S-glycosyltransferase UGT74B1 can glycosylate both S- and O-acceptors: mechanistic insights through substrate specificity

Lafite, Pierre; Marroun, Sami; Coadou, Gaël; Montaut, Sabine; Marquès, Stéphanie; Schuler, Marie; Rollin, Patrick; Tatibouët, Arnaud; Daniellou, Richard; Oulyadi, Hassan

doi:10.1016/j.mcat.2019.110631

Cited by 9 publications

(15 citation statements)

References 45 publications

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“…S-Glycosylation is a form that is rarely reported compared to O-or N-glycosylation in plants, whether endogenous secondary metabolism or detoxification of exogenous compounds. 36 Grubb et al characterized N-hydroxythioamide Sbeta-glucosyltransferase (UGT74B1) and determined its role in the glucosinolate biosynthesis pathway. 10 UGT74B1 can specifically glucosylate the thiohydroxamic acid functional group.…”

Section: Discussionmentioning

confidence: 99%

“…Grubb et al characterized N -hydroxythioamide S -beta- glucosyltransferase (UGT74B1) and determined its role in the glucosinolate biosynthesis pathway . UGT74B1 can specifically glucosylate the thiohydroxamic acid functional group. , One of the key steps in this biosynthesis is the formation of S -glycosidic bonds derived from the conjugation of UDP-glucose and thiohydroxamic acid . The intermediate metabolite CT of FSF has the structure of dehydroxythiooxime, which may be the key to its ability to easily undergo S -glycosylation (Figure ).…”

Section: Discussionmentioning

confidence: 99%

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S-Glycosylation of Fluensulfone in Tomatoes: An Important Way of Fluensulfone Metabolism

Zhang

Cao

et al. 2021

J. Agric. Food Chem.

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Fluensulfone (FSF) becomes increasingly popular because of its nonfumigation application method. However, studies on the metabolic mechanism of FSF in plants are lacking. Here, tomato seedling was cultivated in hydroponic media to investigate the connection among FSF’s metabolism in tomato, the regulation of tomato endogenous glycosides, and the elimination of hydrogen peroxide in tomato cells. The accumulation of FSF was only detected in the lower stems of tomatoes; FSF was mainly metabolized into S-glycosylated conjugates in the roots, and the roots were the tissues with the highest metabolite content; and no FSF and metabolites were detected in the upper leaves. In response to FSF stress (2 mg/L for 7 d), the content of sugar and glycosides in the stems of tomato seedlings significantly increased. The amount of some compounds on the pathway related to glucose was affected by FSF. The three precursor compounds (homomethioine, isoleucine, and l-tyrosine) in the pathway of glucosinolate biosynthesis increased significantly under the stress of FSF, which indicates that FSF may compete with them for UGT74B1. Besides, FSF-induced flavonoid glycosides may play a role in the process of removing hydrogen peroxide. This research provides inspiration for the fate of many xenobiotics containing sulfonyl groups in plants.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

S-Glycosylation of Fluensulfone in Tomatoes: An Important Way of Fluensulfone Metabolism

Zhang

Cao

et al. 2021

J. Agric. Food Chem.

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“…These enzymes have traditionally sparked attention for being the biocatalysts responsible for synthesizing most of the natural glyconjugates. In the last decade, efforts have been made to increase their acceptor range, successfully reporting glycosyltransferases able to form O-, C-, S-, and/or N-glycosidic bonds 72 – 75 . However, the application of glycosyltransferases is still hampered by the high cost of the activated sugars required as glycosylation donors.…”

Section: Discussionmentioning

confidence: 99%

Thioglycoligase derived from fungal GH3 β-xylosidase is a multi-glycoligase with broad acceptor tolerance

et al. 2020

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The synthesis of customized glycoconjugates constitutes a major goal for biocatalysis. To this end, engineered glycosidases have received great attention and, among them, thioglycoligases have proved useful to connect carbohydrates to non-sugar acceptors. However, hitherto the scope of these biocatalysts was considered limited to strong nucleophilic acceptors. Based on the particularities of the GH3 glycosidase family active site, we hypothesized that converting a suitable member into a thioglycoligase could boost the acceptor range. Herein we show the engineering of an acidophilic fungal β-xylosidase into a thioglycoligase with broad acceptor promiscuity. The mutant enzyme displays the ability to form O-, N-, S- and Se- glycosides together with sugar esters and phosphoesters with conversion yields from moderate to high. Analyses also indicate that the pKa of the target compound was the main factor to determine its suitability as glycosylation acceptor. These results expand on the glycoconjugate portfolio attainable through biocatalysis.

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“…S ‐glycosyltransferases are involved in the biosynthesis of biologically active natural products, such as the glycopeptides sublancin [21–23] and thurandacin [24, 25] and the plant glucosinolates [26, 27] . Furthermore, it has been demonstrated that the enzyme engineering of O ‐ and N ‐glycosyltransferases to generate S ‐glycosidic linkages [28–30] .…”

Section: Methodsmentioning

confidence: 99%

Structure‐Function Analysis of the S‐Glycosylation Reaction in the Biosynthesis of Lincosamide Antibiotics

et al. 2023

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The S‐glycosyltransferase LmbT, involved in the biosynthesis of lincomycin A, is the only known enzyme that catalyzes the enzymatic incorporation of rare amino acid L‐ergothioneine (EGT) into secondary metabolites. Here, we show the structure and function analyses of LmbT. Our in vitro analysis of LmbT revealed that the enzyme shows promiscuous substrate specificity toward nitrogenous base moieties in the generation of unnatural nucleotide diphosphate (NDP)‐D‐α‐D‐lincosamides. Furthermore, the X‐ray crystal structures of LmbT in its apo form and in complex with substrates indicated that the large conformational changes of the active site occur upon binding of the substrates, and that EGT is strictly recognized by salt‐bridge and cation‐π interactions with Arg260 and Trp101, respectively. The structure of LmbT in complex with its substrates, the docking model with the EGT‐S‐conjugated lincosamide, and the structure‐based site‐directed mutagenesis analysis revealed the structural details of the LmbT‐catalyzed SN2‐like S‐glycosylation reaction with EGT.

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S-glycosyltransferase UGT74B1 can glycosylate both S- and O-acceptors: mechanistic insights through substrate specificity

Cited by 9 publications

References 45 publications

S-Glycosylation of Fluensulfone in Tomatoes: An Important Way of Fluensulfone Metabolism

S-Glycosylation of Fluensulfone in Tomatoes: An Important Way of Fluensulfone Metabolism

Thioglycoligase derived from fungal GH3 β-xylosidase is a multi-glycoligase with broad acceptor tolerance

Structure‐Function Analysis of the S‐Glycosylation Reaction in the Biosynthesis of Lincosamide Antibiotics

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