Cytochrome P450 5218 (Malassezia globosa) (CYP5218)

CYP5218 (also known as MGL_5218) is a cytochrome P450 enzyme identified in the genome of Malassezia globosa, a lipophilic yeast that is a primary causative agent of common human skin conditions such as dandruff and seborrheic dermatitis. Unlike most other fungi, Malassezia species lack the genetic machinery to synthesize fatty acids de novo and must rely on the uptake and metabolism of host-derived lipids from sebum. CYP5218 belongs to the CYP52 family, which typically functions in the hydroxylation of fatty acids and alkanes, making it a vital component of the yeast's specialized metabolic pathways for processing external lipids. This enzyme is considered an investigational therapeutic target for the development of novel antifungal agents, as its inhibition could disrupt the essential lipid processing required for the yeast's survival and pathogenicity on the skin surface. While traditional azole antifungals primarily target lanosterol 14-alpha demethylase (CYP51), research into CYP5218 aims to identify more selective inhibitors that could provide more effective management of Malassezia-related disorders with reduced potential for off-target effects.

Other names

MGL_5218Cytochrome P450 family 52 memberMalassezia globosa P450

Inhibition of fungal lipid metabolism and fatty acid hydroxylation, leading to disruption of membrane integrity and yeast survival.