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Literature summary for 4.2.1.20 extracted from
- Structures of wild-type and P28L/Y173F tryptophan synthase alpha-subunits from Escherichia coli (2004), Biochem. Biophys. Res. Commun., 323, 1257-1264.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| crystal structures of wild-type and mutant P38L/Y173F alpha-subunit, 2.8 A and 1.8 A resolution, hanging-drop vapour diffusion method | Escherichia coli |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| P38L/Y173F | P28L substitution induces the exposure of hydrophobic amino acids and decreases the secondary structure that causes the aggregation. The Y173E mutation suppresses to transfer a signal from the alpha-subunit core to the alpha-subunit surface involved in interactions with the beta-subunit and increases structural stability | Escherichia coli |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | P0A877 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Escherichia coli |
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Release 2023.1 (January 2023)
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