ArticleThe Journal of biological chemistry2001
The bifunctional Entamoeba histolytica alcohol dehydrogenase 2 (EhADH2) protein is necessary for amebic growth and survival and requires an intact C-terminal domain for both alcohol dahydrogenase and acetaldehyde dehydrogenase activity.
Article in The Journal of biological chemistry, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 64 citations in OpenAlex.
- Article
- The role of AdhE on ethanol tolerance and production in Clostridium thermocellum.The Journal of biological chemistry · 2024Article
- Influence of deep eutectic solvents on redox biocatalysis involving alcohol dehydrogenases.Heliyon · 2024Review
- Decoding triancestral origins, archaic introgression, and natural selection in the Japanese population by whole-genome sequencing.Science advances · 2024Article
- Glycerol biosynthetic pathway plays an essential role in proliferation and antioxidative defense in the human enteric protozoan parasite Entamoeba histolytica.Scientific reports · 2023Article
- The Role of Acetate Kinase in the Human ParasiteParasitologia (Basel, Switzerland) · 2022Article
- Article
- An Alcohol Dehydrogenase 3 (ADH3) fromMicroorganisms · 2020Article
- Anti-amebic effects of Chinese rhubarb (Heliyon · 2020Article
- Revisiting Drug Development Against the Neglected Tropical Disease, Amebiasis.Frontiers in cellular and infection microbiology · 2020Review
- Article
- Association between local alcoholic beverages and amoebic liver abscess in the Indian subcontinent: Weird but true!JGH open : an open access journal of gastroenterology and hepatology · 2019Article
- Entamoeba histolytica under Oxidative Stress: What Countermeasure Mechanisms Are in Place?Cells · 2017Review
- Metabolic engineering of Clostridium autoethanogenum for selective alcohol production.Metabolic engineering · 2017Article
- Identification of S-Nitrosylated (SNO) Proteins inFrontiers in cellular and infection microbiology · 2017Article
- Entamoeba Clone-Recognition Experiments: Morphometrics, Aggregative Behavior, and Cell-Signaling Characterization.The Journal of eukaryotic microbiology · 2016Article
- Diversity and Evolutionary Analysis of Iron-Containing (Type-III) Alcohol Dehydrogenases in Eukaryotes.PloS one · 2016Article
- Cofactor Specificity of the Bifunctional Alcohol and Aldehyde Dehydrogenase (AdhE) in Wild-Type and Mutant Clostridium thermocellum and Thermoanaerobacterium saccharolyticum.Journal of bacteriology · 2015Article
- The Entamoeba histolytica Dnmt2 homolog (Ehmeth) confers resistance to nitrosative stress.Eukaryotic cell · 2014Article
- Article
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
Abstract
The intestinal protozoan pathogen Entamoeba histolytica lacks mitochondria and derives energy from the fermentation of glucose to ethanol with pyruvate, acetyl enzyme Co-A, and acetaldehyde as intermediates. A key enzyme in this pathway may be the 97-kDa bifunctional E. histolytica alcohol dehydrogenase 2 (EhADH2), which possesses both alcohol dehydrogenase (ADH) and acetaldehyde dehydrogenase activity (ALDH). EhADH2 appears to be a fusion protein, with separate N-terminal ALDH and C-terminal ADH domains. Here, we demonstrate that EhADH2 expression is required for E. histolytica growth and survival. We find that a mutant EhADH2 enzyme containing the C-terminal 453 amino acids of EhADH2 has ADH activity but lacks ALDH activity. However, a mutant consisting of the N-terminal half of EhADH2 possessed no ADH or ALDH activity. Alteration of a single histidine to arginine in the putative active site of the ADH domain eliminates both ADH and ALDH activity, and this mutant EhADH2 can serve as a dominant negative, eliminating both ADH and ALDH activity when co-expressed with wild-type EhADH2 in Escherichia coli. These data indicate that EhADH2 enzyme is required for E. histolytica growth and survival and that the C-terminal ADH domain of the enzyme functions as a separate entity. However, ALDH activity requires residues in both the N- and C-terminal halves of the molecule.
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