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6INH

A glycosyltransferase with UDP and the substrate

6INH の概要
エントリーDOI10.2210/pdb6inh/pdb
関連するPDBエントリー6INF
分子名称UDP-glycosyltransferase 76G1, URIDINE-5'-DIPHOSPHATE, 1-O-[(8alpha,9beta,10alpha,13alpha)-13-(beta-D-glucopyranosyloxy)-18-oxokaur-16-en-18-yl]-beta-D-glucopyranose, ... (5 entities in total)
機能のキーワードcomplex, transferase
由来する生物種Stevia rebaudiana (Stevia)
タンパク質・核酸の鎖数1
化学式量合計55032.04
構造登録者
Zhu, X. (登録日: 2018-10-25, 公開日: 2019-07-31, 最終更新日: 2023-11-22)
主引用文献Yang, T.,Zhang, J.,Ke, D.,Yang, W.,Tang, M.,Jiang, J.,Cheng, G.,Li, J.,Cheng, W.,Wei, Y.,Li, Q.,Naismith, J.H.,Zhu, X.
Hydrophobic recognition allows the glycosyltransferase UGT76G1 to catalyze its substrate in two orientations.
Nat Commun, 10:3214-3214, 2019
Cited by
PubMed Abstract: Diets high in sugar are recognized as a serious health problem, and there is a drive to reduce their consumption. Steviol glycosides are natural zero-calorie sweeteners, but the most desirable ones are biosynthesized with low yields. UGT76G1 catalyzes the β (1-3) addition of glucose to steviol glycosides, which gives them the preferred taste. UGT76G1 is able to transfer glucose to multiple steviol substrates yet remains highly specific in the glycosidic linkage it creates. Here, we report multiple complex structures of the enzyme combined with biochemical data, which reveal that the enzyme utilizes hydrophobic interactions for substrate recognition. The lack of a strict three-dimensional recognition arrangement, typical of hydrogen bonds, permits two different orientations for β (1-3) sugar addition. The use of hydrophobic recognition is unusual in a regio- and stereo-specific catalysis. Harnessing such non-specific hydrophobic interactions could have wide applications in the synthesis of complex glycoconjugates.
PubMed: 31324778
DOI: 10.1038/s41467-019-11154-4
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.1 Å)
構造検証レポート
Validation report summary of 6inh
検証レポート(詳細版)ダウンロードをダウンロード

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件を2025-10-15に公開中

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