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

Biochim Biophys Acta. 1996 Apr 10;1306(1):23-6. doi: 10.1016/0167-4781(96)00014-0.

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.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alcohol Oxidoreductases / classification
  • Alcohol Oxidoreductases / genetics*
  • Amino Acid Sequence
  • Anaerobiosis
  • Animals
  • Bacteria / enzymology
  • Base Sequence
  • Cloning, Molecular
  • DNA, Complementary / genetics
  • Entamoeba histolytica / enzymology
  • Entamoeba histolytica / genetics*
  • Genes, Protozoan*
  • Molecular Sequence Data
  • Open Reading Frames
  • Protozoan Proteins / genetics*
  • Saccharomyces cerevisiae / enzymology
  • Sequence Alignment
  • Sequence Homology, Amino Acid
  • Species Specificity

Substances

  • DNA, Complementary
  • Protozoan Proteins
  • Alcohol Oxidoreductases
  • alcohol dehydrogenase (NAD(P)+)

Associated data

  • GENBANK/Z48752