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In molecular biology, palmitoylation is the covalent attachment of fatty acids, such as palmitic acid, to cysteine (S-palmitoylation) and less frequently to serine and threonine (O-palmitoylation) residues of proteins, which are typically membrane proteins. [2] The precise function of palmitoylation depends on the particular protein being ...
palmitoylation (a type of acylation), attachment of palmitate, a C 16 saturated acid; isoprenylation or prenylation, the addition of an isoprenoid group (e.g. farnesol and geranylgeraniol) farnesylation; geranylgeranylation; glypiation, glycosylphosphatidylinositol (GPI) anchor formation via an amide bond to C-terminal tail
The protein palmitoylation is a reversible process. The addition of palmitoyl group increase the membrane association of the substrate protein while the removal by palmitoyl thioesterase decreases the membrane association.
In palmitoleoylation, a palmitoleoyl group (derived from palmitoleic acid, pictured above) is added.. Palmitoleoylation is type of protein lipidation where the monounsaturated fatty acid palmitoleic acid is covalently attached to serine or threonine residues of proteins.
PPT-1 a member of the palmitoyl protein thioesterase family. PPT-1 is a small glycoprotein involved in the catabolism of lipid-modified proteins during lysosomal degradation. This enzyme removes thioester -linked fatty acyl groups such as palmitate from cysteine residues.
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Some members of the family such as ZDHHC3 and ZDHHC7 enhance palmitoylation of proteins such as PSD-95, SNAP-25, GAP43, Gαs. Others such as ZDHHC9 showed specificity only toward the H-Ras protein. [3] However, a recent study questions the involvement of classical enzyme-substrate recognition and specificity in the palmitoylation reaction. [4]
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