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Literature summary for 3.2.1.157 extracted from
- The iota-carrageenase of Alteromonas fortis. A beta-helix fold-containing enzyme for the degradation of a highly polyanionic polysaccharide (2001), J. Biol. Chem., 276, 40202-40209.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| native and selenomethionyl-iota-carrageenase. Single crystals are obtained with polyethylene glycol, and the presence of Ca2+ appears to be crucial for crystallization. High quality crystals, typically 0.25 * 0.25 * 0.15 mM in dimension are grown with 0.1 M sodium cacodylate at pH 6.5, 15-17% polyethylene glycol and 200 mM calcium acetate. Crystallization of Se-Met-iota-carrageenase is performed under similar conditions except for the addition of 1 mM dithiothreitol and the replacement of sodium cacodylate by imidazole to avoid the reaction between cacodylate and dithiothreitol. Crystal structure at 1.6 A resolution | Alteromonas fortis |
General Stability
| General Stability | Organism |
|---|---|
| enzyme contains three calcium binding sites involved in stabilizing the enzyme structure | Alteromonas fortis |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Ca2+ | enzyme contains three calcium binding sites involved in stabilizing the enzyme structure | Alteromonas fortis |  |
| Na+ | the protein contains one sodium and one chloride binding site | Alteromonas fortis | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Alteromonas fortis | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Alteromonas fortis |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| iota-carrageenase | - |
Alteromonas fortis |
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Release 2023.1 (January 2023)
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