Localization of hydrolytic enzymes in Acinetobacter calcoaceticus.
The localization of hydrolytic enzymes, phosphatase, esterase, lipase and palmitoyl-CoA hydrolase was analysed in the cytosol, cytoplasmic membrane, periplasmic fraction, outer membrane and culture supernatant in dependence on the growth rate of the bacteria. The unspecific phosphatase was found to be a cytosolic enzyme. A lipase was the only extracellular enzyme detected. The results pointed to a secretion of the lipase into the culture medium via cytoplasmic and outer membrane. The palmitoyl-CoA hydrolase was found to be attached to the outer membrane, but activities were also detected in the periplasmic fraction. Unspecific esterolytic activities were mainly measured in the cytosol and in the cytoplasmic membrane.
Fischer
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BE
D000150:Acinetobacter / Q000201:enzymology*; D004950:Esterases / Q000032:analysis; D008049:Lipase / Q000032:analysis; D008291:Malate Dehydrogenase / Q000032:analysis; D009097:Multienzyme Complexes / Q000032:analysis; D009247:NADH, NADPH Oxidoreductases / Q000032:analysis; D010170:Palmitoyl-CoA Hydrolase / Q000032:analysis; D010744:Phosphoric Monoester Hydrolases / Q000032:analysis
D009097:Multienzyme Complexes; D008291:Malate Dehydrogenase; C023107:NADH oxidase; D009247:NADH, NADPH Oxidoreductases; D004950:Esterases; D008049:Lipase; D010170:Palmitoyl-CoA Hydrolase; D010744:Phosphoric Monoester Hydrolases