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7ERX

Glycosyltransferase in complex with UDP and STB

7ERX の概要
エントリーDOI10.2210/pdb7erx/pdb
分子名称Glycosyltransferase, GLYCEROL, URIDINE-5'-DIPHOSPHATE, ... (5 entities in total)
機能のキーワードglycosyltransferase in steviol glucosylation, transferase
由来する生物種Oryza sativa subsp. japonica (Rice)
タンパク質・核酸の鎖数1
化学式量合計52181.48
構造登録者
Zhu, X. (登録日: 2021-05-08, 公開日: 2021-12-08, 最終更新日: 2023-11-29)
主引用文献Zhang, J.,Tang, M.,Chen, Y.,Ke, D.,Zhou, J.,Xu, X.,Yang, W.,He, J.,Dong, H.,Wei, Y.,Naismith, J.H.,Lin, Y.,Zhu, X.,Cheng, W.
Catalytic flexibility of rice glycosyltransferase OsUGT91C1 for the production of palatable steviol glycosides.
Nat Commun, 12:7030-7030, 2021
Cited by
PubMed Abstract: Steviol glycosides are the intensely sweet components of extracts from Stevia rebaudiana. These molecules comprise an invariant steviol aglycone decorated with variable glycans and could widely serve as a low-calorie sweetener. However, the most desirable steviol glycosides Reb D and Reb M, devoid of unpleasant aftertaste, are naturally produced only in trace amounts due to low levels of specific β (1-2) glucosylation in Stevia. Here, we report the biochemical and structural characterization of OsUGT91C1, a glycosyltransferase from Oryza sativa, which is efficient at catalyzing β (1-2) glucosylation. The enzyme's ability to bind steviol glycoside substrate in three modes underlies its flexibility to catalyze β (1-2) glucosylation in two distinct orientations as well as β (1-6) glucosylation. Guided by the structural insights, we engineer this enzyme to enhance the desirable β (1-2) glucosylation, eliminate β (1-6) glucosylation, and obtain a promising catalyst for the industrial production of naturally rare but palatable steviol glycosides.
PubMed: 34857750
DOI: 10.1038/s41467-021-27144-4
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.92 Å)
構造検証レポート
Validation report summary of 7erx
検証レポート(詳細版)ダウンロードをダウンロード

246905

件を2025-12-31に公開中

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