title: 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 beta-ketoacyl reductase domains of the multifunctional fatty acid synthase. Overall, the deduced amino acid sequence provides the domains for enoyl reductase, beta-ketoacyl reductase, acyl carrier protein and thioesterase of the mouse fatty acid synthase.
authors.affiliation: Department of Nutrition, Harvard School of Public Health, Boston, MA 02115.
authors.forename: J D
authors.initials: JD
authors.lastname: Paulauskis
authors.forename: H S
authors.initials: HS
authors.lastname: Sul
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D001665:Binding Sites; D003062:Codon; D004247:DNA / Q000235:genetics; D064429:Fatty Acid Synthases / Q000235:genetics*; D051379:Mice; D008969:Molecular Sequence Data; D009249:NADP / Q000378:metabolism*; D012333:RNA, Messenger / Q000235:genetics / Q000378:metabolism*; D012689:Sequence Homology, Nucleic Acid
chemical_list: D003062:Codon; D012333:RNA, Messenger; D009249:NADP; D004247:DNA; D064429:Fatty Acid Synthases