Research strategies and crystallographic analysis of CYP90B1, a key enzyme in brassinosteroid biosynthesis

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  • Fujiyama Keisuke
    Graduate School of Engineering, Tottori University
  • Hino Tomoya
    Graduate School of Engineering, Tottori University Center for Research on Green Sustainable Chemistry, Tottori University
  • Mizutani Masaharu
    Graduate School of Agricultural Science, Kobe University
  • Nagano Shingo
    Graduate School of Engineering, Tottori University Center for Research on Green Sustainable Chemistry, Tottori University

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  • ブラシノステロイド生合成における鍵酵素CYP90B1の結晶構造解析と実験上の工夫について
  • ブラシノステロイド セイゴウセイ ニ オケル カギ コウソ CYP90B1 ノ ケッショウ コウゾウ カイセキ ト ジッケン ジョウ ノ クフウ ニ ツイテ

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<p>Brassinosteroids （BRs） are a class of phytohormone involved in plant growth and environmental stress response.　Since the isolation of the most potent BR, brassinolide, by Grove in 1979, extensive studies in various fields have been achieved to understand BR signaling, biosynthesis, metabolism, and inhibition.　Hitherto, the BR biosynthesis pathway and most of the enzymes, which include several cytochrome P450s （CYP, P450）, involved in the pathway have been identified.　CYP90B1, which is the first and rate-determining enzyme in BR biosynthesis, mediates C22 hydroxylation of campesterol, a common precursor of C28 BRs.　Additionally, CYP90B1 is a target of the BR biosynthesis inhibitor, brassinazole.　Recently, we reported the crystal structures of CYP90B1 with the binding of a substrate and two inhibitors, and analysis of its cholesterol-bound structure and docking simulation of campesterol unveiled the mechanisms of regio- and stereo-selective hydroxylation by CYP90B1.　In this review, we describe and focus on our crystallization strategies for CYP90B1, the enzyme-ligand interactions, and conformational changes induced by ligand binding.</p>

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