Cellular exposure to propachlor inhibits PARK7's ability to deglycate damaged proteins, offering an alternative mechanism by which propachlor exposure can induce protein misfolding beyond direct modification. We speculate that it could be beneficial to the cell that GAPDH is inhibited in concert with PARK7, preventing accumulation of glycating equivalents when the detoxification mechanism is also inhibited. Due to poor reproducibility for profiling the active C106 in PARK7, we were not able to compare whether PARK7 C106 and GAPDH C152 are similarly modified across the range of chloroacetamides investigated in the reported high throughput screen . For the three chloroacetanilides in our present study, however, the relationship holds (Figure ).