PMID: 8611619Apr 10, 1996Paper

Cloning and expression of an Entamoeba histolytica NAPD+(-)dependent alcohol dehydrogenase gene

Biochimica Et Biophysica Acta
M A RodríguezE Orozco

Abstract

In this paper we cloned, sequenced and expressed a novel Entamoeba histolytica alcohol dehydrogenase gene (Ehadh3). Ehadh3 has a predicted 383 amino acids open reading frame, encoding for a 42.3 kDa protein. The deduced amino acid sequence showed 24 to 26% identity to other type III alcohol dehydrogenases found in prokaryotic and lower eukaryotic organisms, but not in mammalia. There are at least two Ehadh3 gene copies in the genome, but only a 1.2 kb transcript was detected. The EhADH3 fusion protein showed a NADP+(-)dependent ADH activity. Ehadh3 may be a good target for the developing of anti-E. histolytica drugs, without producing damage to the human.

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Citations

Aug 5, 2000·Molecular and Biochemical Parasitology·M Dan, C C Wang
Feb 11, 2010·Journal of Biomedicine & Biotechnology·Isabel Wong-BaezaArmando Isibasi
May 13, 2008·Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences·Marek Mentel, William Martin
Jun 13, 2012·Microbiology and Molecular Biology Reviews : MMBR·Miklós MüllerWilliam F Martin
Jun 13, 2002·The Journal of Parasitology·Eva E AvilaRoberto Zazueta-Sandoval
Nov 5, 2019·Biochimica Et Biophysica Acta. Proteins and Proteomics·Poonam KumariSamudrala Gourinath
Jul 2, 1999·Antimicrobial Agents and Chemotherapy·J Samuelson

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