Cloned (Comment) | Organism |
---|---|
expression of wild-type and mutant enzymes in Escherichia coli, sequence comparison | Saccharolobus solfataricus |
Crystallization (Comment) | Organism |
---|---|
TreX in complex with an acarbose ligand, microbatch method under oil at 18°C, dimeric crystal from 16% PEG 8000, 0.2 M NaCl, and 0.1 M CHES buffer, pH 9.5, tetrameric crystal form from 2.2 M ammonium phosphate and 0.1 M Tris-HCl buffer, pH 8.5. For the acarbose intermediate complex crystal, 0.1% acarbose is added to the protein, followed by incubation for 1 h prior to the setup of the crystal in 8% PEG 3000, 0.2M lithium sulfate, and 0.1 M imidazole buffer, pH 8.0, cyroprotection by 20% glycerol in mother liquor, in both crystal forms, the asymmetric unit consists of one dimer, X-ray diffraction structure determination and analysis at 2.8-3.0 A resolution | Saccharolobus solfataricus |
Protein Variants | Comment | Organism |
---|---|---|
additional information | mutations in the N-terminal region result in a sharp increase in alpha-1,4-transferase activity and a reduced level of alpha-1,6-glucosidase activity, overview | Saccharolobus solfataricus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharolobus solfataricus | P95868 | - |
- |
Purification (Comment) | Organism |
---|---|
recombinant wild-type and mutant enzymes from Escherichia coli by nickel affinity chromatography | Saccharolobus solfataricus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | TreX from Sulfolobus solfataricus shows dual activities for alpha-1,4-transferase, EC 2.4.1.25 and alpha-1,6-glucosidase, EC 3.2.1.68, bifunctional mechanism, substrate maltotriose, overview. TreX exhibits two different active-site configurations depending on its oligomeric state | Saccharolobus solfataricus | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
dimer or tetramer | the enzyme exists in two oligomeric states in solution, as a dimer and tetramer | Saccharolobus solfataricus |
More | the structural lid, amino acids 99-97, at the active site generated by the tetramerization is closely associated with the bifunctionality and in particular with the alpha-1,4-transferase activity | Saccharolobus solfataricus |
Synonyms | Comment | Organism |
---|---|---|
alpha-1,4-transferase | - |
Saccharolobus solfataricus |
TreX | - |
Saccharolobus solfataricus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
40 | - |
assay at | Saccharolobus solfataricus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
5.5 | - |
assay at | Saccharolobus solfataricus |