PALMITOYL-COA LIGASE ACTIVITY IN HEPATOPANCREAS AND GILL MICROSOMES OF THE FRESH-WATER SHRIMP MACROBRACHIUM-BORELLII

1. 1. The kinetic parameters of microsomal palmitoyl-CoA ligase from gills and hepatopancreas of Macrobrachium borellii were investigated. 2. 2. The optimal temperature for the enzymatic activity was 37°C in gill microsomes and 30°C in hepatopancreas microsomes. 3. 3. The maximal affinity of the enzyme for its substrate was higher in gill microsomes (apparent Km = 12.59 μM) compared with hepatopancreas microsomes (apparent Km = 49.74 μM). 4. 4. A lower lipid mobility in gill microsomes than in hepatopancreas microsomes was found. It was attributed to a high phosphatidyl ethanolamine content in gill membranes. This could also explain the differences in the optimal temperatures for the activities of the enzyme from both organs. © 1990.