pH 5.8 than at pH 7.0 suggesting that the acidic pH induces a more compact structure At pH 5.8, pH not optimum for the activity, and at 10°C and 100°C, the alpha2 helix region, where the N-terminal active site is localized, is less flexible than at pH 7.0 and pH 10.0 Pyrococcus furiosus
1.8.1.8 7
-
the residual amide II band intensity is higher at pH 5.8 than at pH 7.0 suggesting that the acidic pH induces a more compact structure. At pH 5.8, pH not optimum for the activity, and at 10°C and 100°C, the alpha2 helix region, where the N-terminal active site is localized, is less flexible than at pH 7.0 and pH 10.0 Pyrococcus furiosus
1.8.1.8 10
-
at pH 10.0 the protein undergoes partial unfolding. Decrease in alpha-helix content at pH 10.0, whereas the beta-sheet content remains unaltered. At pH 5.8, pH not optimum for the activity, and at 10°C and 100°C, the alpha2 helix region, where the N-terminal active site is localized, is less flexible than at pH 7.0 and pH 10.0. The C terminal active site at 20°C shows a reduced flexibility at all pH values, while at 100°C the flexibility increases with the pH, with a high value at pH 7.0 Pyrococcus furiosus