Activity of long chain acyl-CoA synthetase in isolated alveolar type II cells.
Fatty-acyl-CoA synthetase activity was determined in rat alveolar type II cells. Compared to whole-lung homogenate, the enzyme specific activity with palmitic acid was 3.6-fold higher in isolated type II alveolar cells. The enzyme in rat alveolar type II cells did not discriminate among various fatty acids, suggesting that supply of fatty acids rather than specificity might be an important factor for their activation in these cells.
D000818:Animals; D003066:Coenzyme A Ligases / Q000378:metabolism*; D005227:Fatty Acids / Q000378:metabolism; D008297:Male; D011650:Pulmonary Alveoli / Q000166:cytology / Q000201:enzymology*; D051381:Rats; D011919:Rats, Inbred Strains; D012097:Repressor Proteins; D029701:Saccharomyces cerevisiae Proteins; D013379:Substrate Specificity; D000098859:Long-Chain-Fatty-Acid-CoA Ligase
D005227:Fatty Acids; D012097:Repressor Proteins; D029701:Saccharomyces cerevisiae Proteins; D003066:Coenzyme A Ligases; C090799:FAA2 protein, S cerevisiae; D000098859:Long-Chain-Fatty-Acid-CoA Ligase