Fig. 2

εPKC phosphorylation on wild type ALDH2, ALDH2*2 and Thr185, Ser279 and Thr412 mutant enzymes. a Increased activity for wild type ALDH2 and ALDH2*2 mutant enzymes by εPKC phosphorylation. ALDH2 wild type (WT) and ALDH2*2 mutant enzyme activities were measured in the absence or presence of εPKC. Enzyme activity was expressed in μmole NADH/min/μg recombinant protein (n = 3, **p < 0.001; bars represent the mean ± SD). b Enzymatic active of the phosphomimetic ALDH2 site-directed mutants, T185E, S279E and T412E. Enzyme activity was expressed in μmole NADH/min/μg recombinant protein (n = 3, *p < 0.05, **p < 0.001 vs. WT; bars represent the mean ± SD). c A structural analysis of the T185E mutation reveals that a glutamate in the position of T185 would clash with the surrounding amino acids, proline 181 and threonine 486. d The effect of εPKC phosphorylation on the phosphomimetic and non-phosphorylatable mutants of ALDH2. The graph displays the enzyme activity of T185, S279 and T412 mutants with or without the phosphorylation of εPKC (n = 3, *p < 0.05, **p < 0.001; bars represent the mean ± SD)