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Literature summary for 2.4.1.7 extracted from
- Adsorption and enzyme activity of sucrose phosphorylase on lipid Langmuir and Langmuir-Blodgett films (2014), Colloids Surf. B Biointerfaces, 116, 497-501.
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | adsorption and enzyme activity of sucrose phosphorylase on lipid Langmuir and Langmuir-Blodgett films with negligible effects on its secondary structure, but providing a favorable environment for preserving the enzyme catalytic activity, attributed to the interaction of the polypeptide structure with the hydrophobic tails of phospholipid dimyristoylphosphatidic acid, thereby facilitating the access of the analyte to the catalytic site of the enzyme, which is ideal for catalyzing the conversion of sucrose to other products, overview | Leuconostoc mesenteroides |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Leuconostoc mesenteroides | - |
- |
- |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| commercial preparation | - |
Leuconostoc mesenteroides | - |
General Information
| General Information | Comment | Organism |
|---|---|---|
| additional information | adsorption and enzyme activity of sucrose phosphorylase on lipid Langmuir and Langmuir-Blodgett films with negligible effects on its secondary structure, but providing a favorable environment for preserving the enzyme catalytic activity, attributed to the interaction of the polypeptide structure with the hydrophobic tails of phospholipid dimyristoylphosphatidic acid, thereby facilitating the access of the analyte to the catalytic site of the enzyme, which is ideal for catalyzing the conversion of sucrose to other products, overview | Leuconostoc mesenteroides |
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