PMID:7935603
| Citation |
Yang, W, Li, E, Kairong, T and Stanley, SL Jr (1994) Entamoeba histolytica has an alcohol dehydrogenase homologous to the multifunctional adhE gene product of Escherichia coli. Mol. Biochem. Parasitol. 64:253-60 |
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| Abstract |
Entamoeba histolytica ferments glucose to ethanol under the anaerobic conditions of the human colon. There is special interest in this metabolic pathway because it provides an opportunity for parasite-specific chemotherapy. Peptide sequences from a 97-kDa E. histolytica protein, which was originally isolated because of extracellular matrix binding properties, were used to clone and sequence a gene that was found to encode an E. histolytica alcohol dehydrogenase and acetaldehyde dehydrogenase (EhADH2). The EhADH2 cDNA clone had an open reading frame encoding 870 amino acids with a predicted molecular weight of 95,758. The EhADH2 cDNA clone was identical in 48% of its amino acids to the multifunctional enzyme (alcohol dehydrogenase, acetyl-CoA reductase, and pyruvate-formate-lyase-deactivase) encoded by the Escherichia coli adhE gene. The isolation of the EhADH2 protein helps define a new family of ADH enzymes that may be specific to anaerobic and facultatively anaerobic organisms. |
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| Keywords |
Alcohol Dehydrogenase/genetics; Alcohol Dehydrogenase/metabolism; Aldehyde Oxidoreductases/genetics; Aldehyde Oxidoreductases/metabolism; Amino Acid Sequence; Animals; Base Sequence; DNA, Complementary/genetics; DNA, Protozoan/genetics; Entamoeba histolytica/enzymology; Entamoeba histolytica/genetics; Escherichia coli/enzymology; Escherichia coli/genetics; Extracellular Matrix/metabolism; Genes, Bacterial; Genes, Protozoan; Molecular Sequence Data; Protozoan Proteins/genetics; Protozoan Proteins/metabolism; Sequence Homology, Amino Acid; Sequence Homology, Nucleic Acid |
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