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Literature summary for 5.4.99.15 extracted from
- Crystallization and improvement of crystal quality for X-ray diffraction of maltooligosyl trehalose synthase by reductive methylation of lysine residues (1999), Acta Crystallogr. Sect. D, 55, 931-933.
No PubMed abstract available
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| hanging-drop vapour-diffusion method at 4°C. The chemical modification of this enzyme by reductive methylation of lysine residues significantly improves the crystal quality for X-ray diffraction experiments. The crystals of the modified enzyme belong to orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 56.70, b = 140.1, c = 205.2 A measured at cryo-temperature, and are found to contain two enzyme molecules per asymmetric unit | Sulfolobus acidocaldarius |
| recombinant enzyme expressed in Escherichia coli, hanging-drop vapour-diffusion method, chemical modification of this enzyme by reductive methylation of lysine residues significantly improves the crystal quality for X-ray diffraction experiments | Sulfolobus acidocaldarius |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Sulfolobus acidocaldarius | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Sulfolobus acidocaldarius |
| recombinant enzyme expressed in Escherichia coli | Sulfolobus acidocaldarius |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| alpha-maltotriosyl trehalose | - |
Sulfolobus acidocaldarius | maltopentaose | - |
? |  |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| maltooligosyl trehalose synthase | - |
Sulfolobus acidocaldarius |
| MTSase | - |
Sulfolobus acidocaldarius |
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Release 2023.1 (January 2023)
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