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. Author manuscript; available in PMC: 2014 Feb 25.
Published in final edited form as: Chem Biol Interact. 2012 Dec 13;202(0):11–21. doi: 10.1016/j.cbi.2012.11.022

Fig. 4.

Fig. 4

Comparative amino acid sequences alignments for ALDH2 and ALDH1B1 subunit binding domains. See Tables 1 and 2 for sources of ALDH1B1 and ALDH2 sequences, respectively. Three regions for vertebrate ALDH2 and ALDH1B1 sequences are shown, including dimer–dimer (β5); NAD+ binding site, monomer–monomer αG and β18, and monomer–monomer (β19). Amino acid residues are color coded: yellow for P (proline); green for hydrophilic amino acids, S (serine), Q (glutamine), N (asparagine), and T (threonine); brown for glycine (G); light blue for hydrophobic amino acids, L (leucine), I (isoleucine), V (valine), M (methionine), W (tryptophan); dark blue for amino acids, T (tyrosine) and H (histidine); purple for acidic amino acids, E (glutamate) and D (aspartate); and red for basic amino acids, K (lysine) and R (arginine). The site of the ALDH2*2 variant (E487K) is identified by the arrow.