Any feedback?
Literature summary for 3.1.4.4 extracted from
- Behaviour of a recombinant cabbage (Brassica oleracea) phospholipase D immobilized on CNBr-activated and antibody supports (2004), Biotechnol. Appl. Biochem., 40, 95-99.
General Stability
| General Stability | Organism |
|---|---|
| binding of PLD2 to the antibody support renders the enzyme remarkably labile to high temperatures and storage | Brassica oleracea |
| coupling of PLD2 to CNBr-activated Sepharose results in significant improvement in storage stability without affecting its thermostability, as compared with the soluble enzyme | Brassica oleracea |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| additional information | phospholipase D2 immobilized covalently on CNBr-activated Sepharose expresses 10% of the activity of the soluble enzyme, the enzyme immobilized by binding on to anti-PLD2 IgG-Sepharose show 38% of the activity of the soluble enzyme | Brassica oleracea |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Brassica oleracea | - |
recombinant | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Brassica oleracea |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| phospholipase D2 | - |
Brassica oleracea |
| PLD2 | - |
Brassica oleracea |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
