Researchers at the Eunice Kennedy Shriver National Institute of Child Health and Human Development (NICHD) recently isolated and identified the physical makeup of DHHC enzymes (palmitoyltransferases), which alter other proteins by connecting them to lipid (fatty acid) chains of assorted lengths, a modification known as palmitoylation that has the capacity to alter target protein characteristics.
NICHD researchers affiliated with the National Institutes of Health (NIH) mapped out what they call the first three-dimensional structure representing DHHC proteins with the aim of providing a template for therapeutic treatment formulation, an HIH release said. They have postulated that by blocking DHHC activity, cancer treatments may become more effective; but no currently authorized regimens exist that could mitigate DHHC enzyme activity.
“Mutations in DHHC enzymes are associated with various cancers and neurological disorders,” Anirban Banerjee, lead author of NICHD’s recent study examining DHHC enzyme structure, said in the release. “Our study offers a starting point for developing … inhibitors that may aid in treatment of common cancers and advance the field of protein palmitoylation.”
Banerjee and his team discovered that a part of DHHC20 affects its lipid chain length, which in turn impacts the attachment of fatty acids such as palmitic acid to a targeted protein.
In addition to the newly gained understanding, the team’s work may also serve to inform scientists how multiple enzymes work together, the release said.