The enzyme catalyses the posttranslational protein palmitoylation that plays a role in protein-membrane interactions, protein trafficking, and enzyme activity. Palmitoylation increases the hydrophobicity of proteins or protein domains and contributes to their membrane association.
The enzyme catalyses the posttranslational protein palmitoylation that plays a role in protein-membrane interactions, protein trafficking, and enzyme activity. Palmitoylation increases the hydrophobicity of proteins or protein domains and contributes to their membrane association.
DHHC3 has a broad protein substrate specificity, but only myristoyl-, palmitoyl-, and palmioleoyl-CoA are effective, and longer acyl-CoAs compete less well. The acyl-CoA chain length specificity of DHHC enzyme autoacylation parallels substrate specificity, overview
bound in the cysteine-rich domain. Treatment of isoform DHHC3 with chelating agents in vitro leads to specific structural perturbations and activity deficits also observed in conserved cysteine mutants. The stoichiometry of zinc binding is 2 mol of zinc/mol of DHHC3 protein
mice homozygous for DHHC5, are born at half the expected rate, and survivors show a marked deficit in contextual fear conditioning, an indicator of defective hippocampal-dependent learning. DHHC5 is highly enriched in a post-synaptic density preparation and co-immunoprecipitates with post-synaptic density protein PSD-95, an interaction that is mediated through binding of the carboxyl terminus of DHHC5 and the PDZ3 domain of PSD-95
isoform DHHC5 palmitoylates cardiac phosphoprotein phospholemman at two juxtamembrane cysteines, C40 and C42. Phospholemman interaction with and palmitoylation by DHHC5 is independent of the DHHC5 PSD-95/Discslarge/ZO-1 homology binding motif, but requires an about 120 amino acid region of the DHHC5 intracellular C-tail immediately after the fourth transmembrane domain. Phospholemman mutant C42A but not phospholemman mutant C40A inhibits the cardiac Na pump
mutation of highly conserved cysteine residue of the cysteine-rich domain, results in activity deficits and a structural perturbation. About 10% of wild-type activity
mutation of highly conserved cysteine residue of the cysteine-rich domain, results in activity deficits and a structural perturbation. Less than 5% of wild-type activity
mutation of highly conserved cysteine residue of the cysteine-rich domain, results in activity deficits and a structural perturbation. About 15% of wild-type activity. Mutation reduces the palmitoylation level of DHHC3