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Results 1 - 10 of 38 > >>
EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.B26-999 - an important role of the sequence segment present only in hyperthermophilic beta-glycosidases, in the thermal adaptation of archaea beta-glycosidases is hypothesized. The thermostabilization mechanism could occur as a consequence of numerous favorable ionic interactions of the 83–124 sequence with the other part of protein matrix that becomes more rigid and less accessible to the insult of thermal-activated solvent molecules 721008
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.B26-999 - inactivation is coupled to irreversible aggregation 722214
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.B26-999 - protein contains 68 tryptophans, two distinct classes of tryptophanyl residues that differ in microenvironmental characteristics. The conformational dynamics of the two classes of tryptophanyl residues is affected differently by temperature, suggesting that the protein regions in which they are located give different contributions to enzyme properties, such as flexibility, stability and function 724903
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.B26-999 - the conformational transitions of thermophilic beta-glycosidase from Sulfolobus solfataricus and the mechanism of its thermal and chemical activation are studied by electron paramagnetic resonance of nitroxide spin labels immobilized on the protein matrix 721362
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.B26-999 - the fluorescence emission is characterized by a bimodal lifetime distribution, suggesting that the enzyme structure contains rigid and flexible regions, properly located in the macromolecule. The enzyme activity and thermostability appear to be related to the dynamic properties of these regions as evidenced by perturbation studies of the enzyme structure at alkaline pH and by addition of detergents such as SDS. The pH increase affects the protein dynamics with a remarkable loss of thermal stability and activity; these changes occur without any significant variation in the secondary structure as revealed by far-UV dichroic measurements. In the presence of 0.02% (w/v) SDS at alkaline pH, the enzymatic activity and thermostability are recovered. Under these conditions, the conformational dynamics appear to be similar to that evidenced at neutral pH. Further inreases in SDS concentration, at alkaline pH, render the activity and thermostability of beta-glycosidase similar to those observed in the absence of detergent 721006
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.B26-999 - the thermostability is affected by the nature and charge of the cations, reaching maximal effects for the case of Mg2+. Cations can cause a strong attenuation of the ion pair interactions E474–K72 and D473–R402, with consequent partial dissociation of the tetrameric structure 724893
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.B26-999 - the thermostable enzyme is an interesting model system for the study of protein adaptation to high temperatures. The largest ion-pair network of the enzyme is located at the tetrameric interface of the molecule 721007
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.B26-999 - thermostability is not affected by the presence of Mg2+ 724623
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.B265 - after a storage greater than 40 h at atmospheric pressure, the residual activity decreases 724406
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.B2630 100 pH 6.5, no denaturation occurrs in the temperature range of 30 to 100°C for both the native and recombinant enzyme 722128
Results 1 - 10 of 38 > >>