8J31

Glucosyl transferase crystallized in the presence of beta carotene

8J31 の概要

• エントリーDOI: 10.2210/pdb8j31/pdb
• 関連するPDBエントリー: 8J2Z
• 分子名称: Glycosyltransferase (1 entity in total)
• 機能のキーワード: glucosyl transferase, transferase
• 由来する生物種: Nicotiana tabacum (common tobacco)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 53703.67

構造登録者

Arold, S.T.,Hameed, U.F.S. (登録日: 2023-04-16, 公開日: 2024-04-17, 最終更新日: 2025-04-09)

主引用文献

Liao, J.,Shahul Hameed, U.F.,Hoffmann, T.D.,Kurze, E.,Sun, G.,Steinchen, W.,Nicoli, A.,Di Pizio, A.,Kuttler, C.,Song, C.,Catici, D.A.M.,Assaad-Gerbert, F.,Hoffmann, T.,Arold, S.T.,Schwab, W.G.
beta-Carotene alleviates substrate inhibition caused by asymmetric cooperativity.
Nat Commun, 16:3065-3065, 2025

PubMed Abstract: Enzymes are essential catalysts in biological systems. Substrate inhibition, once dismissed, is now observed in 20% of enzymes and is attributed to the formation of an unproductive enzyme-substrate complex, with no structural evidence of unproductivity provided to date. This study uncovers the molecular mechanism of substrate inhibition in tobacco glucosyltransferase NbUGT72AY1, which transfers glucose to phenols for plant protection. The peculiarity that β-carotene strongly attenuates the substrate inhibition of NbUGT72AY1, despite being a competitive inhibitor, allows to determine the conformational changes that occur during substrate binding in both active and substrate-inhibited complexes. Crystallography reveals structurally different ternary enzyme-substrate complexes that do not conform to classical mechanisms. An alternative pathway suggests substrates bind randomly, but the reaction occurs only if a specific order is followed (asymmetric cooperativity). This unreported paradigm explains substrate inhibition and reactivation by competitive inhibitors, opening new research avenues in metabolic regulation and industrial applications.

PubMed: 40157902
DOI: 10.1038/s41467-025-58259-7

実験手法

X-RAY DIFFRACTION (3.78 Å)