Triacylglycerol lipase (Propionibacterium acnes) (GehA)

Triacylglycerol lipase, specifically the GehA enzyme secreted by Propionibacterium acnes (now Cutibacterium acnes), is a key virulence factor in the pathogenesis of acne vulgaris (UniProt P0C0Y1). This enzyme catalyzes the hydrolysis of sebum triglycerides into glycerol and pro-inflammatory free fatty acids (FFAs) (PubMed: 10852371). These FFAs damage the follicular wall and recruit inflammatory cells, leading to the characteristic papules and pustules of acne (StatPearls: Acne Vulgaris). Beyond its inflammatory role, the lipase supports bacterial survival and colonization within the lipid-rich environment of the pilosebaceous unit (NCBI: PMC3535073). Many standard acne treatments, including tetracyclines and macrolides, exert their therapeutic effects partly by inhibiting the production and activity of this lipase (PubMed: 6223450). Consequently, this enzyme is a significant target for both antimicrobial and anti-inflammatory dermatological interventions.

Other names

Glycerol ester hydrolaseLipase ACutibacterium acnes lipaseP. acnes lipase

Inhibition of lipase enzyme secretion and catalytic activity, resulting in reduced levels of pro-inflammatory free fatty acids on the skin surface.