1979/11/01 by Hansjorg ENGESER, Hansjörg Engeser, Karin Hübner +5 · 3 citations
Chemistry · Biochemistry, Genetics and Molecular Biology · Materials Science · #Mass Spectrometry Techniques and Applications #Enzyme Catalysis and Immobilization #Enzyme Structure and Function
paper · pdf · doi:10.1111/j.1432-1033.1979.tb19734.x
Active-site peptides of malonyl and palmitoyl transferase from yeast fatty acid synthetase were isolated and sequenced to try to prove the hypothesis [J. Ayling, R. Pirson & F. Lynen (1979) Biochemistry 11, 526--533] that both enzymes are identical. For this purpose synthetase modified with 5,5'-dithiobis(2-nitrobenzoic acid) was labelled with either [14C]malonyl or [14C]palmitoyl residues followed by proteolytic digestion of the labelled protein. [14C]Malonyl-peptides were isolated by conventional purification procedures; their structures were determined by a combination of methods. [14C]Palmitoyl-peptide material was purified by high-performance liquid chromatography and the structure determined by solid-phase Edman degradation and other analytical methods. Serine was identified as the acyl acceptor group in both transferases. Comparison of the sequence data available shows that the sequence around the acyl acceptor group in both cases is identical. This proves the identity of malonyl and palmitoyl transferase.