Structural analysis of the acetaldehyde dehydrogenase activity of Entamoeba histolytica alcohol dehydrogenase 2 (EhADH2), a member of the ADHE enzyme family

Molecular and Biochemical Parasitology
Minghe ChenSamuel L Stanley

Abstract

The ADHE family of enzymes are bifunctional acetaldehyde dehydrogenase (ALDH)/alcohol dehydrogenase (ADH) enzymes that probably arose from the fusion of genes encoding separate ALDH and ADH enzymes. Here we have used the Entamoeba histolytica alcohol dehydrogenase 2 (EhADH2) enzyme as a prototype to analyze the structure and function of the ALDH domain of ADHE enzymes. We find that the N-terminal domain of EhADH2, encompassing amino acids 1-446, is sufficient for ALDH activity, consistent with the concept that EhADH2, and other members of the ADHE family comprise fusion peptides. In addition, we show, using site directed mutagenesis, that the catalytic mechanism for the ALDH activity appears to be similar to that described for other members of the ALDH extended family.

Citations

Oct 13, 2006·Parasitology·J TolstrupI Bruchhaus
Dec 22, 2009·The Journal of Eukaryotic Microbiology·Guillermo Paz-Y-Miño C, Avelina Espinosa
Jan 24, 2017·Metabolic Engineering·Fungmin LiewNigel P Minton
Oct 9, 2013·Acta Crystallographica. Section D, Biological Crystallography·Jonathan ExtanceMichael J Danson
Aug 22, 2020·International Journal for Parasitology·Magda Reyes-LópezMireya de la Garza

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