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.
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.
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
D004187:Disaccharides; D006539:Heptoses; D008070:Lipopolysaccharides; D000581:Amidohydrolases; D005944:Glucosamine