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Updated: Jun 5, 2026

Defining Substrate Specificities for Lipase and Phospholipase Candidates
Published on: November 23, 2016
Discrimination between the regioisomeric 1,2- and 1,3-diacylglycerophosphocholines by phospholipases
Johanna Mansfeld1, Wolfgang Brandt, Regine Haftendorn
1Institute of Biochemistry and Biotechnology, Martin-Luther University Halle-Wittenberg, Saale, Kurt-Mothes, Germany. mansfeld@biochemtech.uni-halle.de
Abstract:
The artificial 1,3-diacyl-glycero-2-phosphocholines (1,3-PCs), which form similar aggregate structures as the naturally occurring 1,2-diacyl-sn-glycero-3-phosphocholines (1,2-PCs), were tested as substrates for different classes of phospholipases such as phospholipase A(2) (PLA(2)) from porcine pancreas, bee and snake venom, and Arabidopsis thaliana, phospholipase C (PLC) from Bacillus cereus, and phospholipase D (PLD) from cabbage and Streptomyces species. The regioisomers of the natural phospholipids were shown to bind to all investigated phospholipases with an affinity similar to the corresponding naturally occurring phospholipids, however their hydrolysis was reduced to different degrees (PLA(2)s and PLC) or even abolished (PLDs belonging to the PLD superfamily). The results are in accordance with binding models obtained by docking the substrates to the crystal structures or homology models of the phospholipases.
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