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Literature summary for 3.1.8.1 extracted from
- Enhanced activity and stability of organophosphorus hydrolase via interaction with an amphiphilic polymer (2014), Chem. Commun. (Camb. ), 50, 5345-5348.
Application
| Application | Comment | Organism |
|---|---|---|
| degradation | activity and stability of organophosphorus hydrolase are enhanced by interactions between the hydrophobic poly(propylene oxide) block of amphiphilic Pluronics and the enzyme. The strategy provides an efficient route to new formulations for decontaminating organophosphate neurotoxins | Brevundimonas diminuta |
General Stability
| General Stability | Organism |
|---|---|
| the hydrophobic poly(propylene oxide) blocks of Pluronic interact with hydrophobic amino acids of the enzyme, resulting in an increased activity and pot life for dilute concentrations, methanol inhibition, enhanced stability against high temperature, and extended shelf life | Brevundimonas diminuta |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Brevundimonas diminuta | - |
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