title: The structure of lipopolysaccharide from an Escherichia coli heptose-less mutant. III. Two fatty acyl amidases from Dictyostelium discoideum and their action on lipopolysaccharide derivatives.
abstract: Two fatty acyl amidases have been partially purified from the slime mold, Dictyostelium discoideum. Their action on lipopolysaccharide derivatives, especially Compound I, has been studied. Amidase I removes specifically the beta-hydroxymyristyl group, which is present on the amino group adjacent to the C-1 phosphate. The product, Compound V, is then a substrate for Amidase II, which removes the remaining beta-hydroxymyristyl group from the amino group in the distal glucosamine ring to give Compound VI. Compound I itself is resistant to Amidase II. Thus, the two enzymes show a high degree of structural specificity. The structure of lipopolysaccharide from the E. coli K-12 mutant is concluded in the light of studies reported in this and the accompanying papers, and this structure is discussed in relation to other bacterial lipopolysaccharides.
mesh_terms: D000581:Amidohydrolases; D004023:Dictyostelium / Q000201:enzymology*; D004187:Disaccharides / Q000032:analysis; D004926:Escherichia coli / Q000378:metabolism*; D005944:Glucosamine / Q000032:analysis; D006539:Heptoses / Q000378:metabolism*; D008070:Lipopolysaccharides; D008968:Molecular Conformation
chemical_list: D004187:Disaccharides; D006539:Heptoses; D008070:Lipopolysaccharides; D000581:Amidohydrolases; D005944:Glucosamine