Several enzymes with active cysteines prone to electrophilic modification had significantly greater affinity for DNAJB8 H31Q after acetochlor exposure. Thymidylate Synthase (TYMS) (Fold Change = 3, q value = .003), an enzyme essential for production of thymidine nucleotides , has an active site cysteine that is specifically targeted by an electrophilic chemotherapeutic drug . Another protein with significantly increased Hsp40 affinity following acetochlor treatment is eukaryotic translation initiation factor 3 subunit E (eIF3e) (Fold Change = 1.96, q value = .0004) which plays a role in tumor growth and the hypoxia response . Acetyl-CoA acetyltransferase 1 (ACAT1; Fold change = 2.91, q value = .02) was significantly destabilized, consistent with its multiple reactive cysteines . It's possible that adduct formation could stabilize rather than destabilize a protein, leading to a decrease in Hsp40 affinity. Choline /ethanolaminephosphotransferase 1 (CEPT1) and microsomal glutathionine Stransferase 3 (MGST3) bind less to DNAJB8 H31Q after treatment, indicating stabilization.