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P8398

Sigma-Aldrich

Phospholipase D from cabbage

Type IV, lyophilized powder, ≥100 units/mg solid

Synonym(s):

Lecithinase D, Phosphatidylcholine phosphatidohydrolase, Phospholipase D from white cabbage

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About This Item

CAS Number:
Enzyme Commission number:
EC Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

type

Type IV

form

lyophilized powder

specific activity

≥100 units/mg solid

composition

Protein, ~25%

storage temp.

−20°C

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General description

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.

Application

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.

Biochem/physiol Actions

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.

Unit Definition

One unit will liberate 1.0 μmol of choline from L-α-phosphatidylcholine (egg yolk) per hr at pH 5.6 at 30 °C.

Analysis Note

Protein determined using biuret.

Pictograms

Health hazard

Signal Word

Danger

Hazard Statements

Precautionary Statements

Hazard Classifications

Resp. Sens. 1

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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T T Allgyer et al.
Biochemistry, 18(24), 5348-5353 (1979-11-27)
Phospholipase D has been purified 680-fold from an acetone powder of savoy cabbage in an overall yield of 30%. The purification involves solubilization of the acetone powder in a Ca2+-containing buffer and subsequent ammonium sulfate fractionation. Gel filtration on Sephadex
D U Kim et al.
Biochimica et biophysica acta, 1437(3), 409-414 (1999-04-02)
We cloned and expressed a full-length cDNA encoding a phospholipase D of type alpha (PLDalpha) from cabbage. Analysis of the cDNA predicted an 812-amino-acid protein of 92.0 kDa. The deduced amino acid sequence of cabbage PLD has 83% and 80%
Alexandra Lerchner et al.
Protein engineering, design & selection : PEDS, 19(10), 443-452 (2006-07-18)
In addition to hydrolysis of glycerophospholipids, phospholipases D (PLDs) catalyze the head group exchange. The molecular basis of this transphosphatidylation potential, which strongly varies for PLDs from different sources, is unknown hitherto. Recently, the genes of two PLD isoenzymes from
Cindy Y Jao et al.
Proceedings of the National Academy of Sciences of the United States of America, 106(36), 15332-15337 (2009-08-27)
Choline (Cho)-containing phospholipids are the most abundant phospholipids in cellular membranes and play fundamental structural as well as regulatory roles in cell metabolism and signaling. Although much is known about the biochemistry and metabolism of Cho phospholipids, their cell biology
Susanne Stumpe et al.
The FEBS journal, 274(10), 2630-2640 (2007-04-25)
Phospholipases D play an important role in the regulation of cellular processes in plants and mammals. Moreover, they are an essential tool in the synthesis of phospholipids and phospholipid analogs. Knowledge of phospholipase D structures, however, is widely restricted to

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