Molecular cloning and sequencing of human palmitoyl-CoA ligase and its tissue specific expression.
A complimentary DNA clone encoding the entire human palmitoyl-CoA ligase has been isolated from a liver cDNA library and sequenced in it's entirety. The predicted product is a 699 amino acid protein. Southern analysis utilizing the human palmitoyl-CoA ligase gene as a probe revealed varying degrees of similarity amongst various mammalian species. The palmitoyl-CoA ligase gene is highly expressed in liver, heart, skeletal muscle and kidney, and to a lesser extent in brain, lung, placenta and pancreas. The expression of palmitoyl-CoA ligase in various tissue parallels the function of this enzyme in the metabolism of fatty acids in these tissues.
Ghosh
B
B
Department of Pediatrics, Medical University of South Carolina, Charleston 29425, USA.
Barbosa
E
E
Singh
I
I
D000595:Amino Acid Sequence; D003001:Cloning, Molecular; D003066:Coenzyme A Ligases / Q000737:chemistry* / Q000235:genetics; D006801:Humans; D008969:Molecular Sequence Data; D009928:Organ Specificity; D012097:Repressor Proteins; D029701:Saccharomyces cerevisiae Proteins; D017386:Sequence Homology, Amino Acid; D013045:Species Specificity; D000098859:Long-Chain-Fatty-Acid-CoA Ligase
D012097:Repressor Proteins; D029701:Saccharomyces cerevisiae Proteins; D003066:Coenzyme A Ligases; C090799:FAA2 protein, S cerevisiae; D000098859:Long-Chain-Fatty-Acid-CoA Ligase