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Literature summary for 4.2.2.1 extracted from
- Role of ionic interactions and linker in the domain interaction and modulation of functional activity of hyaluronate lyases (2007), Biochem. Biophys. Res. Commun., 353, 286-292.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| cloning, overexpression and purification of the C-terminal domain swapped chimeras of SpnHL and SagHL (hyaluronate lyase from Streptococcus agalactiae), modified enzyme SpnHLv/SagHLv (where the size of linker connecting the alpha-domain to C-terminal domain is enlarged by two amino acid) | Streptococcus pneumoniae |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | C-terminal domain swapped chimeras of SpnHL and SagHL, modified enzyme SpnHLv/SagHLv (where the size of linker connecting the alpha-domain to C-terminal domain is enlarged by two amino acid) | Streptococcus pneumoniae |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | Km-values of C-terminal domain swapped chimeras of SpnHL and SagHL, modified enzyme SpnHLv/SagHLv (where the size of linker connecting the alpha-domain to C-terminal domain is enlarged by two amino acid) | Streptococcus pneumoniae |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Streptococcus pneumoniae | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| cloning, overexpression and purification of the C-terminal domain swapped chimeras of SpnHL and SagHL, modified enzyme SpnHLv/SagHLv (where the size of linker connecting the alpha-domain to C-terminal domain is enlarged by two amino acid) | Streptococcus pneumoniae |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | C-terminal domain does not bind directly to the substrate, instead the domain contributes to the interaction with the polymeric hyaluronan for catalysis. Furthermore, the substrate specificity exchanges with the size of catalytic cleft. The role of linker connecting alpha-domain to C-terminal domain is found to hold the C-terminal domain in a conformation suitable for achieving maximum activity | Streptococcus pneumoniae | ? | - |
? |  |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| spnHL | - |
Streptococcus pneumoniae |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | turnover numbers of C-terminal domain swapped chimeras of SpnHL and SagHL, modified enzyme SpnHLv/SagHLv (where the size of linker connecting the alpha-domain to C-terminal domain is enlarged by two amino acid) | Streptococcus pneumoniae |
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