Table 3 Difference between C112 and C146 residues in RPE65 protein.
From: The dual roles of RPE65 S-palmitoylation in membrane association and visual cycle function
| Â | Cysteine 112 (C112) | Cysteine 146 (C146) |
|---|---|---|
Residue location in the 3-D structure | located in surface-exposed highly mobile loop | located in hydrophobic substrate-binding cleft |
MS-coupled acyl exchange labeling identified modification | ±Palmitoylation (shows NEM and 4-VP modification) | +Palmitoylation (only 4-VP modification) |
Membrane binding of RPE65 | significantly affect membrane binding | No role in membrane binding |
Catalytic activity of RPE65 | mutation abolishes activity | mutation reduces activity |
Proposed source of palmitoyl moiety | DHHC38 -mediated palmitoylation using palmitoyl-CoA | Substrate mediated palmitoylation |
