13.オーキシン不活性化を阻害する化学的ツール : IAA-アミノ酸複合体合成酵素(GH3)阻害剤の設計とin vivo活性(口頭発表)

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The formation and degradation of IAA-amino acid conjugates (IAA-aa) play an important role in auxin homeostasis. GH3s encode IAA-aa synthetases, but their functional redundancy has hampered the genetic approach to study auxin homeostasis. GH3s belong to the acyl-activating enzyme superfamily that activates IAA by adenylation. According to this catalytic mechanism, we designed and synthesized N-sulfamoyladenosine (SA) derivatives of auxins (IAA-SA, PAA-SA, NAA-SA and 2,4-D-SA) as intermediate analog inhibitors of GH3s. These compounds not only served as potent in vitro inhibitors of GH3s with IC_<50> values of 3 to 45 μM, but also exhibited in vivo activities. In the excised Arabidopsis leaves treated with exogenous IAA, the endogenous levels of IAA-Asp, IAA-Glu and IAA-Gln greatly increased. When the SA derivatives were applied together with IAA, the increase was significantly repressed. Thus, the SA-derivatives of auxins were adsorbed in plant tissues and inhibited GH3s involved in lAA-aa synthesis, thereby serving as highly effective chemical tools to probe otherwise inaccessible auxin homeostasis. The cell permeability was suggested to be an important factor that affected the in vivo activities of SA derivatives. We therefore designed and synthesized a series of N-acylsulfamide derivatives that are chemically stable and more hydrophobic than SA derivatives. The results on N-acylsulfamide derivatives will also be presented.
植物化学調節学会の論文
2007-10-05

13.オーキシン不活性化を阻害する化学的ツール : IAA-アミノ酸複合体合成酵素(GH3)阻害剤の設計とin vivo活性(口頭発表)

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