Lipases specifically degrading lipopolysaccharide: fatty acyl amidases from Dictyostelium discoideum.
Two specific fatty acyl amidases that hydrolyze lipopolysaccharide have been isolated from the slime mold Dictyostelium discoideum. Esterases as well as phosphatases acting on lipid A derivatives were also observed. The first amidase (I) hydrolyzes the fatty amide adjacent to the C-1 phosphate on the disaccharide backbone of lipid A. Amidase II cleaves the distal amide, but only after deacylation of the first site. The range of specificity and the structural determinants important to specificity of the amidases were evaluated in studies of specifically modified derivatives of lipid A. In light of the effects of lipopolysaccharide on the biology of D. discoideum, a role for the amidases and other lipopolysaccharide-specific catabolic enzymes is discussed.
D000581:Amidohydrolases / Q000032:analysis* / Q000502:physiology; D004023:Dictyostelium / Q000201:enzymology*; D008070:Lipopolysaccharides / Q000378:metabolism*
D008070:Lipopolysaccharides; D000581:Amidohydrolases; C035588:fatty acyl amidases