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Literature summary for 3.5.1.1 extracted from
- Crystal structure and allosteric regulation of the cytoplasmic Escherichia coli L-asparaginase I (2007), J. Mol. Biol., 369, 794-811.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
- |
Escherichia coli |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| R240A | mutation increases the [S]0.5 value to 5.9 mM, presumably by reducing the affinity of the site for L-asparagine, although the enzyme retains cooperativity | Escherichia coli |
| T162A | mutation results in an active enzyme with no cooperativity | Escherichia coli |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| cytoplasm | - |
Escherichia coli | 5737 | - |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| AnsA | - |
Escherichia coli |
| L-asparaginase I | - |
Escherichia coli |
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Release 2023.1 (January 2023)
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