title: Sequence of a tryptic peptide from the NADPH binding site of the enoyl reductase domain of fatty acid synthase.
abstract: Fatty acid synthase from the uropygial gland of goose was inhibited by treatment with pyridoxal 5'-phosphate by selectively modifying a lysine residue at the NADPH binding site of the enoyl reductase domain (A. J. Poulose and P. E. Kolattukudy (1980) Arch. Biochem. Biophys. 201, 313-321). Distribution of radioactivity in tryptic peptides generated from the synthase treated with pyridoxal 5'-phosphate/NaB3H4 in the presence and absence of 2'-monophosphoadenosine-5'-diphosphoribose, which protects the enzyme from inactivation by pyridoxal phosphate, showed that modification of one specific peptide was prevented by the protector. This peptide was purified by a combination of Sephadex G-25 column chromatography, anion-exchange chromatography, and high-performance liquid chromatography. The primary structure of this peptide is Val-Phe-Thr-Thr-Val-Gly-Ser-Ala-Glu-Lys(Pxy)-Arg.
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002384:Catalysis; D044943:Fatty Acid Desaturases / Q000378:metabolism*; D064429:Fatty Acid Synthases / Q000037:antagonists & inhibitors / Q000378:metabolism*; D005777:Geese; D009249:NADP / Q000378:metabolism*; D010446:Peptide Fragments / Q000302:isolation & purification*; D014357:Trypsin
chemical_list: D010446:Peptide Fragments; D009249:NADP; D044943:Fatty Acid Desaturases; D064429:Fatty Acid Synthases; D014357:Trypsin