Zinc finger DHHC-type palmitoyltransferase 20 (ZDHHC20)

Zinc finger DHHC-type palmitoyltransferase 20 (ZDHHC20) is an integral membrane enzyme responsible for the covalent attachment of palmitate or other long-chain fatty acids onto substrate proteins via a thioester linkage, a process known as S-palmitoylation[1][3][5]. ZDHHC20 contains a characteristic DHHC (Asp-His-His-Cys) cysteine-rich domain, coordinating zinc ions crucial for structural integrity, and features four transmembrane helices forming a lipid-binding cavity that determines acyl chain selectivity[1][3][4]. Its catalytic activity relies on a two-step mechanism, involving first autopalmitoylation on the DHHC cysteine and then transfer of the palmitoyl group to the substrate protein. ZDHHC20 is localized mainly in the plasma membrane and Golgi apparatus[3][5], with activities implicated in regulating membrane protein function, viral protein modification, and possibly other cellular processes. Inhibition of ZDHHC20 can block palmitoylation-dependent functions, and its specificity is structurally defined by the residues composing its substrate cavity[1][4].

Other names

Palmitoyltransferase ZDHHC20DHHC20FLJ25952Acyltransferase ZDHHC20DHHC domain-containing cysteine-rich protein 20Zinc finger DHHC domain-containing protein 204933421L13RikDHHC-20ZDHHC Palmitoyltransferase 20

Inhibition of protein S-palmitoylation (by covalent modification or blocking of the DHHC cysteine catalytic site)[1]