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Updated: Jun 13, 2025

Defining Substrate Specificities for Lipase and Phospholipase Candidates
Published on: November 23, 2016
VWA7 - A Putative Human Phosphatidylcholine-specific Phospholipase C.
Alexander Klipp1, Christina Greitens1, Jean-Christophe Leroux1
1Institute of Pharmaceutical Sciences, Department of Chemistry and Applied Biosciences, ETH Zürich, Vladimir-Prelog-Weg 1-5/10, 8093 Zürich, Switzerland.
Researchers identified human von Willebrand factor A domain-containing protein 7 (VWA7) as a potential phosphatidylcholine-specific phospholipase C (pc-PLC). Biochemical analysis confirmed VWA7
Area of Science:
- Biochemistry
- Molecular Biology
- Enzymology
Background:
- The existence of mammalian phosphatidylcholine-specific phospholipase C (pc-PLC) has been known for over 40 years.
- The specific gene encoding this mammalian enzyme has remained elusive until now.
Purpose of the Study:
- To identify the gene responsible for mammalian pc-PLC activity.
- To characterize the biochemical function and properties of the putative pc-PLC enzyme.
Main Methods:
- Structural comparison of human VWA7 with known bacterial pc-PLC.
- Investigation of VWA7 localization and activity in mammalian cells.
- Expression and activity assays of VWA7 variants in bacteria.
Main Results:
- Human VWA7 shares significant structural similarity with Bacillus cereus pc-PLC, including a conserved active site.
- pc-PLC activity was confirmed for bacterial VWA7 variants, with specific activity reaching up to 733 mU/mg.
- VWA7 variants demonstrated activity in mammalian cells, supporting its role as human pc-PLC.
Conclusions:
- Human von Willebrand factor A domain-containing protein 7 (VWA7) is identified as the putative pc-PLC.
- These findings provide biochemical evidence for VWA7's enzymatic activity and pave the way for further research.
- This study establishes a foundation for understanding the role of human pc-PLC and the VWA7 protein.
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