ZDHHCenzymer

ZDHHC enzymes, also known as palmitoyltransferases, are a family of integral membrane proteins that catalyze the palmitoylation of other proteins. Palmitoylation is a post-translational modification where a palmitate group, a type of fatty acid, is covalently attached to a cysteine residue. This lipidation process can affect protein localization, stability, function, and interactions.

The ZDHHC enzyme family is characterized by a conserved cysteine-rich domain (CRD) that contains the catalytic cysteine residue essential for palmitoylation. This domain is part of a larger catalytic domain that also includes histidine and aspartate residues. The enzymes are typically found embedded in the membranes of the endoplasmic reticulum, Golgi apparatus, and plasma membrane, reflecting the diverse locations of their substrate proteins.

There are over 20 known ZDHHC enzymes in humans, each exhibiting some degree of substrate specificity. They play crucial roles in a wide array of cellular processes, including signal transduction, protein trafficking, and membrane protein regulation. Dysregulation of ZDHHC enzyme activity has been implicated in various diseases, such as cancer, neurological disorders, and cardiovascular diseases, making them targets of ongoing research. Understanding the specific functions and substrates of individual ZDHHC enzymes is an active area of investigation in cell biology and biochemistry.