1029292-76-9Relevant academic research and scientific papers
Structure-activity relationship of uniconazole, a potent inhibitor of ABA 8′-hydroxylase, with a focus on hydrophilic functional groups and conformation
Todoroki, Yasushi,Kobayashi, Kyotaro,Yoneyama, Hidetaka,Hiramatsu, Saori,Jin, Mei-Hong,Watanabe, Bunta,Mizutani, Masaharu,Hirai, Nobuhiro
, p. 3141 - 3152 (2008/09/19)
The plant growth retardant S-(+)-uniconazole (UNI-OH) is a strong inhibitor of abscisic acid (ABA) 8′-hydroxylase, a key enzyme in the catabolism of ABA, a plant hormone involved in stress tolerance, stomatal closure, flowering, seed dormancy, and other physiological events. In the present study, we focused on the two polar sites of UNI-OH and synthesized 3- and 2″-modified analogs. Conformational analysis and an in vitro enzyme inhibition assay yielded new findings on the structure-activity relationship of UNI-OH: (1) by substituting imidazole for triazole, which increases affinity to heme iron, we identified a more potent compound, IMI-OH; (2) the polar group at the 3-position increases affinity for the active site by electrostatic or hydrogen-bonding interactions; (3) the conformer preference for a polar environment partially contributes to affinity for the active site. These findings should be useful for designing potent azole-containing specific inhibitors of ABA 8′-hydroxylase.
