作者: Shogo Matsumoto , Rika Ozawa , Kyoichi Uchiumi , Masaaki Kurihara
DOI: 10.1271/BBB.60.369
关键词: Reductase 、 Kinase 、 Biochemistry 、 Bombykol 、 Long-chain-fatty-acid—CoA ligase 、 Phosphorylation 、 Biology 、 Biosynthesis 、 Enzyme 、 Dephosphorylation
摘要: Cell-free production of bombykol was done by incubating a pheromone gland homogenate in the presence NADPH, ATP, and CoA. Addition n-hexane to reaction mixture stimulated production, resulting 238 ng from equivalent 2 glands after 23 h. Removal either or CoA resulted no stimulation suggesting that final step biosynthetic pathway is acyl synthetase reductase, sequentially. Incubation first with ATP high concentrations suppressed bombykol. Since incubation also inhibited conversion [1-14C]palmitoyl into 1-hexadecanol, inhibitory action seemed attributable inactivation reductase phosphorylation, as mediated protein kinase homogenate. Our results suggest activity biosynthesis regulated phosphorylation/dephosphorylation, activation occurs dephosphorylation phosphoprotein phosphatase.