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Literature summary for 3.2.1.B26 extracted from
- Tryptophanyl fluorescence lifetime distribution of hyperthermophilic beta-glycosidase from molecular dynamics simulation: a comparison with the experimental data (2000), Protein Sci., 9, 1730-1742.
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Saccharolobus solfataricus | - |
- |
- |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| tetramer | contains 17 tryptophanyl residues for each subunit. Molecular dynamic simulation studies performed on the multitryptophan subunit of the beta-glycosidase. The molecular dynamic trajectories obtained from the simulation provide information about the distances and mobility of solvent molecules and specific amino acid residues able to quench the tryptophanyl fluorescence in each tryptophan environment. From these data, the fluorescence lifetime for each tryptophan residue of Sbgly can be estimated using a modified Stern-Volmer expr. The results are in agreement with the emission decay of the enzyme experimentally detected | Saccharolobus solfataricus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| Sbetagly | - |
Saccharolobus solfataricus |
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