MOLECULAR-CLONING AND SEQUENCING OF HUMAN PALMITOYL-COA LIGASE AND ITS TISSUE-SPECIFIC EXPRESSION

A complimentary DNA clone encoding the entire human palmitoyl-CoA liga se has been isolated from a liver cDNA library and sequenced in it's e ntirety. The predicted product is a 699 amino acid protein. Southern a nalysis utilizing the human palmitoyl-CoA ligase gene as a probe revea led varying degrees of similarity amongst various mammalian species. T he palmitoyl-CoA ligase gene is highly expressed in liver, heart, skel etal muscle and kidney, and to a lesser extent in brain, lung, placent a and pancreas. The expression of palmitoyl-CoA ligase in various tiss ue parallels the function of this enzyme in the metabolism of fatty ac ids in these tissues.