書誌事項
- タイトル別名
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- Research strategies and crystallographic analysis of CYP90B1, a key enzyme in brassinosteroid biosynthesis
- 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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説明
<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>
収録刊行物
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- 植物の生長調節
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植物の生長調節 56 (1), 35-41, 2021
一般社団法人 植物化学調節学会
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詳細情報 詳細情報について
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- CRID
- 1390572633001252864
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- NII論文ID
- 130008161586
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- NII書誌ID
- AA11550064
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- ISSN
- 21896305
- 13465406
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- NDL書誌ID
- 031583797
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- 本文言語コード
- ja
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- データソース種別
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- JaLC
- NDL
- CiNii Articles
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- 抄録ライセンスフラグ
- 使用不可
