Studies on alanine aminotransferase in nematodes.
L-alanine aminotransferase was demonstrated in a range of gastrointestinal, free-living and entomophagous nematodes. As in mammals, nematode L-alanine aminotransferase was found to exist in the form of mitochondrial and cytosolic isoenzymes. Whilst the majority of nematode enzymes exhibited a greater overall capacity for L-alanine synthesis than for L-alanine catabolism in vitro, the opposite was true for rat liver L-alanine aminotransferase. In contrast with rat liver, certain gastrointestinal nematodes were apparently able to transaminate D-alanine at low rates. H. contortus cytosolic L-alanine aminotransferase differed significantly from the mammalian enzyme with respect to both thermal stability and response to potential protective reagents.
Walker
J
J
Department of Biological Sciences, University College of Wales, U.K.
Barrett
J
J
D000410:Alanine Transaminase / Q000032:analysis*; D000818:Animals; D003600:Cytosol / Q000201:enzymology; D007527:Isoenzymes / Q000032:analysis*; D008099:Liver / Q000201:enzymology; D008928:Mitochondria / Q000201:enzymology; D009348:Nematoda / Q000201:enzymology*; D051381:Rats
D007527:Isoenzymes; D000410:Alanine Transaminase