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Literature summary for 4.2.2.1 extracted from
- Insights into the mechanism of action of hyaluronate lyase: role of C-terminal domain and Ca2+ in the functional regulation of enzyme (2006), J. Biol. Chem., 281, 28336-28344.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| cloning overexpression, and purification of SagHL and its different fragments/domains | Streptococcus agalactiae |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| additional information | calcium ions do not interact with the enzyme, and its role actually is in modulating the hyaluronan conformation and not in the functional regulation of enzyme | Streptococcus agalactiae |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 92000 | - |
gel filtration | Streptococcus agalactiae |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Streptococcus agalactiae | Q53591 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| cloning overexpression, and purification of SagHL and its different fragments/domains | Streptococcus agalactiae |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| SagHL | - |
Streptococcus agalactiae |
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Release 2023.1 (January 2023)
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