Plasmanylethanolamine desaturase 1 (PEDS1)

Plasmanylethanolamine desaturase 1 (PEDS1) is an integral membrane enzyme encoded by the TMEM189 gene, best known for catalyzing the final step in plasmalogen biosynthesis—specifically introducing the 1-O-alk-1′-enyl double bond that creates the characteristic vinyl ether linkage in plasmalogen lipids[3][4][5]. This activity is dependent on a conserved motif of histidine residues and requires a di-iron center for function, typical of lipid desaturases[2][3][4]. PEDS1 is widely expressed, highly evolutionarily conserved, and essential for proper membrane lipid structure, impacting physical properties such as membrane fluidity and organization as well as cell signaling and antioxidative protection[4]. Dysfunction of PEDS1 is associated with pathologies such as cancer and neurodegenerative diseases, partly because abnormal plasmalogen levels are linked to these conditions[4][5]. Recent research has also uncovered a regulatory role for TMEM189/PEDS1 in autophagy through modulation of ULK1 kinase stability and turnover[1]. While no specific drugs are currently reported to directly interact with PEDS1, alterations in plasmalogen biosynthesis and PEDS1 activity may influence cell survival pathways, particularly in the context of ferroptosis and oxidative stress[1][4].

Other names

Transmembrane protein 189TMEM189KUACarF homologCarFPEDS