Structural basis for plant-specific type III polyketide synthase based on the X-ray crystal structure analysis and computational chemistry

We solved crystal structure of an octaketide synthase (OKS) F66L/N222G mutant enzyme that catalyzes the longest number of malonyl-CoA condensations to produce TW95a. Furthermore, we succeeded in producing an OKS mutant enzyme that increased enzyme activity for the formation of TW95a to approximately 1.5 times on the basis of the crystal structure. In addition, we succeeded in cloning a novel type III PKS that specifically catalyzes the formation of quinolinone.