Functional characterization of TMEM86A and TMEM86B mutants by a novel lysoplasmalogenase assay.

ABSTRACT: Plasmalogens are an abundant class of glycero-phospholipids with a characteristic 1-O-alk-1'-enyl double bond. While their synthesis has been extensively investigated, their degradation remains understudied. Plasmalogen deficiencies are associated with severe disorders in humans and interfering with their degradation would be a treatment option, but it remains out of reach due to limited knowledge. The plasmalogen double bond is degraded either directly by a plasmalogenase or by conversion to the 2' lyso forms by phospholipase and subsequent cleavage by lysoplasmalogenase (E.C. 3.3.2.2). Two lysoplasmalogenases are known so far, TMEM86A and TMEM86B. While TMEM86B has been expressed in bacteria, purified, and shown to encode lysoplasmalogenase activity by a coupled optical assay, the closel

SUBMITTER: Kummer D 

PROVIDER: S-EPMC11994398 | biostudies-literature | 2025 Apr

REPOSITORIES: biostudies-literature