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Literature summary for 3.4.21.50 extracted from
- Crystallization and preliminary crystallographic analysis of Achromobacter protease I mutants (2010), Acta Crystallogr. Sect. F, 66, 1531-1532.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| mutants H210S and W169F, to 2.0 and 2.3 A resolution, respectively | Achromobacter lyticus |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| H210S | crystallization data. Optimum pH value shifts from around pH 9 of wild-type to approximately pH 7, while retaining high activity | Achromobacter lyticus |
| W169F | crystallization data. Optimum pH value shifts from around pH 9 of wild-type to approximately pH 7, while retaining high activity | Achromobacter lyticus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Achromobacter lyticus | P15636 | - |
- |
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