Regulation of DGKε Activity and Substrate Acyl Chain Specificity by Negatively Charged Phospholipids.

ABSTRACT: Diacylglycerol kinase ε (DGKε) is a membrane-bound enzyme that catalyzes the ATP-dependent phosphorylation of diacylglycerol to form phosphatidic acid (PA) in the phosphatidylinositol cycle. DGKε lacks a putative regulatory domain and has recently been reported to be regulated by highly curved membranes. To further study the effect of other membrane properties as a regulatory mechanism of DGKε, our work reports the effect of negatively charged phospholipids on DGKε activity and substrate acyl chain specificity. These studies were conducted using purified DGKε and detergent-free phospholipid aggregates, which present a more suitable model system to access the impact of membrane physical properties on membrane-active enzymes. The structural properties of the different model membranes were st

SUBMITTER: Bozelli JC 

PROVIDER: S-EPMC7036746 | biostudies-literature | 2020 Feb

REPOSITORIES: biostudies-literature