Phospholipase D (PLD) from cabbage comprises the C2 domain, PLD superfamily specific conserved regions (I–IV) with HxKx4Dx6GSxN (HKD) motif. Structurally, it is a barrel-shaped monomer bound to calcium ions.
Phospholipase D (PLD) is used to hydrolyze the phosphate bonds of phospholipids and sphingomyelin to give the corresponding phosphatidic acid. It has also been used to study metabolic labeling and direct imaging of choline phospholipids in vivo by measuring propargyl-Cho incorporation. Furthermore, PLD is used in purification and kinetic studies.
The enzyme has been used for the preparation of Bodipy-phosphatidylcholine during the preparation of fluorescently labelled lipids.
500 units in glass bottle
2500 units in poly bottle
Phospholipase D from cabbage is widely used in biocatalytic transphosphatidylation reactions.
The amino acid sequence of cabbage PLD has 83% and 80% identity with Arabidopsis PLDα and castor bean PLD. It hydrolyzes the phosphate bonds of phospholipids and sphingomyelin to give the corresponding phosphatidic acid.
Hydrolyzes the phosphate bonds of phospholipids and sphingomyelin to give the corresponding phosphatidic acid.
One unit will liberate 1.0 μmol of choline from L-α-phosphatidylcholine (egg yolk) per hr at pH 5.6 at 30 °C.
Protein determined using biuret.