Structure of mouse fatty acid synthase mRNA identification of the two NADPH binding sites

Abstract

Overlapping cDNA clones corresponding to 3.3 kb covering the carboxy-half and 3′ non-coding regions of the single 8.2 kb mouse fatty acid synthase mRNA were isolated and sequenced. The sequence coded for 838 amino acid residues, followed by termination codon TAG, 771 nucleotides of 3′ untranslated sequence and a poly A tail. For the first time, the two putative components of the NADPH binding sites of fatty acid synthase were identified, thereby making it possible to assign the enoyl reductase and β-ketoacyl reductase domains of the multifunctional fatty acid synthase. Overall, the deduced amino acid sequence provides the domains for enoyl reductase, β-ketoacyl reductase, acyl carrier protein and thioesterase of the mouse fatty acid synthase.