Inhibition of Acetolactate Synthase from Pea by Pyrimidine Derivatives

Pyrimidine 유도체에 의한 완두 Acetolactate Synthase의 저해에 관한 연구

  • Joo, Young A (Department of Biochemistry, Chunbuk University) ;
  • Kim, Dae Whang (Korea Research Institute of Chemical Technology) ;
  • Chang, Soo Ik (Department of Biochemistry, Chunbuk University) ;
  • Choi, Jung Do (Department of Biochemistry, Chunbuk University)
  • Published : 19970600


Acetolactate synthase(ALS) is the common enzyme in the biosynthetic of valine, leucine, and isoleucine, and is the target of several classes of structually unrelated herbicides, including sulfonylureas, imidazolinones, and triazolopyrimidines. In an effort to develop new and desirable herbicides, we have synthesized 4,6-dimethoxypyrimidine derivatives, and examined their inhibitory activities on pea ALS. The most active compound was found to be K11570 and $IC_{50}$ value for K11570 was 0.2 ${\mu}M.$ The inhibition of pea ALS by K11570 was biphasic, showing increased inhibition with incubation time. The K11570 showed mixed-type inhibition with respect to substrate pyruvate. Dual inhibition analysis of K11570 versus sufonylurea herbicide Ally and feedback inhibitor leucine revealed that three inhibitors were competitive for binding to ALS. The arginine modified enzyme showed decreased inhibition by K11570, sufonylurea Ally, and leucine, in constrast to, tryptophan modification did not affect on the sensitivity of ALS to the inhibitors.



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