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. Author manuscript; available in PMC: 2016 Mar 30.
Published in final edited form as: J Eukaryot Microbiol. 2009 Dec 18;57(1):11–18. doi: 10.1111/j.1550-7408.2009.00458.x

Fig. 7.

Fig. 7

Schematic diagram of Entamoeba histolytica alcohol dehydrogenase 2 (EhADH2). The enzymatic activities reside in two separate, interacting domains: N-terminal aldehyde dehydrogenase (ALDH) and C-terminal alcohol dehydrogenase (ADH) (catalytic residues: Cys252 and His754, respectively). Conserved amino acids essential for each domain’s function are shown; the iron-binding region in ADH is crucial for Eh-ADH2 activity and interaction between domains (Espinosa et al. 2001, 2009).