Paulauskis_1989_Biochem.Biophys.Res.Commun_158_690

Reference

Title : Structure of mouse fatty acid synthase mRNA. Identification of the two NADPH binding sites - Paulauskis_1989_Biochem.Biophys.Res.Commun_158_690
Author(s) : Paulauskis JD , Sul HS
Ref : Biochemical & Biophysical Research Communications , 158 :690 , 1989
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.

PubMedSearch : Paulauskis_1989_Biochem.Biophys.Res.Commun_158_690
PubMedID: 2920037
Gene_locus related to this paper: mouse-FASN

Related information

Gene_locus mouse-FASN

Citations formats

Paulauskis JD, Sul HS (1989)
Structure of mouse fatty acid synthase mRNA. Identification of the two NADPH binding sites
Biochemical & Biophysical Research Communications 158 :690

Paulauskis JD, Sul HS (1989)
Biochemical & Biophysical Research Communications 158 :690