Abstract 2595 A spastic paraplegia-related DDHD2 functions as a lipase and transacylase that can remodel the acyl-chains of triglycerides
Objective: This study aims to elucidate the substrate specificity of DDHD2 as a lipase towards phospholipids and neutral lipids, and to define its molecular mechanisms to enhance our understanding of this enzyme's function. Methods: We employed protein purification, enzyme activity assays, liposome co-sedimentation assays and liquid chromatography-mass spectrometry (LC-MS) to investigate DDHD2's substrate specificity and enzymatic mechanisms. Results: DDHD2 exhibited a marked preference for hydrolyzing diacylglycerol (DAG) over phospholipids.
Authors
- Abdou Thiam
- Yong‐Mi Choi (ORCID: https://orcid.org/0000-0002-5776-3602)
- Daniel Canals (ORCID: https://orcid.org/0000-0002-9293-5123)
- Michael V. Airola (ORCID: https://orcid.org/0000-0003-4981-1253)
- Lingshuang Wu
Institutions
- Bridge University (SS)
Publication Details
- Journal
- Journal of Biological Chemistry
- Published
- 2025-05-01
- DOI
- https://doi.org/10.1016/j.jbc.2025.109440
- Primary Topic
- Hereditary Neurological Disorders
- Type
- article
- Field-Weighted Citation Impact
- 0.00
Funders
- National Institutes of Health