Abstract
The formation and degradation of indole acetic acid-amino acid conjugates (IAA-aa) play an important role in auxin homeostasis. GH3s, the early auxin-responsive genes, encode IAA-aa synthetases. 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-acylsulfamoyladenosine derivatives (sulfamates) of auxins as the intermediate analog inhibitors of GH3s. We previously presented that these compounds served as potent in vitro inhibitors of GH3s, and also exhibited in vivo activities.
In this study, we have designed and synthesized a series of N-acylsulfamoylaminoadenosine derivatives (sulfamides, acyl = IAA, PAA, NAA and 2,4-D) to improve chemical stability and hydrophobicity of the inhibitors. The sulfamides were found to exhibit potent in vitro inhibitory activities toward GH3 and were stable under acidic and basic conditions.
